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lipolytica","tax_id":4952},{"name":"Neurospora crassa","tax_id":5141},{"name":"Aspergillus nidulans","tax_id":162425},{"name":"Saccharomyces cerevisiae","tax_id":4932},{"name":"Diospyros kaki","tax_id":35925},{"name":"Ostreococcus 'lucimarinus'","tax_id":242159},{"name":"Fusarium graminearum","tax_id":5518}],"document_location":["BDRAW","DDESC"],"count":219,"data_source":["USPTO_FULLTEXT_RB","EMBLPAT_EBI","DDBJPAT","GBPAT_NCBI"]},"has_sequence":true,"legal_status":{"ipr_type":"patent for invention","granted":true,"earliest_filing_date":"2007-09-28","grant_date":"2014-04-08","anticipated_term_date":"2030-04-08","has_disclaimer":false,"patent_status":"ACTIVE","publication_count":2,"has_spc":false,"has_grant_event":true,"has_entry_into_national_phase":false},"abstract":{"en":[{"text":"The present invention provides systems for producing engineered oleaginous yeast or fungi that express carotenoids.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"abstract_lang":["en"],"has_abstract":true,"claim":{"en":[{"text":"1. An engineered Y. lipolytica strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one retinologenic modification selected from the group consisting of increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide, increased expression or activity of a retinol dehydrogenase polypeptide, and combinations thereof; wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"2. The engineered Y. lipolytica strain of claim 1 , wherein the strain does not naturally produce the at least one retinolic compound.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"3. The engineered Y. lipolytica strain of claim 1 , further comprising at least one oleaginic modification.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"4. The engineered Y. lipolytica strain of claim 3 , wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide, selected from the group consisting of acetyl-CoA carboxylase polypeptide, pyruvate decarboxylase polypeptide, isocitrate dehydrogenase polypeptide, ATP-citrate lyase polypeptide, malic enzyme polypeptide, AMP deaminase polypeptide, malate dehydrogenase polypeptide, glucose-6-phosphate dehydrogenase polypeptide, 6-phosphogluconate dehydrogenase polypeptide, fructose 1,6 bisphosphatase polypeptide, NADH kinase polypeptide, transhydrogenase polypeptide, acyl-CoA:diacylglycerol acyltransferase polypeptide, phospholipid:diacylglycerol acyltransferase polypeptide, acyl-CoA:cholesterol acyltransferase polypeptide, triglyceride lipase polypeptide, acyl-coenzyme A oxidase polypeptide and combinations thereof.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"5. The engineered Y. lipolytica strain of claim 3 , wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide selected from the group consisting of a polypeptide in any one of Tables 1 through 6 or 31-47.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"6. The engineered Y. lipolytica strain of claim 1 , wherein the at least one retinologenic modification confers to the engineered strain the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"7. The engineered Y. lipolytica strain of claim 1 , wherein the at least one retinologenic modification confers to the engineered strain the ability to produce at least one retinolic compound which a non-engineered strain does not naturally produce.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"8. The engineered Y. lipolytica strain of claim 1 , wherein the at least one retinologenic modification increases expression or activity of beta-carotene 15,15′-monoxygenase or beta carotene retinol dehydrogenase.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"9. The engineered Y. lipolytica strain of claim 1 , wherein the beta-carotene 15,15′-monooxygenase polypeptide is selected from the group consisting of a polypeptide in Table 67.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"10. The engineered Y. lipolytica strain of claim 1 , wherein the at least one retinologenic modification further comprises decreasing the expression or activity of one or more components of the SAGA histone acetyltransferase complex.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"11. The engineered Y. lipolytica strain of claim 10 , wherein the at least one retinologenic modification comprises disruption of the endogenous SPT8 gene.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"12. The engineered Y. lipolytica strain of claim 10 wherein the one or more components of the SAGA histone acetyltransferase complex are selected from the polypeptides listed in Table 69.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"13. The engineered Y. lipolytica strain of claim 1 , wherein the retinologenic modification further comprises altering the expression or activity of one or more carotenoid biosynthesis polypeptides.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"14. The engineered Y. lipolytica strain of claim 13 , wherein the one or more carotenoid biosynthesis polypeptides are selected from the group consisting of phytoene synthase, phytoene dehydrogenase, lycopene cyclase, carotene ketolase, carotene hydroxylase, astaxanthin synthase, carotenoid epsilon hydroxylase, lycopene cyclase, carotenoid glucosyltransferase, acyl CoA:diacyglycerol acyltransferase, geranylgeranylpyrophosphate synthase, and truncated HMG-CoA reductase.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"15. The engineered Y. lipolytica strain of claim 13 , wherein the one or more carotenoid biosynthesis polypeptides are selected from the sequences provided in Tables 17a-25.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"16. A method of producing a retinolic compound, the method comprising steps of: a. cultivating the fungus of claim 1 under conditions that allow production of the retinolic compound; b. and isolating the produced retinolic compound.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"17. The engineered Y. lipolytica strain of claim 1 , wherein the at least one retinologenic modification comprises introduction of a gene encoding a heterologous beta-carotene 15,15′-monooxygenase polypeptide, a heterologous retinol dehydrogenase polypeptide, or combinations thereof.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"18. The engineered Y. lipolytica strain of claim 1 , wherein the retinol dehydrogenase polypeptide is selected from the group consisting of a polypeptide in Table 68.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"19. An engineered Y. lipolytica strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one genetic modification selected from the group consisting of: increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide; increased expression or activity of a retinol dehydrogenase polypeptide; increased expression or activity of phytoene synthase; increased expression or activity of lycopene cyclase; increased expression or activity of phytoene dehydrogenease; increased expression or activity of geranylgeranylpyrophosphate synthase; increased expression or activity of truncated HMG-CoA reductase; and combinations thereof; wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"},{"text":"20. The engineered Y. lipolytica strain of claim 19 , wherein the genetic modification comprises introduction of one or more heterologous genes encoding metabolic enzymes selected from the group consisting of: beta-carotene 15,15′-monooxygenase, phytoene synthase, lycopene cyclase, phytoene dehydrogenease, geranylgeranylpyrophosphate synthase, truncated HMG-CoA reductase, and combinations thereof.","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}]},"claim_lang":["en"],"has_claim":true,"description":{"en":{"text":"CROSS REFERENCE TO RELATED APPLICATIONS This application is a national phase application under 35 U.S.C. §371 of PCT International Application No. PCT/US2007/021092, filed Sep. 28, 2007, which is copending with, shares at least one common inventor with, and claims priority to U.S. provisional patent application No. 60/848,062, filed Sep. 28, 2006. This application is also copending with, shares at least one common inventor with, and claims priority to U.S. provisional patent application No. 60/902,145, filed Feb. 16, 2007. The entire contents of each of these applications are hereby incorporated by reference. SEQUENCE LISTING In accordance with 37 CFR 1.52(e)(5), a Sequence Listing in the form of a text file (entitled “2005862-0053_SL.txt,” created on Feb. 11, 2013, and 329,074 bytes in size) is incorporated herein by reference in its entirety. BACKGROUND OF THE INVENTION Carotenoids are organic pigments ranging in color from yellow to red that are naturally produced by certain organisms, including photosynthetic organisms (e.g., plants, algae, cyanobacteria), and some fungi. Carotenoids are responsible for the orange color of carrots, as well as the pink in flamingos and salmon, and the red in lobsters and shrimp. Animals, however, cannot produce carotenoids and must receive them through their diet. Carotenoid pigments (e.g., β-carotene and astaxanthin) are used industrially as ingredients for food and feed stocks, both serving a nutritional function and enhancing consumer acceptability. For example, astaxanthin is widely used in salmon aquaculture to provide the orange coloration characteristic of their wild counterparts. Some carotenoids are also precursors of vitamin A. Also, carotenoids have antioxidant properties, and may have various health benefits (see, for example, Jyonouchi et al., Nutr. Cancer 16:93, 1991; Giovannucci et al., J. Natl. Cancer Inst. 87:1767, 1995; Miki, Pure Appl. Chem 63:141, 1991; Chew et al., Anticancer Res. 19:1849, 1999; Wang et al., Antimicrob. Agents Chemother. 44:2452, 2000). Some carotenoids such as β-carotene, lycopene, and lutein are currently sold as nutritional supplements. In general, the biological systems that produce carotenoids are industrially intractable and/or produce the compounds at such low levels that commercial scale isolation is not practicable. Thus, most carotenoids used in industry are produced by chemical synthesis. There is a need for improved biological systems that produce carotenoids. Some efforts have previously been made to genetically engineer certain bacteria or fungi to produce higher levels of carotenoids (see, for example, Misawa et al., J. Biotechnol. 59:169, 1998; Visser et al., FEMS Yeast Research 4:221, 2003). However, improved systems, allowing higher levels of production and greater ease of isolation, are needed. SUMMARY OF THE INVENTION The present invention provides improved systems for the biological production of carotenoids and/or retinolic compounds. In one aspect, the invention encompasses the discovery that it is desirable to produce carotenoids and/or retinolic compounds in oleaginous organisms. Without wishing to be bound by any particular theory, the present inventors propose that biological systems may be able to accumulate higher levels of carotenoids and/or retinolic compounds if the compounds are sequestered in lipid bodies. Regardless of whether absolute levels are higher, however, carotenoids and/or retinolic compounds that are accumulated within lipid bodies in oleaginous organisms are readily isolatable through isolation of the lipid bodies. The present invention therefore provides oleaginous fungi (including, for example, yeast) that produce one or more carotenoids and/or retinolic compounds. The present invention also provides methods of constructing such yeast and fungi, methods of using such yeast and fungi to produce carotenoids and/or retinolic compounds, and methods of preparing carotenoid-containing compositions and/or retinolic compound-containing compositions, such as food or feed additives, or nutritional supplements, using carotenoids and/or retinolic compounds produced in such oleaginous yeast or fungi. In particular, the present invention provides systems and methods for generating yeast and fungi containing one or more oleaginic and/or carotenogenic and/or retinologenic modifications that increase the oleaginicity and/or alter their carotenoid-producing and/or retinolic compound-producing capabilities as compared with otherwise identical organisms that lack the modification(s). The present invention further encompasses the general recognition that lipid-accumulating systems are useful for the production and/or isolation of lipophilic agents (such as, but not limited to isoprenoids, or isoprenoid-derived compounds such as retinolic compounds, carotenoids, ubiquinones, lanosterol, zymosterol, ergosterol, vitamins (e.g., vitamins A, E, D, K, specifically 7-dehydrocholesterol (provitamin D3), sterols (e.g., squalene), etc.). According to the present invention, it is desirable to engineer organisms to produce such lipophilic agents and/or to accumulate lipid. Indeed, one aspect of the present invention is the recognition that host cells can be engineered to accumulate in lipid bodies any of a variety of hydrophilic and/or fat soluble compounds (e.g., retinolic compounds, carotenoids, ubiquinones, vitamins, squalene, etc.) having negligible solubility in water (whether hot or cold) and an appropriate solubility in oil. In some embodiments of the invention, modified host cells are engineered to produce one or more lipophilic agents characterized by negligible solubility in water and detectable solubility in one or more oils. In some embodiments, such lipophilic agents (including, but not limited to carotenoids and/or retinolic compounds) have a solubility in oil below about 0.2%. In some embodiments, such lipophilic agents have a solubility in oil within the range of about <0.001%-0.2%. The present invention therefore provides engineered host cells (and methods of making and using them) that contain lipid bodies and that further contain one or more compounds accumulated in the lipid bodies, where the compounds are characterized by a negligible solubility in water and a solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%. For example, in some embodiments, such lipophilic agents have a solubility in oil below about 0.15%, 0.14%, 0.13%, 0.12%, 0.11%, 0.10%, 0.09, 0.08%, 0.07%, 0.06%, 0.05%, 0.04%, 0.03%, 0.02%, 0.01%, 0.05%, or less. In some embodiments, the lipophilic agents show such solubility in an oil selected from the group consisting of sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof. In some embodiments, the present invention provides a recombinant fungus. In certain embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid and/or retinolic compound, and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, which parental fungus both is not oleaginous and does not accumulate the carotenoid and/or retinolic compound to at least about 1% of its dry cell weight, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not produce. In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid selected from the group consisting of antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, a C30 carotenoid, and combinations thereof, and can accumulate the produced carotenoid to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid which the parental fungus does not naturally produce. In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, and combinations thereof, and can accumulate the produced retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one retinolic compound which the parental fungus does not naturally produce. In some embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid and/or retinolic compound, and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium ( Gibberella ), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia ( Hansenula ), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces ( Phaffia ), and Yarrowia ; or is a species selected from the group consisting of: Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi ( Gibberella zeae ), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), and Yarrowia lipolytica , wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not naturally produce. In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one carotenoid selected from the group consisting of antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, a C30 carotenoid, and combinations thereof, and can accumulate the produced carotenoid to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium ( Gibberella ), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia ( Hansenula ), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces ( Phaffia ), and Yarrowia , or is of a species selected from the group consisting of Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi ( Gibberella zeae ), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), and Yarrowia lipolytica , wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid which the parental fungus does not naturally produce. In other embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, and combinations thereof, and can accumulate the produced retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium ( Gibberella ), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia ( Hansenula ), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces ( Phaffia ), and Yarrowia , or is of a species selected from the group consisting of Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi ( Gibberella zeae ), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), and Yarrowia lipolytica , wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one retinolic compound which the parental fungus does not naturally produce. In certain embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent selected from the group consisting of retinolic compounds, carotenoids, ubiquinone, vitamin K, vitamin E, squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), and combinations thereof and can accumulate the produced carotenoid and/or retinolic compound to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one carotenoid and/or retinolic compound to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one carotenoid and/or retinolic compound which the parental fungus does not naturally produce. In some embodiments, the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent characterized by a negligible solubility in water and solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%, and combinations thereof and can accumulate the produced small molecule lipophilic agent to at least about 1% of its dry cell weight; wherein the recombinant fungus comprises at least one modification as compared with a parental fungus, the at least one modification being selected from the group consisting of retinologenic modifications, carotenogenic modifications, oleaginic modifications, and combinations thereof, and wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one small molecule lipophilic agent to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one small molecule lipophilic agent which the parental fungus does not naturally produce. In other embodiments the recombinant fungus is oleaginous in that it can accumulate lipid to at least about 20% of its dry cell weight; and the recombinant fungus produces at least one small molecule lipophilic agent selected from the group consisting of retinolic compounds, carotenoids, ubiquinone, vitamin K, vitamin E, squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), and can accumulate the produced small molecule lipophilic agent to at least about 1% of its dry cell weight; wherein the recombinant fungus is a member of a genus selected from the group consisting of Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium ( Gibberella ), Kluyveromyces, Neurospora, Penicillium, Pichia ( Hansenula ), Puccinia, Saccharomyces, Schizosaccharomyces, Sclerotium, Trichoderms, Ustilago , and Xanthophyllomyces ( Phaffia ) and comprises at least one genetic modification as compared with a parental fungus, wherein the at least one modification alters oleaginicity of the recombinant fungus, confers to the recombinant fungus oleaginy, confers to the recombinant fungus the ability to produce the at least one small molecule lipophilic agent to a level at least about 1% of its dry cell weight, or confers to the recombinant fungus the ability to produce at least one small molecule lipophilic agent which the parental fungus does not naturally produce. In some embodiments, the present invention provides a strain of Yarrowia lipolytica comprising one or more modifications selected from the group consisting of an oleaginic modification, a carotenogenic modification, and combinations thereof, such that the strain accumulates from 1% to 15% of its dry cell weight as at least one carotenoid. In some embodiments, the present invention provides a strain of Yarrowia lipolytica comprising one or more modifications selected from the group consisting of an oleaginic modification, a retinologenic modification, and combinations thereof, such that the strain accumulates from 1% to 15% of its dry cell weight as at least one retinolic compound. In some embodiments, the present invention provides an engineered Y. lipolytica strain that produces β-carotene, the strain containing one or more carotenogenic modifications selected from the group consisting of: increased expression or activity of a Y. lipolytica GGPP synthase polypeptide; expression or activity of a truncated HMG CoA reductase polypeptide; expression or activity of a phytoene dehydrogenase polypeptide; expression or activity of a phytoene synthase/lycopene cyclase polypeptide; increased expression or activity of an FPP synthase polypeptide; increased expression or activity of an IPP isomerase polypeptide; increased expression or activity of an HMG synthase polypeptide; increased expression or activity of a mevalonate kinase polypeptide; increased expression or activity of a phosphomevalonate kinase polypeptide; increased expression or activity of a mevalonate pyrophosphate decarboxylate polypeptide; increased expression or activity of a malic enzyme polypeptide; increased expression or activity of a malate dehydrogenase polypeptide; increased expression or activity of an AMP deaminase polypeptide; increased expression or activity of a glucose 6 phosphate dehydrogenase polypeptide; increased expression or activity of a malate dehydrogenase homolog2 polypeptide; increased expression or activity of a GND1-6-phosphogluconate dehydrogenase polypeptide; increased expression or activity of a isocitrate dehydrogenase polypeptide; increased expression or activity of a IDH2-isocitrate dehydrogenase polypeptide; increased expression or activity of a fructose 1,6 bisphosphatase polypeptide; increased expression or activity of a Erg10-acetoacetyl CoA thiolase polypeptide; increased expression or activity of a ATP citrate lyase subunit 2 polypeptide; increased expression or activity of a ATP citrate lyase subunit 1 polypeptide; decreased expression or activity of a squalene synthase polypeptide; decreased expression or activity of a prenyldiphosphate synthase polypeptide; or decreased expression or activity of a PHB polyprenyltransferase polypeptide; and combinations thereof. In some embodiments, the present invention provides an engineered Y. lipolytica strain that produces Vitamin A, the strain containing one or more retinologenic modifications selected from the group consisting of: increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide; increased expression or activity of a retinol dehydrogenase polypeptide; and combinations thereof. In some embodiments, the present invention provides an engineered Y. lipolytica strain containing a truncated HMG CoA reductase polypeptide. In some embodiments, the present invention provides an engineered Y. lipolytica strain having increased expression or activity of a GGPP synthase gene. In some embodiments, the present invention provides an engineered Y. lipolytica strain having decreased expression or activity of a squalene synthase polypeptide. In some embodiments, the present invention provides an engineered Y. lipolytica strain containing a heterologous phytoene dehydrogenase (carB) polypeptide and a heterologous phytoene synthase/lycopene cyclase (carRP) polypeptide. In some embodiments, the present invention provides a genetically modified Y. lipolytica strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof. In certain embodiments, the present invention provides a genetically modified Candida utilis strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof. In other embodiments, the present invention provides a genetically modified Saccharomyces cerevisiae strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof. In some embodiments, the present invention provides a genetically modified Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ) strain comprising an altered activity or expression of one or more enzymes when compared to an unmodified strain, wherein the altered activity or expression of one or more enzymes is selected from the group consisting of: increased activity or expression of a beta-carotene 15,15′-monooxygenase polypeptide; increased activity or expression of a retinol dehydrogenase polypeptide; increased activity or expression of acetyl-CoA thiolase, increased activity or expression of HMG-CoA synthase, increased activity or expression of HMG-CoA reductase, increased activity or expression of mevalonate kinase, increased activity or expression of phosphomevalonate kinase, increased activity or expression of mevalonate PP decarboxylase, decreased activity or expression of acetyl-CoA carboxylase, increased activity or expression of IPP isomerase, increased activity or expression of GPP synthase, increased activity or expression of FPP synthase, increased activity or expression of squalene synthase, decreased activity or expression of squalene synthase, increased activity or expression of GGPP synthase, decreased activity or expression of GGPP synthase, increased activity or expression of glucose-6-phosphate dehydrogenase, increased activity or expression of 6-phosphogluconate dehydrogenase, increased activity or expression of fructose 1,6 bisphosphatase, increased activity or expression of NADH kinase, increased activity or expression of transhydrogenase, and combinations thereof. In other embodiments, the present invention provides a method of producing a carotenoid, the method comprising steps of cultivating a fungus under conditions that allow production of the carotenoid; and isolating the produced carotenoid. In other embodiments, the present invention provides a method of producing a retinolic compound, the method comprising steps of cultivating a fungus under conditions that allow production of the retinolic compound; and isolating the produced retinolic compound. In certain embodiments, the present invention provides an isolated carotenoid composition, prepared by a method comprising steps of cultivating the fungus under conditions that allow production of a carotenoid; and isolating the produced carotenoid. In certain embodiments, the present invention provides an isolated retinolic compound composition, prepared by a method comprising steps of cultivating the fungus under conditions that allow production of a retinolic compound; and isolating the produced retinolic compound. In other embodiments, the present invention provides a composition comprising lipid bodies; at least one carotenoid compound; and intact fungal cells. In other embodiments, the present invention provides a composition comprising lipid bodies; at least one retinolic compound; and intact fungal cells. In some embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one carotenoid compound; intact fungal cells; and a binder or filler. In some embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one retinolic compound; intact fungal cells; and a binder or filler. In certain embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one carotenoid compound; intact fungal cells; and one or more other agents selected from the group consisting of chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, and combinations thereof. In certain embodiments, the present invention provides a composition comprising: an oil suspension comprising: lipid bodies; at least one retinolic compound; intact fungal cells; and one or more other agents selected from the group consisting of chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, and combinations thereof. In some embodiments, the present invention provides a feedstuff comprising a carotenoid in lipid bodies. In other embodiments, the present invention provides a feedstuff comprising a carotenoid in lipid bodies; wherein the carotenoid is selected from the group consisting of astaxanthin, β-carotene, canthaxanthin, zeaxanthin, lutein, lycopene, echinenone, β-cryptoxanthin and combinations thereof. In some embodiments, the present invention provides a feedstuff comprising a retinolic compound in lipid bodies. In other embodiments, the present invention provides a feedstuff comprising a retinolic compound in lipid bodies; wherein the retinolic compound is selected from the group consisting of retinol, retainal, retinoic acid, and combinations thereof. In certain embodiments, the present invention provides a carotenoid composition comprising a Y. lipolytica cell containing at least 1% carotenoids by weight. In other embodiments, the present invention provides a carotenoid composition comprising Y. lipolytica lipid bodies; and at least one carotenoid compound, wherein the at least one carotenoid compound is present at a level that is at least 1% by weight of the lipid bodies. In certain embodiments, the present invention provides a retinolic compound composition comprising a Y. lipolytica cell containing at least 1% retinolic compounds by weight. In other embodiments, the present invention provides a retinolic compound composition comprising Y. lipolytica lipid bodies; and at least one retinolic compound, wherein the at least one retinolic compound is present at a level that is at least 1% by weight of the lipid bodies. Additional aspects of the present invention will be apparent to those of ordinary skill in the art from the present description, including the appended claims. BRIEF DESCRIPTION OF THE DRAWING FIG. 1A-1D depicts certain common carotenoids. FIG. 2 depicts how sufficient levels of acetyl-CoA and NADPH may be accumulated in the cytosol of oleaginous organisms to allow for production of significant levels of cytosolic lipids. Enzymes: 1, pyruvate decarboxylase; 2, malate dehydrogenase; 3, malic enzyme; 4, pyruvate dehydrogenase; 5, citrate synthase; 6, ATP-citrate lyase; 7, citrate/malate translocase. FIGS. 3A and 3B depict the mevalonate isoprenoid biosynthesis pathway, which typically operates in eukaryotes, including fungi. FIG. 4 depicts the mevalonate-independent isoprenoid biosynthesis pathway, also known as the DXP pathway, which typically operates in bacteria and in the plastids of plants. FIG. 5 depicts intermediates in the isoprenoid biosynthesis pathway and how they feed into biosynthetic pathways of other biomolecules, including carotenoids as well as non-carotenoid compounds such as sterols, steroids, and vitamins, such as vitamin E or vitamin K. FIGS. 6A-6D illustrate various carotenoid biosynthetic pathways. FIG. 6A highlights branches leading to various cyclic and acyclic xanthophylls; FIG. 6B shows certain X. dendrorhous pathways that generate dicyclic and monocyclic carotenoids, including astaxanthin; FIG. 6C shows interconnecting pathways for converting β-carotene into any of a variety of other carotenoids, including astaxanthin; FIG. 6D depicts possible routes of synthesis of cyclic carotenoids and common plant and algal xanthophylls from neurosporene. FIG. 7 and subparts FIGS. 7A-7I show an alignment of certain representative fungal HMG-CoA reductase polypeptides (SEQ ID NOs 176-182, respectively, in order of appearance). As can be seen, these polypeptides show very high identity across the catalytic region, and also have complex membrane spanning domains. In some embodiments of the invention, these membrane-spanning domains are disrupted or are removed, so that, for example, a hyperactive version of the polypeptide may be produced. FIGS. 8A-8P depict schematic representations of plasmids generated and described in detail in the exemplification. FIGS. 9A-E show production characteristics of certain engineered cells according to the present invention. Specifically, Panel A shows β-Carotene and phytoene production by Strain MF760 when grown in glycerol, glucose or olive oil; Panel B shows dry cell weight accumulation of strain MF760 when grown in glycerol, glucose or olive oil; Panel C shows β-Carotene and dry cell weight analysis of strain MF760 when grown in the presence of a combination of olive oil and glucose; Panel D shows canthaxanthin, echinenone and β-carotene production of strain MF840; and Panel E shows canthaxanthin and echinenone production of strain MF838 in a 2 phase feeding protocol. FIG. 10 is a Table listing certain Y. lipolytica genes representing various polypeptides (e.g., oleaginic and isoprenoid biosynthesis peptides) useful in engineering cells in accordance with the present invention. Figure discloses SEQ ID NOs 183-218, respectively, in order of appearance. FIG. 11 depicts the all-trans-retinol (Vitamin A) biosynthesis pathway, starting with beta-carotene as a substrate. FIG. 12 depicts various characteristics of strain ML1011 (MF740 transformed with multiple integrated copies of the X. autotrophicus crtZ gene) grown under different pH conditions. FIG. 12 a depicts accumulation of total carotenoid (absorbance units per unit dry cell weight) over the course of the fermentation. FIG. 12 b depicts accumulation of zeaxanthin (absorbance units per dry cell weight; AU) over the course of the fermentation. FIG. 12 c depicts the fraction of carotenoid as zeaxanthin (AU zeaxanthin/AU total carotenoid) over the course of the fermentation. FIG. 12 d depicts carbon dioxide evolution over the course of the fermentation. FIG. 12 e depicts biomass accumulation over the course of the fermentation. DEFINITIONS Aromatic amino acid biosynthesis polypeptide: The term “aromatic amino acid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of aromatic amino acids in yeast and/or bacteria through chorismate and the shikimate pathway. For example, as discussed herein, anthranilate synthase, enzymes of the shikimate pathway, chorismate mutase, chorismate synthase, DAHP synthase, and transketolase are all aromatic amino acid biosynthesis polypeptides. Each of these polypeptides is also a ubiquinone biosynthesis polypeptide or a ubiquinone biosynthesis competitor for purposes of the present invention, as production of chorismate is a precursor in the synthesis of para-hydroxybenzoate for the biosynthesis of ubiquinone. Biosynthesis polypeptide: The term “biosynthesis polypeptide” as used herein (typically in reference to a particular compound or class of compounds), refers to polypeptides involved in the production of the compound or class of compounds. In some embodiments of the invention, biosynthesis polypeptides are synthetic enzymes that catalyze particular steps in a synthesis pathway that ultimately produces a relevant compound. In some embodiments, the term “biosynthesis polypeptide” may also encompass polypeptides that do not themselves catalyze synthetic reactions, but that regulate expression and/or activity of other polypeptides that do so. Biosynthesis polypeptides include, for example, aromatic amino acid biosynthesis polypeptides, C 5-9 quinone biosynthesis polypeptides, carotenoid biosynthesis polypeptides, retinolic compound biosynthesis polypeptides, FPP biosynthesis polypeptides, isoprenoid biosynthesis polypeptides, PHB biosynthesis polypeptides, quinone biosynthesis polypeptides, sterol biosynthesis polypeptides, ubiquinone biosynthesis polypeptides, Vitamin D biosynthesis polypeptides, Vitamin E biosynthesis polypeptides, and Vitamin K biosynthesis polypeptides. C 5-9 quinone biosynthesis polypeptide: The term “C 5-9 quinone biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of a C 5-9 quinone, for example a polyprenyldiphosphate synthase polypeptide. To mention but a few, these include, for example, pentaprenyl, hexaprenyl, heptaprenyl, octaprenyl, and/or solanesyl (nonaprenyl) diphosphate synthase polypeptides (i.e., polypeptides that perform the chemical reactions performed by the pentaprenyl, hexaprenyl, heptaprenyl, octaprenyl, and solanesyl (nonaprenyl) polypeptides, respectively (see also Okada et al., Biochim. Biophys. Acta 1302:217, 1996; Okada et al., J. Bacteriol. 179:5992, 1997). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, C 5-9 quinone biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other C 5-9 quinone biosynthesis polypeptides. Carotenogenic modification: The term “carotenogenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more carotenoids, as described herein. For example, a carotenogenic modification may increase the production level of one or more carotenoids, and/or may alter relative production levels of different carotenoids. In principle, an inventive carotenogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more carotenoids in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the carotenogenic modification will comprise a genetic modification, typically resulting in increased production of one or more selected carotenoids. In some embodiments, the carotenogenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the carotenogenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical, and/or physiological modification(s)). In some embodiments, the selected carotenoid is one or more of astaxanthin, β-carotene, canthaxanthin, lutein, lycopene, phytoene, zeaxanthin, and/or modifications of zeaxanthin or astaxanthin (e.g., glucoside, esterified zeaxanthin or astaxanthin). In some embodiments, the selected carotenoid is one or more xanthophylls, and/or a modification thereof (e.g., glucoside, esterified xanthophylls). In certain embodiments, the selected xanthophyl is selected from the group consisting of astaxanthin, lutein, zeaxanthin, lycopene, and modifications thereof. In some embodiments, the selected carotenoid is one or more of astaxanthin, β-carotene, canthaxanthin, lutein, lycopene, and zeaxanthin and/or modifications of zeaxanthin or astaxanthin. In some embodiments, the carotenoid is β-carotene. In some embodiments, the selected carotenoid is astaxanthin. In some embodiments, the selected carotenoid is other than β-carotene. Carotenogenic polypeptide: The term “carotenogenic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of producing carotenoids in a cell, and may include polypeptides that are involved in processes other than carotenoid production but whose activities affect the extent or level of production of one or more carotenoids, for example by scavenging a substrate or reactant utilized by a carotenoid polypeptide that is directly involved in carotenoid production. Carotenogenic polypeptides include isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, and isoprenoid biosynthesis competitor polypeptides, as those terms are defined herein. The term also encompasses polypeptides that may affect the extent to which carotenoids are accumulated in lipid bodies. Carotenoid: The term “carotenoid” is understood in the art to refer to a structurally diverse class of pigments derived from isoprenoid pathway intermediates. The commitment step in carotenoid biosynthesis is the formation of phytoene from geranylgeranyl pyrophosphate. Carotenoids can be acyclic or cyclic, and may or may not contain oxygen, so that the term carotenoids include both carotenes and xanthophylls. In general, carotenoids are hydrocarbon compounds having a conjugated polyene carbon skeleton formally derived from the five-carbon compound IPP, including triterpenes (C 30 diapocarotenoids) and tetraterpenes (C 40 carotenoids) as well as their oxygenated derivatives and other compounds that are, for example, C 35 , C 50 , C 60 , C 70 , C 80 in length or other lengths. Many carotenoids have strong light absorbing properties and may range in length in excess of C 200 . C 30 diapocarotenoids typically consist of six isoprenoid units joined in such a manner that the arrangement of isoprenoid units is reversed at the center of the molecule so that the two central methyl groups are in a 1,6-positional relationship and the remaining non-terminal methyl groups are in a 1,5-positional relationship. Such C 30 carotenoids may be formally derived from the acyclic C 30 H 42 structure, having a long central chain of conjugated double bonds, by: (i) hydrogenation (ii) dehydrogenation, (iii) cyclization, (iv) oxidation, (v) esterification/glycosylation, or any combination of these processes. C 40 carotenoids typically consist of eight isoprenoid units joined in such a manner that the arrangement of isoprenoid units is reversed at the center of the molecule so that the two central methyl groups are in a 1,6-positional relationship and the remaining non-terminal methyl groups are in a 1,5-positional relationship. Such C 40 carotenoids may be formally derived from the acyclic C 40 H 56 structure, having a long central chain of conjugated double bonds, by (i) hydrogenation, (ii) dehydrogenation, (iii) cyclization, (iv) oxidation, (v) esterification/glycosylation, or any combination of these processes. The class of C 40 carotenoids also includes certain compounds that arise from rearrangements of the carbon skeleton, or by the (formal) removal of part of this structure. More than 600 different carotenoids have been identified in nature; certain common carotenoids are depicted in FIG. 1 . Carotenoids include but are not limited to: antheraxanthin, adonirubin, adonixanthin, astaxanthin, canthaxanthin, capsorubrin, β-cryptoxanthin, α-carotene, β-carotene, β,ψ-carotene, δ-carotene, ε-carotene, echinenone, 3-hydroxyechinenone, 3′-hydroxyechinenone, γ-carotene, ψ-carotene, 4-keto-γ-carotene, ζ-carotene, α-cryptoxanthin, deoxyflexixanthin, diatoxanthin, 7,8-didehydroastaxanthin, didehydrolycopene, fucoxanthin, fucoxanthinol, isorenieratene, β-isorenieratene, lactucaxanthin, lutein, lycopene, myxobactone, neoxanthin, neurosporene, hydroxyneurosporene, peridinin, phytoene, rhodopin, rhodopin glucoside, 4-keto-rubixanthin, siphonaxanthin, spheroidene, spheroidenone, spirilloxanthin, torulene, 4-keto-torulene, 3-hydroxy-4-keto-torulene, uriolide, uriolide acetate, violaxanthin, zeaxanthin-β-diglucoside, zeaxanthin, and C30 carotenoids. Additionally, carotenoid compounds include derivatives of these molecules, which may include hydroxy-, methoxy-, oxo-, epoxy-, carboxy-, or aldehydic functional groups. Further, included carotenoid compounds include ester (e.g., glycoside ester, fatty acid ester) and sulfate derivatives (e.g., esterified xanthophylls). Carotenoid biosynthesis polypeptide: The term “carotenoid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more carotenoids. To mention but a few, these carotenoid biosynthesis polypeptides include, for example, polypeptides of phytoene synthase, phytoene dehydrogenase (or desaturase), lycopene cyclase, carotenoid ketolase, carotenoid hydroxylase, astaxanthin synthase, carotenoid epsilon hydroxylase, lycopene cyclase (beta and epsilon subunits), carotenoid glucosyltransferase, and acyl CoA:diacyglycerol acyltransferase. In some instances, a single gene may encode a protein with multiple carotenoid biosynthesis polypeptide activities. Representative examples of carotenoid biosynthesis polypeptide sequences are presented in Tables 17a-25. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, carotenoid biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other carotenoid biosynthesis polypeptides. FPP biosynthesis polypeptides: The term “FPP biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of farnesyl pyrophosphate. As discussed herein, farnesyl pyrophosphate represents the branchpoint between the sterol biosynthesis pathway and the carotenoid and other biosynthesis pathways. One specific example of an FPP biosynthesis polypeptide is FPP synthase. Representative examples of FPP synthase polypeptide sequences are presented in Table 14. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, FPP biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other FPP biosynthesis polypeptides. Gene: The term “gene”, as used herein, generally refers to a nucleic acid encoding a polypeptide, optionally including certain regulatory elements that may affect expression of one or more gene products (i.e., RNA or protein). Heterologous: The term “heterologous”, as used herein to refer to genes or polypeptides, refers to a gene or polypeptide that does not naturally occur in the organism in which it is being expressed. It will be understood that, in general, when a heterologous gene or polypeptide is selected for introduction into and/or expression by a host cell, the particular source organism from which the heterologous gene or polypeptide may be selected is not essential to the practice of the present invention. Relevant considerations may include, for example, how closely related the potential source and host organisms are in evolution, or how related the source organism is with other source organisms from which sequences of other relevant polypeptides have been selected. Where a plurality of different heterologous polypeptides are to be introduced into and/or expressed by a host cell, different polypeptides may be from different source organisms, or from the same source organism. To give but one example, in some cases, individual polypeptides may represent individual subunits of a complex protein activity and/or may be required to work in concert with other polypeptides in order to achieve the goals of the present invention. In some embodiments, it will often be desirable for such polypeptides to be from the same source organism, and/or to be sufficiently related to function appropriately when expressed together in a host cell. In some embodiments, such polypeptides may be from different, even unrelated source organisms. It will further be understood that, where a heterologous polypeptide is to be expressed in a host cell, it will often be desirable to utilize nucleic acid sequences encoding the polypeptide that have been adjusted to accommodate codon preferences of the host cell and/or to link the encoding sequences with regulatory elements active in the host cell. For example, when the host cell is a Yarrowia strain (e.g., Yarrowia lipolytica ), it will often be desirable to alter the gene sequence encoding a given polypeptide such that it conforms more closely with the codon preferences of such a Yarrowia strain. In certain embodiments, a gene sequence encoding a given polypeptide is altered to conform more closely with the codon preference of a species related to the host cell. For example, when the host cell is a Yarrowia strain (e.g., Yarrowia lipolytica ), it will often be desirable to alter the gene sequence encoding a given polypeptide such that it conforms more closely with the codon preferences of a related fungal strain. Such embodiments are advantageous when the gene sequence encoding a given polypeptide is difficult to optimize to conform to the codon preference of the host cell due to experimental (e.g., cloning) and/or other reasons. In certain embodiments, the gene sequence encoding a given polypeptide is optimized even when such a gene sequence is derived from the host cell itself (and thus is not heterologous). For example, a gene sequence encoding a polypeptide of interest may not be codon optimized for expression in a given host cell even though such a gene sequence is isolated from the host cell strain. In such embodiments, the gene sequence may be further optimized to account for codon preferences of the host cell. Those of ordinary skill in the art will be aware of host cell codon preferences and will be able to employ inventive methods and compositions disclosed herein to optimize expression of a given polypeptide in the host cell. Host cell: As used herein, the “host cell” is a fungal cell or yeast cell that is manipulated according to the present invention to accumulate lipid and/or to express one or more carotenoids as described herein. A “modified host cell”, as used herein, is any host cell which has been modified, engineered, or manipulated in accordance with the present invention as compared with a parental cell. In some embodiments, the modified host cell has at least one carotenogenic and/or at least one oleaginic modification. In some embodiments, the modified host cell containing at least one oleaginic modification and/or one carotenogenic modification further has at least one sterologenic modification and/or at least one quinonogenic modification. In some embodiments, the parental cell is a naturally occurring parental cell. Isolated: The term “isolated”, as used herein, means that the isolated entity has been separated from at least one component with which it was previously associated. When most other components have been removed, the isolated entity is “purified” or “concentrated”. Isolation and/or purification and/or concentration may be performed using any techniques known in the art including, for example, fractionation, extraction, precipitation, or other separation. Isoprenoid biosynthesis competitor: The term “isoprenoid biosynthesis competitor”, as used herein, refers to an agent whose presence or activity in a cell reduces the level of geranylgeranyl diphosphate (GGPP) available to enter the carotenoid biosynthesis pathway. The term “isoprenoid biosynthesis competitor” encompasses both polypeptide and non-polypeptide (e.g., small molecule) inhibitor agents. Those of ordinary skill in the art will appreciate that certain competitor agents that do not act as inhibitors of isoprenoid biosynthesis generally can nonetheless act as inhibitors of biosynthesis of a particular isoprenoid compound. Particular examples of isoprenoid biosynthesis competitor agents act on isoprenoid intermediates prior to GGPP, such that less GGPP is generated (see, for example, FIG. 5 ). Squalene synthase is but one isoprenoid biosynthesis competitor polypeptide according to the present invention; representative squalene synthase sequences are presented in Table 16. Prenyldiphosphate synthase enzymes and para-hydroxybenzoate (PHB) polyprenyltransferase are yet additional isoprenoid biosynthesis competitor polypeptides according to the present invention; representative prenyldiphosphate synthase enzymes and PHB polyprenyltransferase polypeptides are presented in Tables 29 and 30, respectively. In certain embodiments, one or more polypeptide components of the SAGA complex are isoprenoid biosynthesis competitors according to the present invention. Genes encoding SAGA complex polypeptides are presented in Table 69. In certain embodiments, a polypeptide encoded by these and other SAGA complex genes is an isoprenoid biosynthesis competitor polypeptide according to the present invention. Those of ordinary skill in the art, considering the known metabolic pathways relating to isoprenoid production and/or metabolism (see, for example, FIGS. 3-6 and other Figures and references herein) will readily appreciate a variety of other particular isoprenoid biosynthesis competitors, including isoprenoid biosynthesis polypeptides. Isoprenoid biosynthesis polypeptide: The term “isoprenoid biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of isoprenoids. For example, as discussed herein, acetoacetyl-CoA thiolase, HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, mevalonate pyrophosphate decarboxylase, IPP isomerase, FPP synthase, and GGPP synthase, are all involved in the mevalonate pathway for isoprenoid biosynthesis. Each of these proteins is also an isoprenoid biosynthesis polypeptide for purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 7-15. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, isoprenoid biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other isoprenoid biosynthesis polypeptides (e.g., of one or more enzymes that participates in isoprenoid synthesis). Thus, for instance, transcription factors that regulate expression of isoprenoid biosynthesis enzymes can be isoprenoid biosynthesis polypeptides for purposes of the present invention. To give but a couple of examples, the S. cerevisae Upc2 and YLR228c genes, and the Y. lipolytica YALI0B00660g gene encode transcription factors that are isoprenoid biosynthesis polypeptides according to certain embodiments of the present invention. For instance, the semidominant upc2-1 point mutant (G888D) exhibits increases sterol levels (Crowley et al. J Bacteriol. 180: 4177-4183, 1998). Corresponding YLR228c mutants have been made and tested (Shianna et al. J Bacteriology 183:830-834, 2001); such mutants may be useful in accordance with the present invention, as may be YALI0B00660g derivatives with corresponding upc2-1 mutation(s). Isoprenoid pathway: The term “isoprenoid pathway” is understood in the art to refer to a metabolic pathway that either produces or utilizes the five-carbon metabolite isopentyl pyrophosphate (IPP). As discussed herein, two different pathways can produce the common isoprenoid precursor IPP—the “mevalonate pathway” and the “non-mevalonate pathway”. The term “isoprenoid pathway” is sufficiently general to encompass both of these types of pathway. Biosynthesis of isoprenoids from IPP occurs by polymerization of several five-carbon isoprene subunits. Isoprenoid metabolites derived from IPP are of varying size and chemical structure, including both cyclic and acyclic molecules. Isoprenoid metabolites include, but are not limited to, monoterpenes, sesquiterpenes, diterpenes, sterols, and polyprenols such as carotenoids. Oleaginic modification: The term “oleaginic modification”, as used herein, refers to a modification of a host organism that adjusts the desirable oleaginy of that host organism, as described herein. In some cases, the host organism will already be oleaginous in that it will have the ability to accumulate lipid to at least about 20% of its dry cell weight. It may nonetheless be desirable to apply an oleaginic modification to such an organism, in accordance with the present invention, for example to increase (or, in some cases, possibly to decrease) its total lipid accumulation, or to adjust the types or amounts of one or more particular lipids it accumulates (e.g., to increase relative accumulation of triacylglycerol). In other cases, the host organism may be non-oleaginous (though may contain some enzymatic and regulatory components used in other organisms to accumulate lipid), and may require oleaginic modification in order to become oleaginous in accordance with the present invention. The present invention also contemplates application of oleaginic modification to non-oleaginous host strains such that their oleaginicity is increased even though, even after being modified, they may not be oleaginous as defined herein. In principle, the oleaginic modification may be any chemical, physiological, genetic, or other modification that appropriately alters oleaginy of a host organism as compared with an otherwise identical organism not subjected to the oleaginic modification. In most embodiments, however, the oleaginic modification will comprise a genetic modification, typically resulting in increased production and/or activity of one or more oleaginic polypeptides. In some embodiments, the oleaginic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the oleaginic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical and/or physiological modification(s)). Oleaginic polypeptide: The term “oleaginic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of lipid accumulation in a cell and may include polypeptides that are involved in processes other than lipid biosynthesis but whose activities affect the extent or level of accumulation of one or more lipids, for example by scavenging a substrate or reactant utilized by an oleaginic polypeptide that is directly involved in lipid accumulation. For example, as discussed herein, acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, malate dehydrogenase, and AMP deaminase, among other proteins, are all involved in lipid accumulation in cells. In general, reducing the activity of pyruvate decarboxylase or isocitrate dehydrogenase, and/or increasing the activity of acetyl CoA carboxylase, ATP-citrate lyase, malic enzyme, malate dehydrogenase, and/or AMP deaminase is expected to promote oleaginy. Each of these proteins is an oleaginic peptide for the purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 1-6, and 30. Other peptides that can be involved in regenerating NADPH may include, for example, 6-phosphogluconate dehydrogenase (gnd); Fructose 1,6 bisphosphatase (fbp); Glucose 6 phosphate dehydrogenase (g6pd); NADH kinase (EC 2.7.1.86); and/or transhydrogenase (EC 1.6.1.1 and 1.6.1.2). Alternative or additional strategies to promote oleaginy may include one or more of the following: (1) increased or heterologous expression of one or more of acyl-CoA:diacylglycerol acyltransferase (e.g., DGA1; YALI0E32769g); phospholipid:diacylglycerol acyltransferase (e.g., LRO1; YALI0E16797g); and acyl-CoA:cholesterol acyltransferase (e.g., ARE genes such as ARE1, ARE2, YALI0F06578g), which are involved in triglyceride synthesis (Kalscheuer et al. Appl Environ Microbiol p. 7119-7125, 2004; Oelkers et al. J Biol Chem 277:8877-8881, 2002; and Sorger et al. J Biol Chem 279:31190-31196, 2004), (2) decreased expression of triglyceride lipases (e.g., TGL3 and/or TGL4; YALI0D17534g and/or YALI0F10010g (Kurat et al. J Biol Chem 281:491-500, 2006); and (3) decreased expression of one or more acyl-coenzyme A oxidase activities, for example encoded by POX genes (e.g. POX1, POX2, POX3, POX4, POX5; YALI0C23859g, YALI0D24750g, YALI0E06567g, YALI0E27654g, YALI0E32835g, YALI0F10857g; see, for example, Mlickova et al. Appl Environ Microbiol 70: 3918-3924, 2004; Binns et al. J Cell Biol 173:719, 2006). Each of these proteins is an oleaginic peptide for the purposes of the present invention, and sequences of representative examples of these enzymes are provided in Tables 31-43 and 45-47. Oleaginous: The term “oleaginous”, refers to the ability of an organism to accumulate lipid to at least about 20% of its dry cell weight. In certain embodiments of the invention, oleaginous yeast or fungi accumulate lipid to at least about 25% of their dry cell weight. In other embodiments, inventive oleaginous yeast or fungi accumulate lipid within the range of about 20-45% (e.g., about 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, 41%, 42%, 43%, 44%, 45%, or more) of their dry cell weight. In some embodiments, oleaginous organisms may accumulate lipid to as much as about 70% of their dry cell weight. In some embodiments of the invention, oleaginous organisms may accumulate a large fraction of total lipid accumulation in the form of triacylglycerol. In certain embodiments, the majority of the accumulated lipid is in the form of triacylglycerol. Alternatively or additionally, the lipid may accumulate in the form of intracellular lipid bodies, or oil bodies. In certain embodiments, the present invention utilizes yeast or fungi that are naturally oleaginous. In some aspects, naturally oleaginous organisms are manipulated (e.g., genetically, chemically, or otherwise) so as to further increase the level of accumulated lipid in the organism. In other embodiments, yeast or fungi that are not naturally oleaginous are manipulated (e.g., genetically, chemically, or otherwise) to accumulate lipid as described herein. For example, for the purposes of the present invention, Saccharomyces cerevisiae, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), and Candida utilis are not naturally oleaginous fungi. PHB polypeptide or PHB biosynthesis polypeptide: The terms “PHB polypeptide” or “PHB biosynthesis polypeptide” as used herein refers to a polypeptide that is involved in the synthesis of para-hydroxybenzoate from chorismate. In prokaryotes and lower eukaryotes, synthesis of para-hydroxybenzoate occurs by the action of chorismate pyruvate lyase. Biosynthesis of para-hydroxybenzoate from tyrosine or phenylalanine occurs through a five-step process in mammalian cells. Lower eukaryotes such as yeast can utilize either method for production of para-hydroxybenzoate. For example, enzymes of the shikimate pathway, chorismate synthase, DAHP synthase, and transketolase are all PHB biosynthesis polypeptides. Each of these polypeptides is also a ubiquinone biosynthesis polypeptide or a ubiquinone biosynthesis competitor polypeptide for purposes of the present invention. Polypeptide: The term “polypeptide”, as used herein, generally has its art-recognized meaning of a polymer of at least three amino acids. However, the term is also used to refer to specific functional classes of polypeptides, such as, for example, oleaginic polypeptides, carotenogenic polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, etc. For each such class, the present specification provides several examples of known sequences of such polypeptides. Those of ordinary skill in the art will appreciate, however, that the term “polypeptide” is intended to be sufficiently general as to encompass not only polypeptides having the complete sequence recited herein (or in a reference or database specifically mentioned herein), but also to encompass polypeptides that represent functional fragments (i.e., fragments retaining at least one activity) of such complete polypeptides. Moreover, those of ordinary skill in the art understand that protein sequences generally tolerate some substitution without destroying activity. Thus, any polypeptide that retains activity and shares at least about 30-40% overall sequence identity, often greater than about 50%, 60%, 70%, or 80%, and further usually including at least one region of much higher identity, often greater than 90% or even 95%, 96%, 97%, 98%, or 99% in one or more highly conserved regions (e.g., isocitrate dehydrogenase polypeptides often share a conserved AMP-binding motif; HMG-CoA reductase polypeptides typically include a highly conserved catalytic domain (see, for example, FIG. 7 ); acetyl coA carboxylase typically has a carboxyl transferase domain; see, for example, Downing et al., Chem. Abs. 93:484, 1980; Gil et al., Cell 41:249, 1985; Jitrapakdee et al. Curr Protein Pept Sci. 4:217, 2003; U.S. Pat. No. 5,349,126, each of which is incorporated herein by reference in its entirety), usually encompassing at least 3-4 and often up to 20 or more amino acids, with another polypeptide of the same class, is encompassed within the relevant term “polypeptide” as used herein. Other regions of similarity and/or identity can be determined by those of ordinary skill in the art by analysis of the sequences of various polypeptides presented in the Tables herein. Quinone biosynthesis polypeptide: A “quinone biosynthesis polypeptide”, as that term is used herein, refers to any polypeptide involved in the synthesis of one or more quinone derived compound, as described herein. In particular, quinone biosynthesis polypeptides include ubiquinone biosynthesis polypeptides, C 5-9 quinone biosynthesis polypeptides, vitamin K biosynthesis polypeptides, and vitamin E biosynthesis polypeptides. Quinonogenic modification: The term “quinonogenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more quinone derived compounds (e.g., ubiquinone, vitamin K compounds, vitamin E compounds, etc.), as described herein. For example, a quinonogenic modification may increase the production level of a particular quinone derived compound, or of a variety of different quinone derived compounds. In some embodiments of the invention, production of a particular quinone derived compound may be increased while production of other quinone derived compounds is decreased. In some embodiments of the invention, production of a plurality of different quinone derived compounds is increased. In principle, an inventive quinonogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more quinone derived compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the quinonogenic modification will comprise a genetic modification, typically resulting in increased production of one or more quinone derived compounds (e.g., ubiquinone, vitamin K compounds, vitamin E compounds). In some embodiments, the quinonogenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the quinonogenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical and/or physiological modification(s)). Retinologenic modification: The term “retinologenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more retinolic compounds, as described herein. For example, a retinologenic modification may increase the production level of one or more retinolic compounds, and/or may alter relative production levels of different retinolic compounds. In principle, an inventive retinologenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more retinolic compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the retinologenic modification will comprise a genetic modification, typically resulting in increased production of one or more selected retinolic compounds. In some embodiments, the retinologenic modification comprises at least one chemical, physiological, genetic, or other modification; in other embodiments, the retinologenic modification comprises more than one chemical, physiological, genetic, or other modification. In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic, chemical, and/or physiological modification(s)). In some embodiments, the selected retinolic compound is one or more of retinol, retinal, and retinoic acid. In some embodiments, the selected retinolic compound is retinol or esters of retinol, including but not limited to retinyl palmitate or retinyl acetate. In some embodiments, the selected retinolic compound is retinoic acid. In some embodiments, the selected retinolic compound is other than retinol. Retinologenic polypeptide: The term “retinologenic polypeptide”, as used herein, refers to any polypeptide that is involved in the process of producing retinolic compounds in a cell, and may include polypeptides that are involved in processes other than retinolic compound production but whose activities affect the extent or level of production of one or more retinolic compounds, for example by scavenging a substrate or reactant utilized by a retinologenic polypeptide that is directly involved in retinolic compound production. Retinologenic polypeptides include retinolic compound biosynthesis polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, and isoprenoid biosynthesis competitor polypeptides, as those terms are defined herein. The term also encompasses polypeptides that may affect the extent to which retinolic compounds are accumulated in lipid bodies. Retinolic compounds: The term “retinolic compound” is understood in the art to refer to a structurally similar class of compounds derived from certain carotenoids, collectively referred to as Vitamin A. All forms of Vitamin A have a beta-ionone ring to which an isoprenoid chain is attached. Retinolic compounds include, for example, retinol (the alcohol form), retinal (the aldehyde form), and retinoic acid (the acid form). Many different geometric isomers of retinol, retinal and retinoic acid are possible as a result of either a trans or cis configuration of four of the five double bonds found in the polyene chain. The cis isomers are less stable and can readily convert to the all-trans configuration. Nevertheless, some cis isomers are found naturally and carry out essential functions. For example, the 11-cis-retinal isomer is the chromophore of rhodopsin, the vertebrate photoreceptor molecule. The term retinolic compound also includes esters of retinol such as retinyl palmitate or retinyl acetate. Hydrolysis of retinyl esters results in retinol. Retinal, also known as retinaldehyde, can be reversibly reduced to produce retinol or it can be irreversibly oxidized to produce retinoic acid. The best described active retinoid metabolites are 11-cis-retinal and the all-trans and 9-cis-isomers of retinoic acid. Retinolic compound biosynthesis polypeptides: The term “retinolic compound biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more retinolic compounds. To mention but a few, these retinolic compound biosynthesis polypeptides include, for example, polypeptides of beta-carotene 15,15′-monooxygenase (also known as beta-carotene dioxygenase) and/or beta-carotene retinol dehydrogenase. In some instances, a single gene may encode a protein with multiple retinolic compound biosynthesis polypeptide activities. Representative examples of retinolic compound biosynthesis polypeptide sequences are presented in Tables 67 and 68. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, retinolic compound biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other retinolic compound biosynthesis polypeptides. Small Molecule: In general, a small molecule is understood in the art to be an organic molecule that is less than about 5 kilodaltons (Kd) in size. In some embodiments, the small molecule is less than about 3 Kd, 2 Kd, or 1 Kd. In some embodiments, the small molecule is less than about 800 daltons (D), 600 D, 500 D, 400 D, 300 D, 200 D, or 100 D. In some embodiments, small molecules are non-polymeric. In some embodiments, small molecules are not proteins, peptides, or amino acids. In some embodiments, small molecules are not nucleic acids or nucleotides. In some embodiments, small molecules are not saccharides or polysaccharides. Source organism: The term “source organism”, as used herein, refers to the organism in which a particular polypeptide sequence can be found in nature. Thus, for example, if one or more heterologous polypeptides is/are being expressed in a host organism, the organism in which the polypeptides are expressed in nature (and/or from which their genes were originally cloned) is referred to as the “source organism”. Where multiple heterologous polypeptides are being expressed in a host organism, one or more source organism(s) may be utilized for independent selection of each of the heterologous polypeptide(s). It will be appreciated that any and all organisms that naturally contain relevant polypeptide sequences may be used as source organisms in accordance with the present invention. Representative source organisms include, for example, animal, mammalian, insect, plant, fungal, yeast, algal, bacterial, cyanobacterial, archaebacterial and protozoal source organisms. Sterol biosynthesis polypeptide: The term “sterol biosynthesis polypeptide”, as used herein, refers to any polypeptide that is involved in the synthesis of one or more sterol compounds. Thus, sterol biosynthesis polypeptides can include isoprenoid biosynthesis polypeptides to the extent that they are involved in production of isopentyl pyrophosphate. Moreover, the term refers to any polypeptide that acts downstream of farnesyl pyrophosphate and in involved in the production of one or more sterol compounds. For example, sterol biosynthesis polypeptides include squalene synthase, which catalyses conversion of farnesyl pyrophosphate to presqualene pyrophosphate, and further catalyzes conversion of presqualene pyrophosphate to squalene, e.g., the enzyme with EC number 2.5.1.21. In some embodiments of the invention, sterol biosynthesis polypeptides further include one or more polypeptides involved in metabolizing squalene into a vitamin D compound. Thus, sterol biosynthesis polypeptides can include one or more of the polypeptides designated by EC number 1.14.99.7, 5.4.99.7, 5.4.99.8, 5.3.3.5, 1.14.21.6, 1.14.15.-, and/or 1.14.13.13, as well as other enzyme polypeptides involved in the sterol biosynthesis pathways. Furthermore, sterol biosynthesis polypeptides can include one or more enzyme polypeptides including, for example, C-14 demethylase (ERG9), squalene monooxygenase (ERG1), 2,3-oxidosqualene-lanosterol synthase (ERG7), C-1 demethylase (ERG11), C-14 reductase (ERG24), C-4 methyloxidase (ERG25), C-4 decarboxylase (ERG26), 3-ketoreductase (ERG27), C-24 methyltransferase (ERG6), Δ8-7 isomerase (ERG2), C-5 desaturase (ERG3), C-22 desaturase (ERG5) and/or C-24 reductase (ERG4) polypeptides, and/or other polypeptides involved in producing one or more vitamin D compounds (e.g., vitamin D2, vitamin D3, or a precursor thereof). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, sterol biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other sterol biosynthesis polypeptides. Thus, for instance, transcription factors that regulate expression of sterol biosynthesis enzymes can be sterol biosynthesis polypeptides for purposes of the present invention. To give but a couple of examples, the S. cerevisiae Upc2 and YLR228c genes, and the Y. lipolytica YALI0B00660g gene encode transcription factors that are sterol biosynthesis polypeptides according to certain embodiments of the present invention. For instance, the semidominant upc2-1 point mutation (G888D) exhibits increased sterol levels (Crowley et al., J. Bacteriol 180:4177-4183, 1998). Corresponding YLR228c mutants have been made and tested (Shianna et al., J Bacteriol 183:830, 2001); such mutants may be useful in accordance with the present invention, as may be YALI0B00660g derivatives with corresponding upc2-1 mutation(s). Representative examples of sterol biosynthesis polypeptide sequences are presented in Tables 53-66. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, sterol biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other sterol biosynthesis polypeptides. Sterologenic modification: The term “sterologenic modification”, as used herein, refers to a modification of a host organism that adjusts production of one or more sterol compounds (e.g., squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3), vitamin D compound(s), etc.), as described herein. For example, a sterologenic modification may increase the production level of a particular sterol compound, or of a variety of different sterol compounds. In some embodiments of the invention, production of a particular sterol compound may be increased while production of other sterol compounds is decreased. In some embodiments of the invention, production of a plurality of different sterol compounds is increased. In principle, an inventive sterologenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of one or more sterol compounds in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the sterologenic modification will comprise a genetic modification, typically resulting in increased production of one or more sterol compounds (e.g., squalene, lanosterol, zymosterol, ergosterol, 7-dehydrocholesterol (provitamin D3) or vitamin D compound(s)). In certain aspects where more than one modification is utilized, such modifications can comprise any combination of chemical, physiological, genetic, or other modification (e.g., one or more genetic modification and chemical or physiological modification). Ubiquinone biosynthesis polypeptide: The term “ubiquinone biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of ubiquinone. To mention but a few, these ubiquinone biosynthesis polypeptides include, for example, polypeptides of prenyldiphosphate synthase, PHB-polyprenyltransferase, and O-methyltransferase, as well as C 5-9 quinone biosynthesis polypeptides. As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, ubiquinone biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other ubiquinone biosynthesis polypeptides. Ubiquinogenic modification: The term “ubiquinogenic modification”, as used herein, refers to a modification of a host organism that adjusts production of ubiquinone (e.g., CoQ10), as described herein. For example, a ubiquinogenic modification may increase the production level of ubiquinone (e.g., CoQ10), and/or may alter relative levels of ubiquinone and/or ubiquinol. In principle, an inventive ubiquinogenic modification may be any chemical, physiological, genetic, or other modification that appropriately alters production of ubiquinone (e.g., CoQ10) in a host organism produced by that organism as compared with the level produced in an otherwise identical organism not subject to the same modification. In most embodiments, however, the ubiquinogenic modification will comprise a genetic modification, typically resulting in increased production of ubiquinone (CoQ10). Vitamin D biosynthesis polypeptide: The term “vitamin D biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of one or more vitamin D compounds. To mention but a few, these include, for example, polypeptides enzymes with EC numbers the 1.14.99.7, 5.4.99.7, 5.4.99.8, 5.3.3.5, and/or 1.14.21.6. They further can include the hydroxylases that convert vitamin D 3 to calcitriol (e.g., polypeptides enzymes with EC numbers 1.14.15.- and 1.14.13.13). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin D biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other vitamin D biosynthesis polypeptides. Vitamin E biosynthesis polypeptide: The term “vitamin E biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of vitamin E. To mention but a few, these include, for example, tyrA, pds1(hppd), VTE1, HPT1(VTE2), VTE3, VTE4, and/or GGH polypeptides (i.e., polypeptides that perform the chemical reactions performed by tyrA, pds1(hppd), VTE1, HPT1(VTE2), VTE3, VTE4, and/or GGH, respectively). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin E biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other vitamin E biosynthesis polypeptides. Vitamin K biosynthesis polypeptide: The term “vitamin K biosynthesis polypeptide” refers to any polypeptide that is involved in the synthesis of vitamin K. To mention but a few, these include, for example, MenF, MenD, MenC, MenE, MenB, MenA, UbiE, and/or MenG polypeptides (i.e., polypeptides that perform the chemical reactions performed by MenF, MenD, MenC, MenE, MenB, MenA, UbiE, and/or MenG, respectively). As will be appreciated by those of ordinary skill in the art, in some embodiments of the invention, vitamin K biosynthesis polypeptides include polypeptides that affect the expression and/or activity of one or more other carotenoid biosynthesis polypeptides. DETAILED DESCRIPTION OF CERTAIN PREFERRED EMBODIMENTS OF THE INVENTION As noted above, the present invention encompasses the discovery that carotenoids and/or retinolic compounds can desirably be produced in oleaginous yeast and fungi. According to the present invention, strains that both (i) accumulate lipid, often in the form of cytoplasmic oil bodies and typically to at least about 20% of their dry cell weight; and (ii) produce carotenoid(s) and/or retinolic compound(s) at a level at least about 1%, and in some embodiments at least about 3-20%, of their dry cell weight, are generated through manipulation of host cells (i.e., strains, including, e.g., naturally-occurring strains, strains which have been previously modified, etc.). These manipulated host cells are then used to produce carotenoids and/or retinolic compounds, so that carotenoids and/or retinolic compounds that partition into the lipid bodies can readily be isolated. In general, it will be desirable to balance oleaginy and carotenoid production in inventive cells such that, as soon as a minimum desirable level of oleaginy is achieved, substantially all further carbon which is capable of being utilized and diverted into biosynthesis of products is diverted into a carotenoid and/or retinolic compounds production pathway. In some embodiments of the invention, this strategy involves engineering cells to be oleaginous; in other embodiments, it involves engineering cells to accumulate a higher level of lipid, particularly cytoplasmic lipid, than they would accumulate in the absence of such engineering even though the engineered cells may not become “oleaginous” as defined herein. In other embodiments, the extent to which an oleaginous host cell accumulates lipid is actually reduced so that remaining carbon can be utilized in carotenoid and/or retinolic compound production. According to the present invention, the extent of lipid accumulation in a host cell can be adjusted by modifying the level and/or activity of one or more polypeptides involved in lipid accumulation. Such modification can take the form of genetic engineering and/or exposure to particular growth conditions that induce or inhibit lipid accumulation. To give but one example of adjustments that could be made to achieve a desired balance between oleaginy and carotenoid and/or retinolic compound production, we note that, while increasing acetyl CoA carboxylase expression (and/or activity) promotes oleaginy, decreasing its expression and/or activity can promote carotenoid and/or retinolic compound production. Those of ordinary skill in the art will appreciate that the expression and/or activity of acetyl CoA carboxylase, or of other polypeptides may be adjusted up or down as desired according to the characteristics of a particular host cell of interest. We note that engineered cells and processes of using them as described herein may provide one or more advantages as compared with unmodified cells. Such advantages may include, but are not limited to: increased yield (e.g., carotenoid and/or retinolic compound content expressed as either % dry cell weight (mg/mg) or parts per million), titer (g carotenoid/L and/or g retinolic compound/L), specific productivity (mg carotenoid g −1 biomass hour −1 and/or mg retinolic compound g −1 biomass hour −1 ), and/or volumetric productivity (g carotenoid liter −1 hour −1 and/or g retinolic compound liter −1 hour −1 )) of the desired carotenoid and/or retinolic compound (and/or intermediates thereof), and/or decreased formation of undesirable side products (for example, undesirable intermediates). Thus, for example, the specific productivity for one or more desired carotenoids (e.g. β-carotene, astaxanthin), retinolic compound (e.g., retinol, retinal, retinoic acid), total carotenoids and/or total retinolic compounds may be at or about 0.1, at or about 0.11, at or about 0.12, at or about 0.13, at or about 0.14, at or about 0.15, at or about 0.16, at or about 0.17, at or about 0.18, at or about 0.19, at or about 0.2, at or about 0.21, at or about 0.22, at or about 0.23, at or about 0.24, at or about 0.25, at or about 0.26, at or about 0.27, at or about 0.28, at or about 0.29, at or about 0.3, at or about 0.31, at or about 0.32, at or about 0.33, at or about 0.34, at or about 0.35, at or about 0.36, at or about 0.37, at or about 0.38, at or about 0.39, at or about 0.4, at or about 0.41, at or about 0.42, at or about 0.43, at or about 0.44, at or about 0.45, at or about 0.46, at or about 0.47, at or about 0.48, at or about 0.49, at or about 0.5, at or about 0.51, at or about 0.52, at or about 0.53, at or about 0.54, at or about 0.55, at or about 0.56, at or about 0.57, at or about 0.58, at or about 0.59, at or about 0.6, at or about 0.61, at or about 0.62, at or about 0.63, at or about 0.64, at or about 0.65, at or about 0.66, at or about 0.67, at or about 0.68, at or about 0.69, at or about 0.7, at or about 0.71, at or about 0.72, at or about 0.73, at or about 0.74, at or about 0.75, at or about 0.76, at or about 0.77, at or about 0.78, at or about 0.79, at or about 0.8, at or about 0.81, at or about 0.82, at or about 0.83, at or about 0.84, at or about 0.85, at or about 0.86, at or about 0.87, at or about 0.88, at or about 0.89, at or about 0.9, at or about 0.91, at or about 0.92, at or about 0.93, at or about 0.94, at or about 0.95, at or about 0.96, at or about 0.97, at or about 0.98, at or about 0.99, at or about 1, 1.05, at or about 1.1, at or about 1.15, at or about 1.2, at or about 1.25, at or about 1.3, at or about 1.35, at or about 1.4, at or about 1.45, at or about 1.5, at or about 1.55, at or about 1.6, at or about 1.65, at or about 1.7, at or about 1.75, at or about 1.8, at or about 1.85, at or about 1.9, at or about 1.95, at or about 2 mg g −1 hour −1 or more. Thus, for example, the volumetric productivity for one or more desired carotenoids (e.g. β-carotenoid, astaxanthin), retinolic compound (e.g., retinol, retinal, retinoic acid), total carotenoids and/or total retinolic compounds may be at or about 0.01, at or about 0.011, at or about 0.012, at or about 0.013, at or about 0.014, at or about 0.015, at or about 0.016, at or about 0.017, at or about 0.018, at or about 0.019, at or about 0.02, at or about 0.021, at or about 0.022, at or about 0.023, at or about 0.024, at or about 0.025, at or about 0.026, at or about 0.027, at or about 0.028, at or about 0.029, at or about 0.03, at or about 0.031, at or about 0.032, at or about 0.033, at or about 0.034, at or about 0.035, at or about 0.036, at or about 0.037, at or about 0.038, at or about 0.039, at or about 0.04, at or about 0.041, at or about 0.042, at or about 0.043, at or about 0.044, at or about 0.045, at or about 0.046, at or about 0.047, at or about 0.048, at or about 0.049, at or about 0.05, at or about 0.051, at or about 0.052, at or about 0.053, at or about 0.054, at or about 0.055, at or about 0.056, at or about 0.057, at or about 0.058, at or about 0.059, at or about 0.06, at or about 0.061, at or about 0.062, at or about 0.063, at or about 0.064, at or about 0.065, at or about 0.066, at or about 0.067, at or about 0.068, at or about 0.069, at or about 0.07, at or about 0.071, at or about 0.072, at or about 0.073, at or about 0.074, at or about 0.075, at or about 0.076, at or about 0.077, at or about 0.078, at or about 0.079, at or about 0.08, at or about 0.081, at or about 0.082, at or about 0.083, at or about 0.084, at or about 0.085, at or about 0.086, at or about 0.087, at or about 0.088, at or about 0.089, at or about 0.09, at or about 0.091, at or about 0.092, at or about 0.093, at or about 0.094, at or about 0.095, at or about 0.096, at or about 0.097, at or about 0.098, at or about 0.099, at or about 0.1, 0.105, at or about 0.110, at or about 0.115, at or about 0.120, at or about 0.125, at or about 0.130, at or about 0.135, at or about 0.14, at or about 0.145, at or about 0.15, at or about 0.155, at or about 0.16, at or about 0.165, at or about 0.17, at or about 0.175, at or about 0.18, at or about 0.185, at or about 0.19, at or about 0.195, at or about 0.20 grams liter −1 hour −1 or more. Host Cells Those of ordinary skill in the art will readily appreciate that a variety of yeast and fungal strains exist that are naturally oleaginous or that naturally produce carotenoids. Yeast and fungal strains do not naturally produce retinolic compounds. Any of such strains may be utilized as host strains according to the present invention, and may be engineered or otherwise manipulated to generate inventive oleaginous, carotenoid-producing strains and/or oleaginous, retinolic acid compound-producing strains. Alternatively, strains that naturally are neither oleaginous nor: i) carotenoid-producing and/or ii) retinolic compound-producing may be employed. Furthermore, even when a particular strain has a natural capacity for oleaginy or for carotenoid production, its natural capabilities may be adjusted as described herein, so as to change the production level of lipid, carotenoid and/or retinolic compound. In certain embodiments engineering or manipulation of a strain results in modification of a type of lipid, carotenoid and/or retinolic compound which is produced. For example, a strain may be naturally oleaginous and/or carotenogenic, however engineering or modification of the strain may be employed so as to change the type of lipid which is accumulated and or to change the type of carotenoid which is produced. Additionally or alternatively, naturally oleaginous strain may be engineered to permit retinolic compound production. Moreover, further engineering or modification of the strain may be employed so as to change the type of lipid which is accumulated and/or to change the type of retinolic compound which is produced. When selecting a particular yeast or fungal strain for use in accordance with the present invention, it will generally be desirable to select one whose cultivation characteristics are amenable to commercial scale production. For example, it will generally (though not necessarily always) be desirable to avoid filamentous organisms, or organisms with particularly unusual or stringent requirements for growth conditions. However, where conditions for commercial scale production can be applied which allow for utilization of filamentous organisms, these may be selected as host cells. In some embodiments of the invention, it will be desirable to utilize edible organisms as host cells, as they may optionally be formulated directly into food or feed additives, or into nutritional supplements, as desired. For ease of production, some embodiments of the invention utilize host cells that are genetically tractable, amenable to molecular genetics (e.g., can be efficiently transformed, especially with established or available vectors; optionally can incorporate and/or integrate multiple genes, for example sequentially; and/or have known genetic sequence; etc), devoid of complex growth requirements (e.g., a necessity for light), mesophilic (e.g., prefer growth temperatures with in the range of about 20-32° C.) (e.g. 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32° C.), able to assimilate a variety of carbon and nitrogen sources and/or capable of growing to high cell density. Alternatively or additionally, various embodiments of the invention utilize host cells that grow as single cells rather than multicellular organisms (e.g., as mycelia). In general, when it is desirable to utilize a naturally oleaginous organism in accordance with the present invention, any modifiable and cultivatable oleaginous organism may be employed. In certain embodiments of the invention, yeast or fungi of genera including, but not limited to, Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon , and Yarrowia are employed. In certain particular embodiments, organisms of species that include, but are not limited to, Blakeslea trispora, Candida pulcherrima, C. revkaufi, C. tropicalis, Cryptococcus curvatus, Cunninghamella echinulata, C. elegans, C. japonica, Lipomyces starkeyi, L. lipoferus, Mortierella alpina, M. isabellina, M. ramanniana, M. vinacea, Mucor circinelloides, Phycomyces blakesleanus, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, R. gracilis, R. graminis, R. mucilaginosa, R. pinicola, Trichosporon pullans, T. cutaneum , and Yarrowia lipolytica are used. Of these naturally oleaginous strains, some also naturally produce carotenoids and some do not; these strains do not naturally produced retinolic compounds. In most cases, only low levels (less than about 0.05% dry cell weight) of carotenoids are produced by naturally-occurring carotenogenic, oleaginous yeast or fungi. Higher levels of β-carotene are sometimes produced, but high levels of other carotenoids are generally not observed. In general, any organism that is naturally oleaginous and non-carotenoid-producing (e.g., produce less than about 0.05% dry cell weight, do not produce the carotenoid of interest) may be utilized as a host cell in accordance with the present invention. Additionally or alternatively, any organism that is naturally oleaginous and non-retinolic compound-producing (e.g., produce less than about 0.05% dry cell weight, do not produce the retinolic compound of interest) may be utilized as a host cell in accordance with the present invention. For example, introduction of one or more retinologenic modifications (e.g., increased expression of one or more endogenous or heterologous retinologenic polypeptides), in accordance with the present invention, can achieve the goals for retinolic compound production. In some embodiments, the organism is a yeast or fungus from a genus such as, but not limited to, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Pythium, Trichosporon , and Yarrowia ; in some embodiments, the organism is of a species including, but not limited to, Mortierella alpina and Yarrowia lipolytica. Comparably, the present invention may utilize any naturally oleaginous, carotenoid-producing organism as a host cell. In general, the present invention may be utilized to increase carbon flow into the isoprenoid pathway in naturally carotenoid-producing organisms (particularly for organisms other than Blakeslea and Phycomyces ), and/or to shift production from one carotenoid (e.g., β-carotene) to another (e.g., astaxanthin). Introduction of one or more carotenogenic modifications (e.g., increased expression of one or more endogenous or heterologous carotenogenic polypeptides), in accordance with the present invention, can achieve these goals. Additionally or alternatively, the present invention may be utilized to introduce the ability to produce one or more retinolic compounds in such naturally carotenoid-producing host cells. In certain embodiments of the invention, the utilized oleaginous, carotenoid-producing organism is a yeast or fungus, for example of a genus such as, but not limited to, Blakeslea, Mucor, Phycomyces, Rhodosporidium , and Rhodotorula ; in some embodiments, the organism is of a species such as, Mucor circinelloides and Rhodotorula glutinis. When it is desirable to utilize strains that are naturally non-oleaginous as host cells in accordance with the present invention, genera of non-oleaginous yeast or fungi include, but are not limited to, Aspergillus, Botrytis, Cercospora, Fusarium ( Gibberella ), Kluyveromyces, Neurospora, Penicillium, Pichia ( Hansenula ), Puccinia, Saccharomyces, Sclerotium, Trichoderma , and Xanthophyllomyces ( Phaffia ); in some embodiments, the organism is of a species including, but not limited to, Candida utilis, Aspergillus nidulans, A. niger, A. terreus, Botrytis cinerea, Cercospora nicotianae, Fusarium fujikuroi ( Gibberella zeae ), Kluyveromyces lactis, K. lactis, Neurospora crassa, Pichia pastoris, Puccinia distincta, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei , and Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ). It will be appreciated that the term “non-oleaginous”, as used herein, encompasses both strains that naturally have some ability to accumulate lipid, especially cytoplasmically, but do not do so to a level sufficient to qualify as “oleaginous” as defined herein, as well as strains that do not naturally have any ability to accumulate extra lipid, e.g., extra-membranous lipid. It will further be appreciated that, in some embodiments of the invention, it will be sufficient to increase the natural level of oleaginy of a particular host cell, even if the modified cell does not qualify as oleaginous as defined herein. In some embodiments, the cell will be modified to accumulate at least about 19%, 18%, 17%, 16%, 15%, 14%, 13%, 12%, 11%, 10%, 9%, 8%, 7%, 6%, or 5% in dry cell weight as lipid, so long as the accumulation level is more than that observed in the unmodified parental cell. As with the naturally oleaginous organisms, some of the naturally non-oleaginous fungi naturally produce carotenoids, whereas others do not; these strains do not naturally produced retinolic compounds. Genera of naturally non-oleaginous fungi that do not naturally produce carotenoids (e.g., produce less than about 0.05% dry cell weight, do not produce a carotenoid or retinolic compound of interest) may desirably be used as host cells in accordance with the present invention include, but are not limited to, Aspergillus, Kluyveromyces, Penicillium, Saccharomyces , and Pichia ; species include, but are not limited to, Candida utilis, Aspergillus niger and Saccharomyces cerevisiae . Genera of naturally non-oleaginous fungi that do naturally produce carotenoids or retinolic compounds and that may desirably be used as host cells in accordance with the present invention include, but are not limited to, Botrytis, Cercospora, Fusarium ( Gibberella ), Neurospora, Puccinia, Sclerotium, Trichoderma , and Xanthophyllomyces ( Phaffia ); species include, but are not limited to, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ). As discussed above, any of a variety of organisms may be employed as host cells in accordance with the present invention. In certain embodiments of the invention, host cells will be Yarrowia lipolytica cells. Advantages of Y. lipolytica include, for example, tractable genetics and molecular biology, availability of genomic sequence (see, for example. Sherman et al. Nucleic Acids Res. 32(Database issue):D315-8, 2004), suitability to various cost-effective growth conditions, and ability to grow to high cell density. In addition, Y. lipolytica is naturally oleaginous, such that fewer manipulations may be required to generate an oleaginous, carotenoid-producing and/or retinolic compound-producing Y. lipolytica strain than might be required for other organisms. Furthermore, there is already extensive commercial experience with Y. lipolytica. Saccharomyces cerevisiae is also a useful host cell in accordance with the present invention, particularly due to its experimental tractability and the extensive experience that researchers have accumulated with the organism. Although cultivation of Saccharomyces under high carbon conditions may result in increased ethanol production, this can generally be managed by process and/or genetic alterations. Additional useful hosts include Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), which is experimentally tractable and naturally carotenogenic. Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ) strains can produce several carotenoids, including astaxanthin. Aspergillus niger and Mortierella alpina accumulate large amounts of citric acid and fatty acid, respectively; Mortierella alpina is also oleaginous. Neurospora or Gibberella are also useful. They are not naturally oleaginous and tend to produce very low levels of carotenoids, thus extensive modification may be required in accordance with the present invention. Neurospora and Gibberella are considered relatively tractable from an experimental standpoint. Both are filamentous fungi, such that production at commercial scales can be a challenge necessary to overcome in utilization of such strains. Mucor circinelloides is another available useful species. While its molecular genetics are generally less accessible than are those of some other organisms, it naturally produces β-carotene, thus may require less modification than other species available. Candida utilis is a further useful species. Although it is not naturally oleaginous and produces little or no carotenoids, it is amenable to genetic manipulation (for example, see Iwakiri et al. (2006) Yeast 23:23-34, Iwakiri et al. (2005) Yeast 2005 22:1079-87, Iwakiri et al. (2005) Yeast 22:1049-60, Rodriquez et al. (1998) Yeast 14:1399-406, Rodriquez et al. (1998) FEMS Microbiol Lett. 165:335-40, and Kondo et al. (1995) J Bacteriol. 177:7171-7) and furthermore is edible. Molecular genetics can be performed in Blakeslea , though significant effort may be required. Furthermore, cost-effective fermentation conditions can be challenging, as, for example, it may be required that the two mating types are mixed. Fungi of the genus Phycomyces are also possible sources which have the potential to pose fermentation process challenges, and these fungi may be less amenable to manipulate than several other potential host organisms. Additional useful hosts include strains such as Schizosaccharomyces pombe, Saitoella complicata , and Sporidiobolus ruineniae. Those of ordinary skill in the art will appreciate that the selection of a particular host cell for use in accordance with the present invention will also affect, for example, the selection of expression sequences utilized with any heterologous polypeptide to be introduced into the cell, codon bias that can optionally be engineered into any nucleic acid to be expressed in the cell, and will also influence various aspects of culture conditions, etc. Much is known about the different gene regulatory requirements, protein targeting sequence requirements, and cultivation requirements, of different host cells to be utilized in accordance with the present invention (see, for example, with respect to Yarrowia , Barth et al. FEMS Microbiol Rev. 19:219, 1997; Madzak et al. J Biotechnol. 109:63, 2004; see, for example, with respect to Xanthophyllomyces , Verdoes et al. Appl Environ Microbiol 69: 3728-38, 2003; Visser et al. FEMS Yeast Res 4: 221-31, 2003; Martinez et al. Antonie Van Leeuwenhoek. 73(2):147-53, 1998; Kim et al. Appl Environ Microbiol. 64(5):1947-9, 1998; Wery et al. Gene. 184(1):89-97, 1997; see, for example, with respect to Saccharomyces , Guthrie and Fink Methods in Enzymology 194:1-933, 1991). In certain aspects, for example, targeting sequences of the host cell (or closely related analogs) may be useful to include for directing heterologous proteins to subcellular localization. Thus, such useful targeting sequences can be added to heterologous sequence for proper intracellular localization of activity. In other aspects (e.g., addition of mitochondrial targeting sequences), heterologous targeting sequences may be eliminated or altered in the selected heterologous sequence (e.g., alteration or removal of source organism plant chloroplast targeting sequences). To give but a few specific examples, of promoters and/or regulatory sequences that may be employed in expression of polypeptides according to the present invention, useful promoters include, but are not limited to, the Leu2 promoter and variants thereof (see, for example, see U.S. Pat. No. 5,786,212); the EF1alpha protein and ribosomal protein S7 gene promoters (see, for example, PCT Application WO 97/44470); the Gpm (see US20050014270), Xpr2 (see U.S. Pat. No. 4,937,189), Tef1, Gpd1 (see, for example, US Application 2005-0014270A1), Cam1 (YALI0C24420g), YALI0D16467g, Tef4 (YALI0B12562g), Yef3 (YALI0E13277g), Pox2, Yat1 (see, for example US Application 2005-0130280; PCT Application WO 06/052754), Fba1 (see, for example WO05049805), and/or Gpat (see WO06031937) promoters; the sequences represented by SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4, SEQ ID NO: 5, SEQ ID NO: 6, SEQ ID NO: 7, SEQ ID NO: 8, SEQ ID NO: 9, SEQ ID NO: 10, SEQ ID NO: 11, and SEQ ID NO: 12, subsequences thereof, and hybrid and tandem derivatives thereof (e.g., as disclosed in US Application 2004-0146975); the sequences represented by SEQ ID NO: 1, 2, or 3 including fragments (e.g. by 462-1016 and by 197-1016 of SEQ ID NO: 1; by 5-523 of SEQ ID NO:3) and complements thereof (e.g., as disclosed in U.S. Pat. No. 5,952,195); CYP52A2A (see, for example, US Application 2002-0034788); promoter sequences from fungal (e.g., C. tropicalis ) catalase, citrate synthase, 3-ketoacyl-CoA thiolase A, citrate synthase, O-acetylhornserine sulphydrylase, protease, carnitine O-acetyltransferase, hydratase-dehydrogenase, epimerase genes; promoter sequences from Pox4 genes (see, for example, US application 2004-0265980); and/or promoter sequences from Met2, Met3, Met6, Met25 and YALI0D12903g genes. Any such promoters can be used in conjunction with endogenous genes and/or heterologous genes for modification of expression patterns of endogenous polypeptides and/or heterologous polypeptides in accordance with the present invention. Alternatively or additionally, regulatory sequences useful in accordance with the present invention may include one or more Xpr2 promoter fragments, for example as described in U.S. Pat. No. 6,083,717 (e.g. SEQ ID NOS: 1-4 also including sequences with 80% or more identity to these SEQ ID NOs) (e.g., see Example 11) in one or more copies either in single or in tandem. Similarly, exemplary terminator sequences include, but are not limited to, Y. lipolytica Xpr2 (see U.S. Pat. No. 4,937,189) and Pox2 (YALI0F10857g) terminator sequences. In some embodiments of this invention, it may be desirable to fused sequences encoding specific targeting signals to bacterial source genes. For example, in certain embodiments mitochondrial signal sequences are useful in conjunction with, e.g., bacterial polypeptides for effective targeting of polypeptides for proper functioning. Mitochondrial signal sequences are known in the art, and include, but are not limited to example, mitochondrial signal sequences provided in Table 52 below. In other embodiments, it may be desirable to utilize genes from other source organisms such as animals, plants, alga, or microalgae, fungi, yeast, insect, protozoa, and mammals. TABLE 52Examples of mitochondrial targeting sequences.ProteinSpecies(residues)GISequenceYarrowiaNUAM6689648MLSRNLSKFARAGLIRPATTSTHTRLFSVSARRlipoylitica(AA 1-34)L (SEQ ID NO: 171)YarrowiaNUHM50549567MLRLIRPRLAALARPTTRAPQALNARTHIVSVlipoylitica(AA 1-32)(SEQ ID NO: 172)SaccharomycesCoq1536190MFQRSGAAHHIKLISSRRCRFKSSFAVALNAAcerevisiae(AA 1-53)SKLVTPKILWNNPISLVSKEM (SEQ ID NO: 173)YarrowiaCoq160389562MLRVGRIGTKTLASSSLRFVAGARPKSTLTEAlipoylitica(AA 1-77)VLETTGLLKTTPQNPEWSGAVKQASRLVETDTPIRDPFSIVSQEM (SEQ ID NO: 174) Engineering Oleaginy All living organisms synthesize lipids for use in their membranes and various other structures. However, most organisms do not accumulate in excess of about 10% of their dry cell weight as total lipid, and most of this lipid generally resides within cellular membranes. Significant biochemical work has been done to define the metabolic enzymes necessary to confer oleaginy on microorganisms (primarily for the purpose of engineering single cell oils as commercial sources of arachidonic acid and docosahexaenoic acid; see for example Ratledge Biochimie 86:807, 2004, the entire contents of which are incorporated herein by reference). Although this biochemical work is compelling, there only have been a limited number of reports of de novo oleaginy being established through genetic engineering with the genes encoding the key metabolic enzymes. It should be noted that oleaginous organisms typically accumulate lipid only when grown under conditions of carbon excess and nitrogen limitation. The present invention further establishes that the limitation of other nutrients (e.g. phosphate and/or magnesium) can also induce lipid accumulation. The present invention establishes, for example, that limitation of nutrients such as phosphate and/or magnesium can induce lipid accumulation, much as is observed under conditions of nitrogen limitation. Under these conditions, the organism readily depletes the limiting nutrient but continues to assimilate the carbon source. The “excess” carbon is channeled into lipid biosynthesis so that lipids (usually triacylglycerols) accumulate in the cytosol, typically in the form of bodies. It should be noted that oleaginous organisms typically only accumulate lipid when grown under conditions of carbon excess and nitrogen or other nutrient limitation (e.g. phosphate or magnesium). Under these conditions, the organism readily depletes the limiting nutrient but continues to assimilate the carbon source. The “excess” carbon is channeled into lipid biosynthesis so that lipids (usually triacylglycerols) accumulate in the cytosol, typically in the form of bodies. In general, it is thought that, in order to be oleaginous, an organism must produce both acetyl-CoA and NADPH in the cytosol, which can then be utilized by the fatty acid synthase machinery to generate lipids. In at least some oleaginous organisms, acetyl-CoA is generated in the cytosol through the action of ATP-citrate lyase, which catalyzes the reaction: citrate+CoA+ATP→acetyl-CoA+oxaloacetate+ADP+P i . (1) Of course, in order for ATP-citrate lyase to generate appropriate levels of acetyl-CoA in the cytosol, it must first have an available pool of its substrate citric acid. Citric acid is generated in the mitochondria of all eukaryotic cells through the tricarboxylic acid (TCA) cycle, and can be moved into the cytosol (in exchange for malate) by citrate/malate translocase. In most oleaginous organisms, and in some non-oleaginous organisms, the enzyme isocitrate dehydrogenase, which operates as part of the TCA cycle in the mitochondria, is strongly AMP-dependent. Thus, when AMP is depleted from the mitochondria, this enzyme is inactivated. When isocitrate dehydrogenase is inactive, isocitrate accumulates in the mitochondria. This accumulated isocitrate is then equilibrated with citric acid, presumably through the action of aconitase. Therefore, under conditions of low AMP, citrate accumulates in the mitochondria. As noted above, mitochondrial citrate is readily transported into the cytosol. AMP depletion, which in oleaginous organisms is believed to initiate the cascade leading to accumulation of citrate (and therefore acetyl-CoA) in the cytoplasm, occurs as a result of the nutrient depletion mentioned above. When oleaginous cells are grown in the presence of excess carbon source but under conditions limiting for nitrogen or some other nutrient(s) (e.g., phosphate or magnesium), the activity of AMP deaminase, which catalyzes the reaction: AMP→inosine 5′-monophosphate+NH 3 (2) is strongly induced. The increased activity of this enzyme depletes cellular AMP in both the cytosol and the mitochondria. Depletion of AMP from the mitochondria is thought to inactivate the AMP-dependent isocitrate dehydrogenase, resulting in accumulation of citrate in the mitochondria and, therefore, the cytosol. This series of events is depicted diagrammatically in FIG. 2 . As noted above, oleaginy requires both cytosolic acetyl-CoA and cytosolic NADPH. It is believed that, in many oleaginous organisms, appropriate levels of cytosolic NADPH are provided through the action of malic enzyme (Enzyme 3 in FIG. 2 ). Some oleaginous organisms (e.g., Lipomyces and some Candida ) do not appear to have malic enzymes, however, so apparently other enzymes can provide comparable activity, although it is expected that a dedicated source of NADPH is probably required for fatty acid synthesis (see, for example, Wynn et al., Microbiol 145:1911, 1999; Ratledge Adv. Appl. Microbiol. 51:1, 2002, each of which is incorporated herein by reference in its entirety). Other activities which can be involved in regenerating NADPH include, for example, 6-phosphogluconate dehydrogenase (gnd); Fructose 1,6 bisphosphatase (fbp); Glucose 6 phosphate dehydrogenase (g6pd); NADH kinase (EC 2.7.1.86); and/or transhydrogenase (EC 1.6.1.1 and 1.6.1.2). Gnd is part of the pentose phosphate pathway and catalyses the reaction: 6-phospho-D-gluconate+NADP+→D-ribulose 5-phosphate+CO 2 +NADPH Fbp is a hydrolase that catalyses the gluconeogenic reaction: D-fructose 1,6-bisphosphate+H 2 O→D-fructose 6-phosphate+phosphate Fbp redirects carbon flow from glycolysis towards the pentose phosphate pathway. The oxidative portion of the pentose phosphate pathway, which includes glucose 6 phosphate dehydrogenase and 6-phosphogluconate dehydrogenase, enables the regeneration of NADPH. G6pd is part of the pentose phosphate pathway and catalyses the reaction: D-glucose 6-phosphate+NADP + →D-glucono-1,5-lactone 6-phosphate+NADPH+H + NADH kinase catalyzes the reaction: ATP+NADH→ADP+NADPH Transhydrogenase catalyzes the reaction: NADPH+NAD + NADP + +NADH Thus, enhancing the expression and/or activity of any of these enzymes can increase NADPH levels and promote anabolic pathways requiring NADPH. Alternative or additional strategies to promote oleaginy may include one or more of the following: (1) increased or heterologous expression of one or more of acyl-CoA:diacylglycerol acyltransferase (e.g., DGA1; YALI0E32769g); phospholipid:diacylglycerol acyltransferase (e.g., LRO1; YALI0E16797g); and acyl-CoA:cholesterol acyltransferase (e.g., ARE genes such as ARE1, ARE2, YALI0F06578g), which are involved in triglyceride synthesis (Kalscheuer et al. Appl Environ Microbiol p. 7119-7125, 2004; Oelkers et al. J Biol Chem 277:8877-8881, 2002; and Sorger et al. J Biol Chem 279:31190-31196, 2004), (2) decreased expression of triglyceride lipases (e.g., TGL3 and/or TGL4; YALI0D17534g and/or YALI0F10010g (Kurat et al. J Biol Chem 281:491-500, 2006); and (3) decreased expression of one or more acyl-coenzyme A oxidase activities, for example encoded by POX genes (e.g. POX1, POX2, POX3, POX4, POX5; YALI0C23859g, YALI0D24750g, YALI0E06567g, YALI0E27654g, YALI0E32835g, YALI0F10857g; see for example Mlickova et al. Appl Environ Microbiol 70: 3918-3924, 2004; Binns et al. J Cell Biol 173:719, 2006). Thus, according to the present invention, the oleaginy of a host organism may be enhanced by modifying the expression or activity of one or more polypeptides involved in generating cytosolic acetyl-CoA and/or NADPH and/or altering lipid levels through other mechanisms. For example, modification of the expression or activity of one or more of acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, AMP-deaminase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, fructose 1,6 bisphosphatase, NADH kinase, transhydrogenase, acyl-CoA:diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, acyl-CoA:cholesterol acyltransferase, triglyceride lipase, acyl-coenzyme A oxidase can enhance oleaginy in accordance with the present invention. Exemplary polypeptides which can be utilized or derived so as to enhance oleaginy in accordance with the present invention include, but are not limited to those acetyl-CoA carboxylase, pyruvate decarboxylase, isocitrate dehydrogenase, ATP-citrate lyase, malic enzyme, AMP-deaminase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, fructose 1,6 bisphosphatase, NADH kinase, transhydrogenase, acyl-CoA:diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, acyl-CoA:cholesterol acyltransferase, triglyceride lipase, acyl-coenzyme A oxidase polypeptides provided in Tables 1-6, and 31-47, respectively. In some embodiments of the invention, where an oleaginous host cell is employed, enzymes and regulatory components relevant to oleaginy are already in place but could be modified, if desired, by for example altering expression or activity of one or more oleaginic polypeptides and/or by introducing one or more heterologous oleaginic polypeptides. In those embodiments of the invention where a non-oleaginous host cell is employed, it is generally expected that at least one or more heterologous oleaginic polypeptides will be introduced. The present invention contemplates not only introduction of heterologous oleaginous polypeptides, but also adjustment of expression or activity levels of heterologous or endogenous oleaginic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) and/or regulatory factors (e.g., polypeptides that modulate transcription, splicing, translation, modification, etc.) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous oleaginic polypeptide(s)); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., oleaginic polypeptide(s)). In some embodiments, at least one oleaginic polypeptide is introduced into a host cell. In some embodiments of the invention, a plurality (e.g., two or more) of different oleaginic polypeptides is introduced into the same host cell. In some embodiments, the plurality of oleaginic polypeptides contains polypeptides from the same source organism; in other embodiments, the plurality includes polypeptides independently selected from different source organisms. Representative examples of a variety of oleaginic polypeptides that may be introduced into or modified within host cells according to the present invention, include, but are not limited to, those provided in Tables 1-6, and Tables 31-47. As noted above, it is expected that at least some of these polypeptides (e.g., malic enzyme and ATP-citrate lyase) should desirably act in concert, and possibly together with one or more components of fatty acid synthase, such that, in some embodiments of the invention, it will be desirable to utilize two or more oleaginic polypeptides from the same source organism. In certain embodiments, the oleaginy of a host organism is enhanced by growing the organism on a carbon source comprising one or more oils. For example, an organism may be grown on a carbon source comprising one or more oils selected from the group consisting of, for example, olive, canola, corn, sunflower, soybean, cottonseed, rapeseed, etc., and combinations thereof. In certain embodiments, the oleaginy of a host organism is enhanced by growing the organism on a carbon source comprising one or more oils in combination with modifying the expression or activity of one or more polypeptides such as any of those described above (e.g., oleaginic polypeptides such as polypeptides involved in generating cytosolic acetyl-CoA and/or NADPH) and/or altering lipid levels through other mechanisms. In general, source organisms for oleaginic polypeptides to be used in accordance with the present invention include, but are not limited to, Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium ( Gibberella ), Kluyveromyces, Neurospora, Penicillium, Pichia ( Hansenula ), Puccinia, Saccharomyces, Sclerotium, Trichoderma , and Xanthophyllomyces ( Phaffia ). In some embodiments, the source species for acetyl CoA carboxylase, ATP-citrate lyase, malice enzyme and/or AMP deaminase polypeptides include, but are not limited to, Aspergillus nidulans, Cryptococcus neoformans, Fusarium fujikuroi, Kluyveromyces lactis, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Ustilago maydis , and Yarrowia lipolytica ; in some embodiments, source species for pyruvate decarboxylase or isocitrate dehydrogenase polypeptides include, but are not limited to Neurospora crassa, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), Aspergillus niger, Saccharomyces cerevisiae, Mucor circinelloides, Rhodotorula glutinis, Candida utilis, Mortierella alpina , and Yarrowia lipolytica. Aspergillus niger accumulates large amounts of citric acid, whereas Mortierella alpina and Thraustochytrium sp. accumulate large amounts of fatty acid, respectively; Mortierella alpina and Thraustochytrium are also oleaginous. To give but one particular example of a host cell engineered to be oleaginous (or at least to accumulate increased levels of lipid) in accordance with the present invention, S. cerevisiae can be engineered to express one or more oleaginic polypeptides, e.g., from heterologous source organisms. In some embodiments, a plurality of different oleaginic polypeptides are expressed, optionally from different source organisms. For instance, in some embodiments, S. cerevisiae cells are engineered to express (and/or to increase expression of) ATP-citrate lyase (e.g., from N. crassa ), AMP deaminase (e.g., from S. cerevisiae ), and/or malic enzyme (e.g., from M. circinelloides ). In other embodiments, Candida utilis and Phaffia rhodozyma can be similarly modified. Modified S. cerevisiae, C. utilis , and P. rhodozyma strains can be further modified as described herein to increase production of one or more carotenoids. In certain embodiments, host cells are engineered to be olegaginous by introducing one or more oleaginic polypeptides. In general, any oleaginic polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such oleaginic polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, an oleaginic polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal oleaginic polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica olegainic polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae olegainic polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal olegainic polypeptides is introduced into the Y. lipolytica host cell. Engineering Carotenoid Production Carotenoids are synthesized from isoprenoid precursors, some of which are also involved in the production of steroids and sterols. The most common isoprenoid biosynthesis pathway, sometimes referred to as the “mevalonate pathway”, is generally depicted in FIG. 3 . As shown, acetyl-CoA is converted, via hydroxymethylglutaryl-CoA (HMG-CoA), into mevalonate. Mevalonate is then phosphorylated and converted into the five-carbon compound isopentenyl pyrophosphate (IPP). Following isomerization of IPP into dimethylallyl pyrophosphate (DMAPP), three sequential condensation reactions with additional molecules of IPP generate the ten-carbon molecule geranyl pyrophosphate (GPP), followed by the fifteen-carbon molecule farnesyl pyrophosphate (FPP), and finally the twenty-carbon compound geranylgeranyl pyrophosphate (GGPP). An alternative isoprenoid biosynthesis pathway, that is utilized by some organisms (particularly bacteria) and is sometimes called the “mevalonate-independent pathway”, is depicted in FIG. 4 . This pathway is initiated by the synthesis of 1-deoxy-D-xyloglucose-5-phosphate (DOXP) from pyruvate and glyceraldehyde-3-phosphate. DOXP is then converted, via a series of reactions shown in FIG. 4 , into IPP, which isomerizes into DMAPP and is then converted, via GPP and FPP, into GGPP as shown in FIG. 3 and discussed above. Various proteins involved in isoprenoid biosynthesis have been identified and characterized in a number of organisms. Moreover, various aspects of the isoprenoid biosynthesis pathway are conserved throughout the fungal, bacterial, plant and animal kingdoms. For example, polypeptides corresponding to the acetoacetyl-CoA thiolase, HMG-CoA synthase, HMG-CoA reductase, mevalonate kinase, phosphomevalonate kinase, mevalonate pyrophosphate decarboxylase, IPP isomerase, FPP synthase, and GGPP synthase shown in FIG. 3 have been identified in and isolated from a wide variety of organisms and cells. Representative examples of a wide variety of such polypeptides are provided in Tables 7-15. One or more of the polypeptides selected from those provided in any one of Tables 7-15 may be utilized or derived for use in the methods and compositions in accordance with the present invention. Alternatively or additionally, modified mevalonate kinase polypeptides that exhibit decreased feedback inhibition properties (e.g. to farnesyl pyrophosphate (FPP)) may be utilized in accordance with the present invention. Such modified mevalonate kinase polypeptides may be of eukaryotic or prokaryotic origin. For example, modified versions of mevalonate kinase polypeptides from animals (including humans), plants, algae, fungi (including yeast), and/or bacteria may be employed; for instance, modified versions of mevalonate kinase polypeptides disclosed in Table 10 herein may be utilized. Particular examples of modified mevalonate kinase polypeptides include “feedback-resistant mevalonate kinases” disclosed in PCT Application WO 2006/063752. Thus, for example, a modified mevalonate kinase polypeptide may include one or more mutation (s) at one or more amino acid position (s) selected from the group consisting of amino acid positions corresponding to positions 17, 47, 93, 94, 132, 167, 169, 204, and 266 of the amino acid sequence of Paracoccus zeaxanthinifaciens mevalonate kinase as shown in SEQ ID NO: 1 of PCT Application WO 2004/111214. For example, the modified mevalonate kinase polypeptide may contain one or more substitutions at positions corresponding to one or more of I17T, G47D, K93E, V94I, R204H and C266S. To give but a few specific examples, when a modified mevalonate kinase polypeptide comprises 2 amino acid changes as compared with a parent mevalonate kinase polypeptide, it may comprise changes at positions corresponding to the following positions 132/375, 167/169, 17/47 and/or 17/93 of SEQ ID NO: 1 of WO/2004/111214 (e.g. P132A/P375R, R167W/K169Q, I17T/G47D or I17T/K93E); when a modified mevalonate kinase polypeptide comprises 3 amino acid changes as compared with a parent mevalonate kinase, it may comprise changes at positions corresponding to the following positions 17/167/169, 17/132/375, 93/132/375, and/or 17/47/93 of SEQ ID NO: 1 of WO/2004/111214 (e.g., I17T/R167W/K169Q, I17T/P132A/P375R, K93E/P132A/P375R, I17T/R167W/K169H, I17T/R167T/K169M, I17T/R167T/K169Y, I17T/R167F/K169Q, I17T/R167I/K169N, I17T/R167H/K169Y, I17T/G47D/K93E or I17T/G47D/K93Q). Thus, for example, a modified mevalonate kinase polypeptide may include one or more mutation(s) (particularly substitutions), as compared with a parent mevalonate kinase polypeptide, at one or more amino acid position (s) selected from the group consisting of amino acid positions corresponding to positions 55, 59, 66, 83, 106, 111, 117, 142, 152, 158, 218, 231, 249, 367 and 375 of the amino acid sequence of Saccharomyces cerevisiae mevalonate kinase as shown in SEQ ID NO: 1 of PCT application WO 2006/063752. For example, such corresponding substitutions may comprise one or more of P55L, F59S, N66K, C117S, or I152M. A modified mevalonate kinase may comprise a substitution corresponding to F59S substitution. A modified mevalonate kinase polypeptide comprising 2 amino acid changes as compared with its parent mevalonate kinase polypeptide may, for example, comprise changes at positions corresponding to the following positions 55/117, 66/152, 83/249, 111/375 or 106/218 of to SEQ ID NO: 1 of WO2006/063752 (e.g. P55L/C117S, N66K/I152M, K83E/S249P, H111N/K375N or L106P/S218P). A modified mevalonate kinase may comprise a substitution corresponding to N66K/I152M. A modified mevalonate kinase polypeptide comprising 4 amino acid changes as compared with its parent mevalonate kinase polypeptide may have changes at positions corresponding to one or more of the following positions 42/158/231/367 of SEQ ID NO:1 of WO2006/063752 (e.g. I142N/L158S/L231I/T367S). According to the present invention, carotenoid production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in isoprenoid biosynthesis. In some embodiments, such modification involves introduction of one or more heterologous isoprenoid biosynthesis polypeptides into the host cell; alternatively or additionally, modifications may be made to the expression or activity of one or more endogenous or heterologous isoprenoid biosynthesis polypeptides. Given the considerable conservation of components of the isoprenoid biosynthesis polypeptides, it is expected that heterologous isoprenoid biosynthesis polypeptides will often function even in significantly divergent organisms. Furthermore, should it be desirable to introduce more than one heterologous isoprenoid biosynthesis polypeptide (e.g., more than one version of the same polypeptide and/or more that one different polypeptides), in many cases polypeptides from different source organisms will function together. In some embodiments of the invention, a plurality of different heterologous isoprenoid biosynthesis polypeptides is introduced into the same host cell. In some embodiments, this plurality contains only polypeptides from the same source organism (e.g., two or more sequences of, or sequences derived from, the same source organism); in other embodiments the plurality includes polypeptides independently selected from from different source organisms (e.g., two or more sequences of, or sequences derived from, at least two independent source organisms). In some embodiments of the present invention that utilize heterologous isoprenoid biosynthesis polypeptides, the source organisms include, but are not limited to, fungi of the genera Blakeslea, Candida, Cryptococcus, Cunninghamella, Lipomyces, Mortierella, Mucor, Phycomyces, Pythium, Rhodosporidium, Rhodotorula, Trichosporon, Yarrowia, Aspergillus, Botrytis, Cercospora, Fusarium ( Gibberella ), Kluyveromyces, Neurospora, Penicillium, Pichia ( Hansenula ), Puccinia, Saccharomyces, Schizosaccharomyces, Sclerotium, Trichoderms, Ustilago , and Xanthophyllomyces ( Phaffia ). In certain embodiments, the source organisms are of a species including, but not limited to, Cryptococcus neoformans, Fusarium fujikuroi, Kluyveromyces lactis, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Ustilago maydis , and Yarrowia lipolytica. As noted above, the isoprenoid biosynthesis pathway is also involved in the production of non-carotenoid compounds, such as sterols, steroids, and vitamins, such as vitamin E or vitamin K. Proteins that act on isoprenoid biosynthesis pathway intermediates, and divert them into biosynthesis of non-carotenoid compounds are therefore indirect inhibitors of carotenoid biosynthesis (see, for example, FIG. 5 , which illustrates points at which isoprenoid intermediates are channeled into other biosynthesis pathways). Such proteins are therefore considered isoprenoid biosynthesis competitor polypeptides. Reductions of the level or activity of such isoprenoid biosynthesis competitor polypeptides are expected to increase carotenoid production in host cells according to the present invention. Additionally or alternatively, since disruption of the SAGA complex component SPT-8 increases carotenoid production (see e.g., Example 16), increased expression or activity of one or more components of the SAGA complex such as, without limitation, the SPT8 gene, may decrease production of carotenoids and/or retinolic compounds. Thus, polypeptides that comprise the SAGA complex can be considered competitor polypeptides in the situation where they decrease production of carotenoids and/or retinolic compounds. Without wishing to be bound by theory, the present invention encompasses the recognition that increased expression or activity of one or more components of the SAGA complex may act as isoprenoid biosynthesis competitors, thus reducing the amount of carotenoid produced. For example, one or more components of the SAGA complex may act on isoprenoid intermediates prior to GGPP, such that less GGPP is generated and available for the carotenoid generation pathway. In such embodiments, it will be understood that the SAGA polypeptide(s) components whose activity or expression is increased functions as isoprenoid biosynthesis competitor polypeptide(s). Thus, for example, one or more of the polypeptides encoded by the genes listed in Table 69 may function as isoprenoid biosynthesis competitor polypeptides. Such SAGA polypeptides can be expressed individually or in combination with one another. In certain embodiments, SAGA isoprenoid biosynthesis competitor polypeptides are expressed (and/or their activity increased) in combination with an increase in expression and/or activity of one or more additional isoprenoid biosynthesis competitor polypeptides, such as, without limitation, those isoprenoid biosynthesis competitor polypeptides listed in Tables 7-15. In some embodiments of the present invention, production or activity of endogenous isoprenoid biosynthesis competitor polypeptides may be reduced or eliminated in host cells. In some embodiments, this reduction or elimination of the activity of an isoprenoid biosynthesis competitor polypeptide can be achieved by treatment of the host organism with small molecule inhibitors of enzymes of the ergosterol biosynthetic pathway. Enzymes of the ergosterol biosynthetic pathway include, for example, squalene synthase (Erg9), squalene epoxidase (Erg1), 2,3-oxidosqualene-lanosterol cyclase (Erg7), cytochrome P450 lanosterol 14α-demethylase (Erg11), C-14 sterol reductase (Erg24), C-4 sterol methyl oxidase (Erg25), SAM:C-24 sterol methyltransferase (Erg6), C-8 sterol isomerase (Erg2), C-5 sterol desaturase (Erg3), C-22 sterol desaturase (Erg5), and C-24 sterol reductase (Erg4) polypeptides. Each of these enzymes is considered an isoprenoid biosynthesis competitor polypeptide. Regulators of these enzymes may also be considered isoprenoid biosynthesis competitor polypeptides (e.g., the yeast proteins Sut1 (Genbank Accession JC4374 GI:2133159) and Mot3 (Genbank Accession NP — 013786 GI:6323715), which may or may not have homologs in other organisms. In other embodiments, reduction or elimination of the activity of an isoprenoid biosynthesis competitor polypeptide can be achieved by decreasing activity of the ubiquinone biosynthetic pathway. The commitment step in ubiquinone biosynthesis is the formation of para-hydroxybenzoate (PHB) from tyrosine or phenylalanine in mammals or chorismate in bacteria, followed by condensation of PHB and isoprene precursor, resulting in addition of the prenyl group. This reaction is catalyzed by PHB-polyprenyltransferase. The isoprenoid side chain of ubiquinone, which can be of varying length in different organisms, is determined by the prenyldiphosphate synthase enzyme. In organisms that produce the coenzyme Q10 form of ubiquinone, the 3-decaprenyl-4-hydroxybenzoic acid resulting from the condensation of PHB and decaprenyldiphosphate reaction undergoes further modifications, which include hydroxylation, methylation and decarboxylation, in order to form ubiquinone (CoQ10). Thus, reducing the activity of prenyldiphosphate synthase leading from farnesyldiphosphate to extended isoprenoids, or reducing the activity of PHB polyprenyltransferase may be useful in increasing the amount of isoprenoid available for carotenoid biosynthesis. (Examples of prenyldiphosphate synthase and PHB-polyprenyltransferase enzymes are depicted in Tables 29 and 30, respectively). Known small molecule inhibitors of isoprenoid biosynthesis competitor enzymes include, but are not limited to, zaragosic acid (including analogs thereof such as TAN1607A (Biochem Biophys Res Commun 1996 Feb. 15; 219(2):515-520)), RPR 107393 (3-hydroxy-3-[4-(quinolin-6-yl)phenyl]-1-azabicyclo[2-2-2]octane dihydrochloride; J Pharmacol Exp Ther. 1997 May; 281(2):746-52), ER-28448 (5-{N-[2-butenyl-3-(2-methoxyphenyl)]-N-methylamino}-1,1-penthylidenebis(phosphonic acid) trisodium salt; Journal of Lipid Research, Vol. 41, 1136-1144, July 2000), BMS-188494 (The Journal of Clinical Pharmacology, 1998; 38:1116-1121), TAK-475 (1-[2-[(3R,5S)-1-(3-acetoxy-2,2-dimethylpropyl)-7-chloro-1,2,3,5-tetrahydro-2-oxo-5-(2,3-dimethoxyphenyl)-4,1-benzoxazepine-3-yl]acetyl]piperidin-4-acetic acid; Eur J. Pharmacol. 2003 Apr. 11; 466(1-2):155-61), YM-53601 ((E)-2-[2-fluoro-2-(quinuclidin-3-ylidene)ethoxy]-9H-carbazole monohydrochloride; Br J Pharmacol. 2000 September; 131(1):63-70), or squalestatin I that inhibit squalene synthase; terbinafine (e.g., LAMISIL®), naftifine (NAFTIN®), S-allylcysteine, garlic, resveratrol, NB-598 (e.g., from Banyu Pharmaceutical Co), and/or green tea phenols that inhibit squalene epoxidase (see, for example, J. Biol Chem 265:18075, 1990 ; Biochem. Biophys. Res. Commun. 268:767, 2000); various azoles that inhibit cytochrome P450 lanosterol 14α-demethylase; and fenpropimorph that inhibits the C-14 sterol reductase and the C-8 sterol isomerase. In other embodiments, heterologous isoprenoid biosynthesis competitor polypeptides may be utilized (whether functional or non-functional; in some embodiments, dominant negative mutants are employed). One particular isoprenoid biosynthesis competitor polypeptide useful according to the present invention is squalene synthase which has been identified and characterized from a variety of organisms; representative examples of squalene synthase polypeptide sequences are included in Table 16. In some embodiments of the invention that utilize squalene synthase (or modifications of squalene synthase) source organisms include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), Aspergillus niger, Saccharomyces cerevisiae, Mucor circinelloides, Rhotorula glutinis, Candida utilis, Mortierella alpina , and Yarrowia lipolytica. The carotenoid biosynthesis pathway branches off from the isoprenoid biosynthesis pathway at the point where GGPP is formed. The commitment step in carotenoid biosynthesis is the formation of phytoene by the head-to-head condensation of two molecules of GGPP, catalyzed by phytoene synthase (often called crtB; see FIG. 6 ). A series of dehydrogenation reactions, each of which increases the number of conjugated double bonds by two, converts phytoene into lycopene via neurosporene. The pathway branches at various points, both before and after lycopene production, so that a wide range of carotenoids can be generated. For example, action of a cyclase enzyme on lycopene generates γ-carotene; action of a desaturase instead produces 3,4-didehydrolycopene. γ-carotene is converted to β-carotene through the action of a cyclase. β-carotene can be processed into any of a number of products (see, for example, FIG. 6C ), including astaxanthin (via echinenone, hydroxyechinenone, and phoenicoxanthin). According to the present invention, carotenoid production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in carotenoid biosynthesis. As indicated, in some embodiments, it will be desirable to utilize as host cells organisms that naturally produce one or more carotenoids. In some such cases, the focus will be on increasing production of a naturally-produced carotenoid, for example by increasing the level and/or activity of one or more proteins involved in the synthesis of that carotenoid and/or by decreasing the level or activity of one or more proteins involved in a competing biosynthetic pathway. Alternatively or additionally, in some embodiments it will be desirable to generate production of one or more carotenoids not naturally produced by the host cell. According to some embodiments of the invention, it will be desirable to introduce one or more heterologous carotenogenic polypeptides into a host cell. As will be apparent to those of ordinary skill in the art, any of a variety of heterologous polypeptides may be employed; selection will consider, for instance, the particular carotenoid whose production is to be enhanced. The present invention contemplates not only introduction of heterologous carotenogenic polypeptides, but also adjustment of expression or activity levels of heterologous or endogenous carotenogenic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous carotenogenic); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., carotenogenic polypeptide(s)). For example, promoters including, but not limited to those described herein, such as Tef1, Gpd1 promoters can be used in conjunction with endogenous genes and/or heterologous genes for modification of expression patterns of endogenous carotenogenic polypeptide(s) and/or heterologous carotenogenic polypeptide(s). Similarly, exemplary terminator sequences include, but are not limited to, use of Y. lipolytica XPR2 terminator sequences. As indicated in FIG. 6 and in the literature, proteins involved in carotenoid biosynthesis include, but are not limited to, phytoene synthase, phytoene dehydrogenase, lycopene cyclase, carotenoid ketolase, carotenoid hydroxylase, astaxanthin synthase (a single multifunctional enzyme found in some source organisms that typically has both ketolase and hydroxylase activities), carotenoid epsilon hydroxylase, lycopene cyclase (beta and epsilon subunits), carotenoid glucosyltransferase, and acyl CoA:diacyglycerol acyltransferase. Representative example sequences for these carotenoid biosynthesis polypeptides are provided in Tables 17a-25. Alternatively or additionally, modified carotenoid ketolase polypeptides that exhibit improved carotenoid production activity may be utilized in accordance with the present invention. For example, carotenoid ketolase polypeptides comprising one more mutations to corresponding to those identified Sphingomonas sp. DC18 which exhibited improved astaxanthin production (Tao et al. 2006 Metab Eng. 2006 Jun. 27) and Paracoccus sp. strain N81106 which exhibited altered carotenoid production (Ye et al. 2006 Appl Environ Microbiol 72:5829-37). Xanthophylls can be distinguished from other carotenoids by the presence of oxygen containing functional groups on their cyclic end groups. For instance, lutein and zeaxanthin contain a single hydroxyl group on each of their terminal ring structures, while astaxanthin contains both a keto group and a hydroxyl on each terminal ring. This property makes xanthophylls more polar than carotenes such as beta-carotene and lycopene, and thus dramatically reduces their solubility in fats and lipids. Naturally occurring xanthophylls are often found as esters of the terminal hydroxyl groups, both mono- and diesters of fatty acids. They also occur as glucosides in certain species of bacteria. The solubility and dispersibility of xanthophylls can be greatly modified by the addition of ester moieties, and it is known that esterification can also affect the absorbability and/or bioavailability of a given carotenoid. It is an objective of this invention to maximize the amount of a particular xanthophyll accumulating within the intracellular triacylglyceride fraction of oleaginous yeasts, and one mechanism for achieving this goal is to increase the hydrophobic nature of the xanthophyll product that accumulates. One way of achieving this is to engineer the production of fatty-acyl mono- and/or diesters of the target xanthophyll compound. A variety of enzymes can function to esterify carotenoids. For example, carotenoid glucosyltransferases have been identified in several bacterial species (see, e.g., Table 24). In addition, acyl CoA:diacyglycerol acyltransferase (DGAT) and acyl CoA:monoacylglycerol acyltransferases (MGAT), which function in the final steps of triacylglycerol biosynthesis, are likely to serve an additional role in the esterification of xanthophylls. Representative DGAT polypeptides are shown in Table 25. Furthermore, other enzymes may specifically modify carotenoids and molecules of similar structure (e.g. sterols) and be available for modification and ester production. In some embodiments of the invention, potential source organisms for carotenoid biosynthesis polypeptides include, but are not limited to, genera of naturally oleaginous or non-oleaginous fungi that naturally produce carotenoids. These include, but are not limited to, Botrytis, Cercospora, Fusarium ( Gibberella ), Mucor, Neurospora, Phycomyces, Puccina, Rhodotorula, Sclerotium, Trichoderma , and Xanthophyllomyces . Exemplary species include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), Mucor circinelloides , and Rhodotorula glutinis . Of course, carotenoids are produced by a wide range of diverse organisms such as plants, algae, yeast, fungi, bacteria, cyanobacteria, etc. Any such organisms may be source organisms for carotenoid biosynthesis polypeptides according to the present invention. In certain embodiments of the invention, carotenoid production in a host organism may be adjusted by modifying the activity of one or more endogenous genes that affect carotenoid biosynthesis. For example, as shown in Example 16, disruption of the endogenous SPT8 gene (YALI0E23804g) in Yarrowia lipolytica results in increased carotenoid production. SPT8 functions as part of the SAGA histone acetyltransferase complex, which is required for normal expression of some fungal genes and is thought to function as a coactivator complex in a multistep pathway leading to gene activation. Thus, without wishing to be bound by theory, the present invention encompasses the recognition that alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex result in increased carotenoid production. Additionally, it will be appreciated by those of ordinary skill in the art that by increasing production of carotenoid(s) in a host organism by altering the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex, production of a retinolic compound(s) in a host organism able to utilize such a carotenoid(s) as a substrate may also be increased since more of the cartenoid substrate will be available. In Saccharomyces cerevisiae , the SAGA complex is a 1.8-MDa complex comprising a variety of components including distinct classes of transcription factors, such as Ada proteins (Ada1p, Ada2p, Ngg1p/Ada3p, and Ada4p/Gcn5p), TATA-binding protein (TBP)-related SPT proteins (Spt3p, Spt7p, Spt8p, and Spt20p/Ada5p), and TBP-associated factors or (TAFIIs) (TAFII90, TAFII68/61, TAFII60, TAFII25/23, and TAFII17). The SAGA complex also comprises the DNA-dependent protein kinase related molecule Tra1p, acetyltransferase and ubiquitin protease activities. The SAGA complex core comprises Ada and Spt subunits, a subset of Tafs, acetyltransferase and ubiquitin protease activities, the essential factor Tra1p, and two factors related to TBP function, Spt3 and Spt8. Several components of the Saccharomyces cerevisiae SAGA complex and their corresponding Yarrowia lipolytica homologs, are listed in Table 69. Each of these SAGA complex components is encompassed by the recombinant fungal strains, methods and compositions of the present invention. Those of ordinary skill in the art will be aware of these and other SAGA components, and will be able to modify such components in accordance with the present invention. Certain SAGA components are essential. For example, in Saccharomyces cerevisiae , the TRA1 gene is essential. Thus, in certain embodiments, production of a carotenoid is increased by altering expression and/or activity of the TRA1 such that the host organism remains viable. For example, the expression and/or activity of the TRA1 gene or gene product may be decreased to a level below the expression and/or activity of wild type TRA1, but not to such an extent as to result in lethality. Those of ordinary skill in the art will be aware of tra1 mutations that result in decreased expression and/or activity but that do not result in lethality. Furthermore, it will be within the capability of one of ordinary skill in the art to identify such mutations without undue experimentation, for example by employing standard mutatgenesis/screening techniques. In certain embodiments of the present invention, production of one or more carotenoids is increased by alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in one or more of the following host organisms: Aspergillus, Blakeslea, Botrytis, Candida, Cercospora, Cryptococcus, Cunninghamella, Fusarium ( Gibberella ), Kluyveromyces, Lipomyces, Mortierella, Mucor, Neurospora, Penicillium, Phycomyces, Pichia ( Hansenula ), Puccinia, Pythium, Rhodosporidium, Rhodotorula, Saccharomyces, Sclerotium, Trichoderma, Trichosporon, Xanthophyllomyces ( Phaffia ), and Yarrowia ; or is a species selected from the group consisting of: Aspergillus terreus, Aspergillus nidulans, Aspergillus niger, Blakeslea trispora, Botrytis cinerea, Candida japonica, Candida pulcherrima, Candida revkaufi, Candida tropicalis, Candida utilis, Cercospora nicotianae, Cryptococcus curvatus, Cunninghamella echinulata, Cunninghamella elegans, Fusarium fujikuroi ( Gibberella zeae ), Kluyveromyces lactis, Lipomyces starkeyi, Lipomyces lipoferus, Mortierella alpina, Mortierella ramanniana, Mortierella isabellina, Mortierella vinacea, Mucor circinelloides, Neurospora crassa, Phycomyces blakesleanus, Pichia pastoris, Puccinia distincta, Pythium irregulare, Rhodosporidium toruloides, Rhodotorula glutinis, Rhodotorula graminis, Rhodotorula mucilaginosa, Rhodotorula pinicola, Rhodotorula gracilis, Saccharomyces cerevisiae, Sclerotium rolfsii, Trichoderma reesei, Trichosporon cutaneum, Trichosporon pullans, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), and/or Yarrowia lipolytica. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism, in combination with one or more additional carotenogenic modifications as described herein. For example, such one or more additional carotenogenic modifications may comprise heterologous expression of one or more carotenogenic polypeptides, isoprenoid biosynthesis polypeptides, carotenoid biosynthesis polypeptides, etc. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism, in combination with one or more oleaginic modifications, as described herein. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism that is not naturally oleaginous. In certain embodiments, production of one or more carotenoids is increased by altering expression and/or activity of one or more components of the SAGA histone acetyltransferase complex in a host organism that is naturally oleaginous. It will be appreciated that the particular carotenogenic modification to be applied to a host cell in accordance with the present invention will be influenced by which carotenoid(s) is desired to be produced. For example, isoprenoid biosynthesis polypeptides are relevant to the production of most carotenoids. Carotenoid biosynthesis polypeptides are also broadly relevant. Carotenoid ketolase activity is particularly relevant for production of canthaxanthin, as carotenoid hydroxylase activity is for production of lutein and zeaxanthin, among others. Both carotenoid hydroxylase and ketolase activities (and astaxanthin synthase) are particularly useful for production of astaxanthin. In certain embodiments, host cells are engineered to produce carotenoids by introducing one or more carotenoid biosynthesis polypeptides. In general, any carotenoid biosynthesis polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such carotenoid biosynthesis polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, a carotenoid biosynthesis polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal carotenoid biosynthesis polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica carotenoid biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae carotenoid biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal carotenoid biosynthesis polypeptides is introduced into the Y. lipolytica host cell. Engineering Retinolic Compound Production Retinolic compounds are synthesized from certain carotenoid precursors, which are themselves synthesized from isoprenoid precursors, some of which are also involved in the production of steroids and sterols (see description under section entitled “Engineering Carotenoid Production”). Thus, any carotenogenic modification that results in the increased production of a carotenoid from which a retinolic compound can be produced may similarly result in an increased production of a retinolic compound. Retinolic compounds comprise retinol, retinal, and retinoic acid, which together are collectively referred to as “Vitamin A”. In certain embodiments, the retinolic compound retinol is synthesized from the carotenoid precursor beta-carotene. Other carotenoid compounds that contain at least one beta-ionone ring structure, such as alpha-carotene and beta-cryptoxanthin, can be precursor compounds for synthesis of retinolic compounds. According to the present invention, retinolic compound production in a host organism may be adjusted by modifying the expression or activity of one or more proteins involved in retinolic compound biosynthesis. As indicated, in some embodiments, it will be desirable to utilize as host cells organisms that naturally produce one or more retinolic compounds. In some such cases, the focus will be on increasing production of a naturally-produced retinolic compound, for example by increasing the level and/or activity of one or more proteins involved in the synthesis of that retinolic compound and/or by decreasing the level or activity of one or more proteins involved in a competing biosynthetic pathway. Alternatively or additionally, in some embodiments it will be desirable to generate production of one or more retinolic compounds not naturally produced by the host cell. According to some embodiments of the invention, it will be desirable to introduce one or more heterologous retinologenic polypeptides into a host cell. As will be apparent to those of ordinary skill in the art, any of a variety of heterologous polypeptides may be employed; selection will consider, for instance, the particular retinolic compound whose production is to be enhanced. The present invention contemplates not only introduction of heterologous retinologenic polypeptides, but also adjustment of expression or activity levels of heterologous retinologenic polypeptides, including, for example, alteration of constitutive or inducible expression patterns. In some embodiments of the invention, expression patterns are adjusted such that growth in nutrient-limiting conditions is not required to induce oleaginy. For example, genetic modifications comprising alteration and/or addition of regulatory sequences (e.g., promoter elements, terminator elements) may be utilized to confer particular regulation of expression patterns. Such genetic modifications may be utilized in conjunction with endogenous genes (e.g., for regulation of endogenous carotenogenic); alternatively, such genetic modifications may be included so as to confer regulation of expression of at least one heterologous polypeptide (e.g., retinologenic polypeptide(s)). For example, promoters including, but not limited to those described herein, such as Tef1, Gpd1 promoters can be used in conjunction with endogenous genes and/or heterologous genes for modification of expression patterns of endogenous retinologenic polypeptide(s) and/or heterologous retinologenic polypeptide(s). Similarly, exemplary terminator sequences include, but are not limited to, use of Y. lipolytica XPR2 terminator sequences. As indicated in FIG. 11 and in the literature, proteins involved in retinologenic biosynthesis include, but are not limited to, beta-carotene 15,15′-monooxygenase (also known as beta-carotene dioxygenase) and beta carotene retinol dehydrogenase. Representative example sequences for these retinolic compound biosynthesis polypeptides are provided in Tables 67-68. In some embodiments of the invention, potential source organisms for retinolic compound biosynthesis polypeptides include, but are not limited to, genera of naturally oleaginous or non-oleaginous fungi that naturally produce carotenoids. These include, but are not limited to, Botrytis, Cercospora, Fusarium ( Gibberella ), Mucor, Neurospora, Phycomyces, Puccina, Rhodotorula, Sclerotium, Trichoderma , and Xanthophyllomyces . Exemplary species include, but are not limited to, Neurospora crassa, Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), Mucor circinelloides , and Rhodotorula glutinis . Of course, retinolic compounds are produced by a wide range of diverse organisms such as mammals, bacteria, cyanobacteria, etc. Any such organisms may be source organisms for retinolic compound biosynthesis polypeptides according to the present invention. In certain embodiments of the invention, retinolic compound production in a host organism that is able to produce retinolic compounds from carotenoid substrates is adjusted by modifying the activity of one or more endogenous genes that affect carotenoid biosynthesis. For example, as shown in Example 16, disruption of the endogenous SPT8 gene (YALI0E23804g) in Yarrowia lipolytica results in increased carotenoid production. As will be appreciated by those of ordinary skill in the art, increasing production of a carotenoid(s) in a host organism by altering the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex will result in a greater abundance of such a carotenoid(s); hence, production of a retinolic compound(s) in a host organism able to utilize such a carotenoid(s) as a substrate may similarly be increased. Without wishing to be bound by theory, the present invention contemplates that alteration of the expression and/or activity of one or more components of the SAGA histone acetyltransferase complex may result in increased retinolic compound production. In certain embodiments, retinolic compound production is increased in a host organism by altering the expression and/or activity of one or more of: Ada proteins (Ada1p, Ada2p, Ngg1p/Ada3p, and Ada4p/Gcn5p), TATA-binding protein (TBP)-related SPT proteins (Spt3p, Spt7p, Spt8p, and Spt20p/Ada5p), TBP-associated factors or (TAFIIs) (TAFII90, TAFII68/61, TAFII60, TAFII25/23, and TAFII17), Tra1p, and/or proteins encoding the acetyltransferase and/or ubiquitin protease activities. In certain embodiments, retinolic compound production is increased in a host organism by altering the expression and/or activity of one or more polypeptides listed in Table 69. Those of ordinary skill in the art will be aware of these and other SAGA components, and will be able to modify such components in accordance with the present invention. In certain embodiments, host cells are engineered to produce retinolic compounds by introducing one or more carotenoid biosynthesis polypeptides. In general, any retinolic compound biosynthesis polypeptide can be introduced into any host cell of the present invention. In certain embodiments, such retinolic compound biosynthesis polypeptides are codon-optimized to accommodate the codon preferences of the host cell. In certain embodiments, a retinolic compound biosynthesis polypeptide introduced into a host cell is from the same organism as the host cell and/or a related organism. For example, without limitation, the present invention encompasses the recognition that it may be desirable to introduce a fungal retinolic compound biosynthesis polypeptide into a fungal host cell (e.g., from the same and/or a related fungal species). In certain embodiments, the host cell is a Y. lipolytica host cell. In certain aspects of such embodiments, a Y. lipolytica retinolic compound biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, a S. cerevisiae retinolic compound biosynthesis polypeptide is introduced into the Y. lipolytica host cell. In certain aspects, any of a variety of fungal retinolic compound biosynthesis polypeptides is introduced into the Y. lipolytica host cell. Production and Isolation of Carotenoids and/or Retinolic Compounds As discussed above, accumulation of lipid bodies in oleaginous organisms is generally induced by growing the relevant organism in the presence of excess carbon source and limiting nitrogen and/or other nutrients (eg. phosphate and magnesium). Specific conditions for inducing such accumulation have previously been established for a number of different oleaginous organisms (see, for example, Wolf (ed.) Nonconventional yeasts in biotechnology Vol. 1, Springer-Verlag, Berlin, Germany, pp. 313-338; Lipids 18(9):623, 1983 ; Indian J. Exp. Biol. 35(3):313, 1997; J. Ind. Microbiol. Biotechnol. 30(1):75, 2003 ; Bioresour Technol. 95(3):287, 2004, each of which is incorporated herein by reference in its entirety). In general, it will be desirable to cultivate inventive modified host cells under conditions that allow accumulation of at least about 20% of their dry cell weight as lipid. In other embodiments, the inventive modified host cells are grown under conditions that permit accumulation of at least about 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, or even 80% or more of their dry cell weight as lipid. In certain embodiments, the host cells utilized are cells which are naturally oleaginous, and induced to produce lipid to the desired levels. In other embodiments, the host cells are cells which naturally produce lipid, but have been engineered to increase production of lipid such that desired levels of lipid production and accumulation are achieved. In certain embodiments, the host cells of the invention are not naturally oleaginous, but have been engineered to produce lipid such that desired levels of lipid production are obtained. Those of ordinary skill in the art will appreciate that, in general, growth conditions that are effective for inducing lipid accumulation in a source organism, may well also be useful for inducing lipid accumulation in a host cell into which the source organism's oleaginic polypeptides have been introduced. Of course, modifications may be required in light of characteristics of the host cell, which modifications are within the skill of those of ordinary skill in the art. It will also be appreciated by those of ordinary skill in the art that it will often be desirable to ensure that production of the desired carotenoid and/or retinolic compound by the inventive modified host cell occurs at an appropriate time in relation to the induction of oleaginy such that the carotenoid(s) and/or retinolic compound(s) accumulate(s) in the lipid bodies. In some embodiments, it will be desirable to induce production of the carotenoid(s) and/or retinolic compound(s) in a host cell which does not naturally produce the carotenoid(s) and/or retinolic compound(s), such that detectable levels of the carotenoid(s) and/or retinolic compound(s) is/are produced. In certain aspects the host cells which do not naturally produce a certain carotenoid(s) and/or retinolic compound(s) are capable of production of other carotenoid(s) (e.g. certain host cells may, for example, naturally produce β-carotene but may not naturally produce astaxanthin) and/or retinolic compound(s), (e.g. certain host cells may, for example, naturally produce retinal but may not naturally produce retinol); in other aspects the host cells do not naturally produce any carotenoid(s) and/or retinolic compound(s). In other embodiments, it will be desirable to increase production levels of carotenoid(s) and/or retinolic compound(s) in a host cell which does naturally produce low levels of the carotenoid(s) and/or retinolic compound(s), such that increased detectable levels of the carotenoid(s) and/or retinolic compound(s) are produced. In certain aspects, the host cells which do naturally produce the carotenoid(s) (e.g., β-carotene) also produce additional carotenoid(s) (e.g., astaxanthin, etc.) and/or retinolic compound(s) (e.g., retinal); in still other aspects, the cells which naturally produce the carotenoid(s) (e.g., β-carotene) do not produce additional carotenoid(s) and/or retinolic compound(s). In certain embodiments of the invention, it will be desirable to accumulate carotenoids and/or retinolic compounds to levels (i.e., considering the total amount of all produced carotenoids and/or retinolic compounds together or considering a particular carotenoid and/or retinolic compound) that are greater than at least about 1% of the dry weight of the cells. In some embodiments, the total carotenoid and/or retinolic compound accumulation will be to a level at least about 1.5%, at least about 2%, at least about 2.5%, at least about 3%, at least about 3.5%, at least about 4%, at least about 4.5%, at least about 5%, at least about 5.5%, at least about 6%, at least about 6.5%, at least about 7%, at least about 7.5%, at least about 8%, at least about 8.5%, at least about 9%, at least about 9.5%, at least about 10%, at least about 10.5%, at least about 11%, at least about 11.5%, at least about 12%, at least about 12.5%, at least about 13%, at least about 13.5%, at least about 14%, at least about 14.5%, at least about 15%, at least about 15.5%, at least about 16%, at least about 16.5%, at least about 17%, at least about 17.5%, at least about 18%, at least about 18.5%, at least about 19%, at least about 19.5%, at least about 20% or more of the total dry weight of the cells. In some embodiments of the invention, a particular carotenoid and/or retinolic compound may not accumulate to a level as high as 1% of the total dry weight of the cells; appropriately engineered cells according to the present invention, and any lipid bodies, carotenoids and/or retinolic compounds they produce, remain within the scope of the present invention. Thus, in some embodiments, the cells accumulate a given carotenoid and/or retinolic compound to a level below about 1% of the dry weight of the cells. In some embodiments, the carotenoid and/or retinolic compound accumulates to a level below about 0.9%, 0.8%, 0.7%, 0.6%, 0.5%, 0.4%, 0.3%, 0.2%, 0.1%, 0.05%, or lower, of the dry cell weight of the cells. In some embodiments of the invention, carotenoids and/or retinolic compounds accumulate both within lipid bodies and elsewhere in the cells. In some embodiments, carotenoids and/or retinolic compounds accumulate primarily within lipid bodies. In some embodiments, carotenoids and/or retinolic compounds accumulate substantially exclusively within lipid bodies. In some embodiments, at least about 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or more of a desired produced carotenoid and/or retinolic compound accumulates in lipid bodies. In some embodiments of the invention, modified host cells are engineered to produce one or more carotenoid compound(s) and/or retinolic compound(s) characterized by negligible solubility in water (whether hot or cold) and detectable solubility in one or more oils. In some embodiments, such compounds have a solubility in oil below about 0.2%. In some embodiments, such compounds have a solubility in oil within the range of about <0.001%-0.2%. The present invention therefore provides engineered host cells (and methods of making and using them) that contain lipid bodies and that further contain one or more carotenoid compounds and/or retinolic compounds accumulated in the lipid bodies, where the compounds are characterized by a negligible solubility in water and a solubility in oil within the range of about <0.001%-0.2%; 0.004%-0.15%; 0.005-0.1%; or 0.005-0.5%. For example, in some embodiments, such compounds have a solubility in oil below about 0.15%, 0.14%, 0.13%, 0.12%, 0.11%, 0.10%. 0.09, 0.08%, 0.07%, 0.06%, 0.05%, 0.04%, 0.03%, 0.02%, 0.01%, 0.05%, or less. In some embodiments, the compounds show such solubility in an oil selected from the group consisting of sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof. Bacterial carotenogenic genes have already been demonstrated to be transferable to other organisms, and are therefore particularly useful in accordance with the present invention (see, for example, Miura et al., Appl. Environ. Microbiol. 64:1226, 1998). In other embodiments, it may be desirable to utilize genes from other source organisms such as plant, alga, or microalgae; these organisms provide a variety of potential sources for ketolase and hydroxylase polypeptides. Still additional useful source organisms include fungal, yeast, insect, protozoal, and mammalian sources of polypeptides. In some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through expression of a truncated variant of a hydroxymethylglutaryl-CoA (HMG CoA) reductase polypeptide. In some embodiments, the truncated variant is a truncated variant of a Y. lipolytica HMG CoA reductase polypeptide. According to the present invention, expression of such a truncated HMG CoA reductase polypeptide can result in increased isoprenoid and/or carotenoid production in host cells (e.g., Y. lipolytica cells). Alternatively or additionally, in some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that increase(s) level and/or activity of a polypeptide selected from the group consisting of farnesyl pyrophosphate synthase polypeptides, geranylgeranylpyrophosphate synthase polypeptides, and combinations thereof. In some embodiments, the source organism for the selected polypeptide is Y. lipolytica. Alternatively or additionally, in some embodiments of the present invention, isoprenoid production is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that decrease(s) expression or activity of an isoprenoid biosynthesis competitor polypeptide (e.g., of a squalene synthase polypeptide), for example thereby reducing diversion of one or more intermediates away from the isoprenoid and/or carotenoid biosynthesis pathways. In some embodiments, the polypeptide whose expression or activity is reduced is endogenous to the host cell. In some embodiments of the present invention, more than one carotenogenic modification is applied to the same host cell. For example, isoprenoid production may be increased in host cells (e.g., Y. lipolytica cells) through application of at least two or more carotenogenic modifications selected from the group consisting of: expression of a truncated HMG CoA reductase polypeptide, increase in expression and/or activity of farnesyl pyrophosphate synthase polypeptide, increase in expression and/or activity of a geranylgeranylpyrophosphate synthase polypeptide, decrease in expression and/or activity of a squalene synthase polypeptide, and combinations thereof. Furthermore, in some embodiments of the invention, carotenoid production (e.g., production of β-carotene) is increased in host cells (e.g., in Y. lipolytica cells) through application of one or more carotenogenic modification(s) that increase(s) expression and/or activity of a polypeptide selected from the group consisting of phytoene synthase, lycopene cyclase, phytoene dehydrogenase, and combinations thereof. In some embodiments, such increase in expression comprises introduction of one or more genes encoding heterologous polypeptides. In some embodiments, phytoene synthase and lycopene cyclase activities are provided in a single polypeptide or complex (e.g., by the Mucor circinelloides or Neurospora crassa multifunctional phytoene synthase/lycopene cyclase). In some embodiments, phytoene dehydrogenase from Mucor circinelloides or Neurospora crassa is utilized. In some embodiments, production of one or more carotenoids downstream of β-carotene (e.g., of one or more hydroxylated xanthophylls) is increased in host cells that produce β-carotene (including host cells that have been engineered to produce β-carotene, e.g., through application of one or more carotenogenic modifications as described herein) through application of one or more carotenogenic modifications that increase(s) level and/or activity of one or more carotenoid ketolase polypeptides (e.g., from Parvularcula bermudensis and/or Aurantimonase sp. SI85-9A1) to produce one or more ketone-containing carotenoids (e.g., canthaxanthin, echinenone, astaxanthin, and combinations thereof). In some embodiments, production of one or more hydroxylated carotenoids is increased in host cells that produce (including having been engineered to produce) β-carotene and/or one or more ketone-containing carotenoids though application of one or more carotenogenic modifications that increase(s) the level and/or activity of one or more carotenoid hydroxylase polypeptides (e.g., from Xanthobacter autotrophicus and/or Erythrobacter litoralis ) to increase production of one or more hydroxylated carotenoids (e.g., zeaxanthin, lutein, β-cryptoxanthin, astaxanthin, and combinations thereof). Similar approaches to enhance carotenoid production may be employed in other oleaginous or non-oleaginous host organisms (e.g. S. cerevisiae, C. utilis, P. rhodozyma ) can be undertaken, using the same, homologous, or functionally similar carotogenic polypeptides. In some embodiments, the present invention provides modified Y. lipolytica strains that have been engineered to express one or more carotenoid biosynthesis polypeptides and/or isoprenoid biosynthesis polypeptides. For example, in some embodiments, a modified Y. lipolytica strain is engineered to increase expression and/or activity of one or more of phytoene synthase, phytoene dehydrogenase, lycopene cyclase, and GGPP synthase, and/or to decrease expression and/or activity of squalene synthase. In some embodiments, a modified Y. lipolytica strain is engineered to express all of these polypeptides. Such a modified Y. lipolytica strain produces β-carotene (see, for example, Example 2). In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express a truncated HMG CoA reductase; in some such embodiments, the strains are engineered so that expression of the truncated HMG CoA reductase increases β-carotene several fold (for example, 3-4 fold or more). In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express a beta-carotene 15,15′-monooxygenase and/or a retinol dehydrogenase to increase retinolic compound production. In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce β-carotene are further engineered to express carotenoid hydroxylase (to achieve production of zeaxanthin and/or β-cryptoxanthin), carotenoid ketolase (to achieve production of canthaxanthin and/or echinenone), or both (to achieve production of astaxanthin). In some embodiments, inventive modified Y. lipolytica strains that have been engineered to produce, for example, β-carotene, zeaxanthin, canthaxanthin, echinenone, and/or astaxanthin are also engineered to have increased expression of, for example, malic enzyme, mevalonate kinase, etc. It will be appreciated that, in some embodiments of the invention, it may be desirable to engineer a particular host cell by expressing more than one version of a given polypeptide (e.g., isoprenoid biosynthesis polypeptide, carotenoid biosynthesis polypeptide, oleaginic polypeptide, isoprenoid biosynthesis competitor polypeptides, retinolic compound biosynthesis polypeptide, etc.). For example, a given host cell may be engineered to express versions of a given polypeptide from two or more different sources. Where a particular enzyme may be comprised of more than one polypeptide chains, it will often be desirable to utilize all chains from a single source, although this is not required so long as activity is achieved. Also, whenever a host cell is engineered to express a polypeptide from a different source, it may be desirable to alter the gene sequence encoding the polypeptide to account for codon preferences of the host cell. To give but a few specific examples, the present invention provides modified Y. lipolytica strains that have been engineered to express the phytoene synthase/lycopene cyclase bifunctional (carB) polypeptide from M. circinelloides (see, for example, Example 1B), and also to express the phytoene dehydrogenase (carRP) polypeptide from M. circinelloides (see, for example, Example 1A). In some embodiments, the present invention provides such carB+carRP-expressing Y. lipolytica strains that have been engineered to modify expression and/or activity of a truncated HMG-CoA reductase polypeptide from Y. lipolytica and/or one or more Y. lipolytica polypeptides selected from the group consisting of GGPP synthase, FPP synthase (Erg20), IPP isomerase (IDI), HMG synthase (Erg13), mevalonate kinase (Erg12), squalene synthase (Erg9), phosphimevalonate kinase (Erg8), mevalonate pyrophosphate decarboxylase (MVD1), malic enzyme, malate dehydrogenase, glucose 6 phosphate dehydrogenase, malate dehydrogenase homolog 2,6-phosphogluconate dehydrogenase (GND1), isocitrate dehydrogenase, fructose 1,6 bisphosphatase, acetoacetyl CoA thiolase (Erg10), ATP citrate lyase subunit 1, ATP citrate lyase subunit 2, and combinations thereof. The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce β-carotene. The present invention also specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide, and in some embodiments more than one, for example from a source selected from the group consisting of Parvularcula bermudensis (see, for example, Example 1H), Aurantimonas (see, for example, Example 1G), and/or an environmental isolate identified from the Sargasso Sea (see, for example, Example 1F). The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce canthaxanthin, astaxanthin, and/or echinenone. The present invention further specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid hydroxylase (e.g., crtZ) polypeptide, and in some embodiments more than one, from Erythrobacter litoralis (see, for example, Examples 1J and 1L), Novosphingobium aromaticivarans (see, for example, Example 1E), Parvularcula bermudensis (see, for example, Example 1I), Xanthobacter autotrophicus (see, for example, Example 1O), Sphingopyxis alaskensis (see, for example, Example 1M), Chlamydomonas rheinhardtii, Erythrobacter longus, Robiginitalea biformata (see, or example, Example 1N) and/or Pseudomonas putida (see, for example, Example 1P). The present invention therefore specifically provides Y. lipolytica strains that have been engineered to produce zeaxanthin, lutein, β-cryptoxanthin, and/or astaxanthin. The present invention further specifically provides modified Y. lipolytica strains that have been engineered to express at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide in combination with at least one carotenoid hydroxylase (e.g., crtZ) polypeptide. In certain embodiments, the at least one carotenoid ketolatse polypeptide and at least one carotenoid hydroxylase polypeptide are encoded by nucleic acid sequences present in separate nucleic acid molecules. In certain embodiments, the at least one carotenoid ketolatse polypeptide and at least one carotenoid hydroxylase polypeptide are encoded by nucleic acid sequences present in the same nucleic acid molecule. For example, a host organism may be transformed or transfected with a single expression vector, which expression vector comprises both a carotenoid ketolatse polypeptide and a carotenoid hydroxylase polypeptide, each of which comprises sequences sufficient to direct their expression in the host organism. In certain embodiments, the at least one carotenoid ketolase (e.g., crtO/crtW) polypeptide and the at least one carotenoid hydroxylase (e.g., crtZ) polypeptide are expressed as a fusion protein. A representative example of such embodiments is presented in Example 17. In certain embodiments, such a fusion polypeptide is designed such that the carotenoid ketolatse polypeptide is positioned N-terminal to the carotenoid hydroxylase polypeptide. In certain embodiments, such a fusion polypeptide is designed such that the carotenoid ketolatse polypeptide is positioned C-terminal to the carotenoid hydroxylase polypeptide. In embodiments in which the carotenoid ketolatse polypeptide and the carotenoid hydroxylase polypeptide are expressed concurrently (whether from separate nucleic acid molecules or from the same nucleic acid molecule), the polypeptides may be selected from any of a variety of source organisms. As non-limiting examples, the carotenoid hydroxylase polypeptide may be selected from an organism such as Erythrobacter litoralis (see, for example, Examples 1J and 1L), Novosphingobium aromaticivarans (see, for example, Example 1E), Parvularcula bermudensis (see, for example, Example 1I), Xanthobacter autotrophicus (see, for example, Example 1O), Sphingopyxis alaskensis (see, for example, Example 1M), Chlamydomonas rheinhardtii, Erythrobacter longus, Robiginitalea biformata (see, or example, Example 1N) and/or Pseudomonas putida (see, for example, Example 1P). As further non-limiting examples, the carotenoid ketolase polypeptide may be selected from an organism such as Parvularcula bermudensis (see, for example, Example 1H), Aurantimonas (see, for example, Example 1G), and/or an environmental isolate identified from the Sargasso Sea (see, for example, Example 1F). It should be noted that, for inventive organisms that produce more than one carotenoid, it will sometimes be possible to adjust the relative amounts of individual carotenoids produced by adjusting growth conditions. For example, it has been reported that controlling the concentration of dissolved oxygen in a culture during cultivation can regulate relative production levels of certain carotenoids such as β-carotene, echinenone, β-cryptoxanthin, 3-hydroxyechinenone, asteroidenone, canthaxanthin, zeaxanthin, adonirubin, adonixanthin and astaxanthin (see, for example, U.S. Pat. No. 6,825,002 to Tsubokura et al., the entire contents of which are incorporated herein by reference). Additionally or alternatively, the present invention encompasses the recognition that controlling the pH in a culture during cultivation can regulate relative production levels of these and/or other carotenoids (see e.g., Example 18). Particularly for embodiments of the present invention directed toward production of astaxanthin, it will often be desirable to utilize one or more genes from a natural astaxanthin-producing organism. Where multiple heterologous polypeptides are to be expressed, it may be desirable to utilize the same source organism for all, or to utilize closely related source organisms. Inventive modified cells, that have been engineered to produce carotenoids and/or to accumulate lipid (including to be oleaginous), can be cultured under conditions that achieve carotenoid production and/or oleaginy. In some embodiments, it will be desirable to control growth conditions so in order to maximize production of a particular carotenoid or set of carotenoids (including all carotenoids) and/or to optimize accumulation of the particular carotenoid(s) in lipid bodies. In some embodiments it will be desirable to control growth conditions to adjust the relative amounts of different carotenoid products produced. Inventive modified cells, that have been engineered to produce retinolic compounds and/or to accumulate lipid (including to be oleaginous), can be cultured under conditions that achieve retinolic compound production and/or oleaginy. In some embodiments, it will be desirable to control growth conditions so in order to maximize production of a particular retinolic compound or set of retinolic compounds (including all retinolic compounds) and/or to optimize accumulation of the particular retinolic compound (s) in lipid bodies. In some embodiments it will be desirable to control growth conditions to adjust the relative amounts of different retinolic compound products produced. In some embodiments, it will be desirable to limit accumulation of a particular intermediate, for example ensuring that substantially all of a particular intermediate compound is converted so that accumulation is limited. For example, particularly in situations where a downstream enzyme may be less efficient than an upstream enzyme and it is desirable to limit accumulation of the product of the upstream enzyme (e.g., to avoid its being metabolized via a competitive pathway and/or converted into an undesirable product), it may be desirable to grow cells under conditions that control (e.g., slow) activity of the upstream enzyme so that the downstream enzyme can keep pace. Those of ordinary skill in the art will appreciate that any of a variety of growth parameters, including for example amount of a particular nutrient, pH, temperature, pressure, oxygen concentration, timing of feeds, content of feeds, etc can be adjusted as is known in the art to control growth conditions as desired. To give but a few examples, in some embodiments, growth and/or metabolism is/are limited by limiting the amount of biomass accumulation. For example, growth and/or metabolism can be limited by growing cells under conditions that are limiting for a selected nutrient. The selected limiting nutrient can then be added in a regulated fashion, as desired. In some embodiments, the limiting nutrient is carbon, nitrogen (e.g., via limiting ammonium or protein), phosphate, magnesium, one or more trace metals, or combinations thereof. In some embodiments, the limiting nutrient is carbon. In some embodiments, the limiting nutrient is one or more trace metals. In some embodiments, use of a limiting nutrient can by utilized to control metabolism of a particular intermediate and/or to adjust relative production of particular carotenoid compounds and/or retinolic compounds. In some embodiments, this result can be achieved by controlling metabolism of a particular intermediate as discussed above; in some embodiments, it can be achieved, for example, by limiting progress through the carotenoid and/or retinolic compound biosynthesis pathway so that a desired carotenoid product (e.g., β-carotene, canthaxanthin, astaxanthin, etc.) or retinolic compound (e.g., retinal) is not converted to a downstream compound. To give but one example, phosphate limitation can slow the overall rate of clux through the carotenoid biosynthesis pathway and can be utilized to change the ratio of canthaxanthin to echinenone produced. In some embodiments, cells are grown in the presence of excess carbon source and limiting nitrogen, phosphate, and/or magnesium to induce oleaginy. In some embodiments cells are grown in the presence of excess carbon source and limiting nitrogen. In some embodiments, the carbon:nitrogen ratio is within the range of about 200:1, 150:1, 125:1, 100:1, 95:1, 90:1, 85:1, 80:1, 75:1, 70:1, 65:1, 60:1, 55:1, 50:1, 45:1, 40:1, 35:1, 30:1, 25:1, 20:1, 15:1, 10:1, or less. Those of ordinary skill in the art are aware of a wide variety of carbon sources, including, for example, glycerol, glucose, galactose, dextrose, any of a variety of oils (e.g., olive, canola, corn, sunflower, soybean, cottonseed, rapeseed, etc., and combinations thereof) that may be utilized in accordance with the present invention. Combinations of such may also be utilized. For example, common carbon source compositions contain oil:glucose in a ratio within the range of about 5:95 to 50:50 (e.g. about 5:95, about 10:90, about 15:85, about 20:80, about 25:75, about 30:70, about 35:65, about 40:60, about 45:55, about 50:50). Those of ordinary skill in the art are also aware of a variety of different nitrogen sources (e.g., ammonium sulfate, proline, sodium glutamate, soy acid hydrolysate, yeast extract-peptone, yeast nitrogen base, corn steep liquor, etc, and combinations thereof) that can be utilized in accordance with the present invention. In some embodiments, cultures are grown at a selected oxygen concentration (e.g., within a selected range of oxygen concentrations). In some embodiments, oxygen concentration may be varied during culture. In some embodiments, oxygen concentration may be controlled during some periods of culture and not controlled, or controlled at a different point, during others. In some embodiments, oxygen concentration is not controlled. In some embodiments, cultures are grown at an oxygen concentration within the range of about 5-30%, 5-20%, 10-25%, 10-30%, 15-25%, 15-30%, including at about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, or more. In some embodiments, oxygen concentration is maintained above about 20%, at least for some period of the culture. In some embodiments, cells are grown via fed-batch fermentation. In some embodiments, feed is continued until feed exhaustion and/or the feed is controlled to initiate or increase once a certain level of dissolved oxygen is detected in the culture medium (e.g., about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, or more dissolved oxygen). The feed rate can be modulated to maintain the dissolved oxygen at a specific level (e.g., about 5%, 6%, 7%, 8%, 9%, 10%, 11%, 12%, 13%, 14%, 15%, 16%, 17%, 18%, 19%, 20%, 21%, 22%, 23%, 24%, 25%, 26%, 27%, 28%, 29%, 30%, 31%, 32%, 33%, 34%, 35%, 36%, 37%, 38%, 39%, 40%, or more dissolved oxygen). In some embodiments, inventive modified cells are grown in a two-phase feeding protocol in which the first phase is designed to maintain conditions of excess carbon and limiting oxygen, and the second phase results in conditions of excess oxygen and limiting carbon. The carbon sources in each phase can be the same (e.g., both glucose) or different (e.g., glucose then glucose-oil mixture, oil then glucose, or glucose-oil mixture then glucose). The present invention demonstrates that such conditions can achieve high levels of carotenoid production (see, for example, Example 5D). Additionally or alternatively, such conditions also result in high levels of retinolic compound production. For example, high levels of retinolic compound(s) production may be achieved by increasing the levels of a particular carotenoid that is used as a substrate for the production of such a retinolic compound(s). In some embodiments, inventive modified cells are cultivated at constant temperature (e.g., between about 20-40, or 20-30 degrees, including for example at about 20, 20.5, 21, 21.5, 22, 22.5, 23, 23.5, 24, 24.5, 25, 25.5, 26, 26.5, 27, 27.5, 28, 28.5, 29, 29.5, 30° C. or above) and/or pH (e.g., within a range of about 4-7.5, or 4-6.5, 3.5-7, 3.5-4, 4-4.5, 4.5-5, 5-5.5, 5.5-6, 6-6.5, 6.5-7, 7-7.5, 7-8, etc., including at about 4.0, 4.1, 4.2, 4.3, 4.4, 4.5, 4.6, 4.7, 4.8, 4.9, 5.0, 5.1, 5.2, 5.3, 5.4, 5.5, 5.6, 5.7, 5.8, 5.9, 6.0, 6.1, 6.2, 6.3, 6.4, 6.5, 6.6, 6.7, 6.8, 6.9, 7.0, 7.1, 7.2, 7.3, 7.4, 7.5, 7.6, 7.7, 7.8, 7.9, 8.0, 8.1, 8.2, 8.3, 8.4, 8.5 or above); in other embodiments, temperature and/or pH may be varied during the culture period, either gradually or in a stepwise fashion. For example, in some embodiments, the pH is 7.0 at inoculation and is increased to pH 8.0 during the course of the fermentation. The pH may be increased either continuously or in discrete steps. For example, in Example 19, the pH of the culture in increased continuously. In certain embodiments, the pH in increased continuously by increasing the pH at a rate of 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.010, 0.011, 0.012, 0.013, 0.014, 0.015, 0.016, 0.017, 0.018, 0.019, 0.020, 0.021, 0.022, 0.023, 0.024, 0.025, 0.026, 0.027, 0.028, 0.029, 0.030, 0.031, 0.032, 0.033, 0.034, 0.035, 0.036, 0.037, 0.038, 0.039, 0.040, 0.041, 0.042, 0.043, 0.044, 0.045, 0.046, 0.047, 0.048, 0.049, 0.050 or more units/hour. In certain embodiments, the pH in increased in discrete steps by increasing the pH by 0.001, 0.002, 0.003, 0.004, 0.005, 0.006, 0.007, 0.008, 0.009, 0.010, 0.011, 0.012, 0.013, 0.014, 0.015, 0.016, 0.017, 0.018, 0.019, 0.020, 0.021, 0.022, 0.023, 0.024, 0.025, 0.026, 0.027, 0.028, 0.029, 0.030, 0.031, 0.032, 0.033, 0.034, 0.035, 0.036, 0.037, 0.038, 0.039, 0.040, 0.041, 0.042, 0.043, 0.044, 0.045, 0.046, 0.047, 0.048, 0.049, 0.050 or more at each step. In certain embodiments, the pH is increased employing a combination of continuous increase and discrete steps. In certain embodiments, increasing the pH during the course of fermentation results in one or more beneficial effects such as, without limitation, an increase in total biomass accumulation, an increase in the percentage of biomass representing carotenoid accumulation, and, in the case of zeaxanthin production, an increase in the hydroxylation of beta-carotene to zeaxanthin. Those of ordinary skill in the art will be able to select without undue experimentation an appropriate rate of increase, an appropriate type of increase (e.g. continuous, discrete steps or a combination of the two), and/or an optimum pH within the selected range to maximize these and/or other beneficial effects. In some embodiments, the temperature at which inventive cells are cultivated is selected so that production of one or more particular carotenoid compound(s) and/or retinolic compound(s) is adjusted (e.g., so that production of one or more particular compound(s) is increased and/or production of one or more other compound(s) is decreased). In some embodiments, the temperature at which inventive cells are cultivated is selected so that the ratio of one carotenoid compound and/or retinolic compound to another, is adjusted. To give but one example, in some embodiments, a temperature is selected to be sufficiently low that β-carotene levels are reduced and the level of at least one other carotenoid compound(s) (e.g., zeaxanthin) is increased. In some embodiments, cultures are grown at about pH 5.5, at about pH 7.0, and or at a temperature between about 28-30° C. In some embodiments, it may be desirable to grow inventive modified cells under low pH conditions, in order to minimize growth of other cells. In some embodiments, it will be desirable to grow inventive modified cells under relatively higher temperature conditions in order to slow growth rate and/or increase the ultimate dry cell weight output of carotenoids and/or retinolic compounds. In some embodiments, it will be desirable to grow inventive modified cells under conditions in which the pH in increased (e.g. continuously, in discrete steps, or both) during the course of fermentation (e.g. increased from pH 7.0 to pH 8.0). In some embodiments, it will be desirable to grow inventive modified cells under two or more of these conditions. For example, inventive modified cells can be grown under relatively higher temperature conditions while simultaneously increasing the pH over the course of the fermentation. Those of ordinary skill in the art will be able to select appropriate growth conditions to achieve their experimental, production and/or other cell culture goals. One advantage provided by the present invention is that, in addition to allowing the production of high levels of carotenoids and/or retinolic compounds, certain embodiments of the present invention allow produced compounds to be readily isolated because they accumulate in the lipid bodies within oleaginous organisms. Methods and systems for isolating lipid bodies have been established for a wide variety of oleaginous organisms (see, for example, U.S. Pat. Nos. 5,164,308; 5,374,657; 5,422,247; 5,550,156; 5,583,019; 6,166,231; 6,541,049; 6,727,373; 6,750,048; and 6,812,001, each of which is incorporated herein by reference in its entirety). In brief, cells are typically recovered from culture, often by spray drying, filtering or centrifugation. Of course, it is not essential that lipid bodies be specifically isolated in order to collect carotenoid compounds and/or retinolic compounds produced according to the present invention. Any of a variety of approaches can be utilized to isolate and/or purify carotenoids and/or retinolic compounds. Many useful extraction and/or purification procedures for particular carotenoid compounds, and/or for carotenoids generally, are known in the art (see, for example, EP670306, EP719866, U.S. Pat. No. 4,439,629, U.S. Pat. No. 4,680,314, U.S. Pat. No. 5,310,554, U.S. Pat. No. 5,328,845, U.S. Pat. No. 5,356,810, U.S. Pat. No. 5,422,247, U.S. Pat. No. 5,591,343, U.S. Pat. No. 6,166,231, U.S. Pat. No. 6,750,048, U.S. Pat. No. 6,812,001, U.S. Pat. No. 6,818,239, U.S. Pat. No. 7,015,014, US2003/0054070, US2005/0266132, each of which is incorporated herein by reference). In many typical isolation procedures, cells are disrupted (e.g., mechanically (for example using a bead mill, mashing), enzymatically (e.g. using zymolyase or a β-1,3 glucanase such as Glucanex 200G (Novozyme), chemically (e.g., by exposure to a mild caustic agent such as a detergent or 0.1 N NaOH, for example at room temperature or at elevated temperature), using a reducing agent (e.g. dithiothreitol, β-mercaptoethanol), using high pressure homogenization/shearing, by changing pH, etc. and combinations thereof) to allow access of intracellular carotenoid and/or retinolic compound(s) to an extraction solvent, and are then extracted one or more times. In certain embodiments, cells are disrupted mechanically using a bead mill/mashing at high pressure (e.g. at 25K, 10K-30K, 15K-25K, or 20-25K, pound-force per square inch (psi)). Cells may optionally be concentrated (e.g., to at least about 100 g/L or more, including to at least about 120 g/l, 150 g/l, 175 g/L, 200 g/L or more) and/or dried (e.g., with a spray dryer, double drum dryer (e.g. Blaw Knox double drum dryer), single drum vacuum dryer, etc.), prior to exposure to extraction solvent (and/or prior to disruption or homogenization). Disruption can, of course, be performed prior to and/or during exposure to extraction solvent. After extraction, solvent is typically removed (e.g., by evaporation, for example by application of vacuum, change of temperature, etc.). In some instances, cells are disrupted and then subjected to supercritical liquid extraction or solvent extraction. Typical liquids or solvents utilized in such extractions include, for example, organic or non-organic liquids or solvents. To give but a few specific examples, such liquids or solvents may include acetone, supercritical fluids (e.g. carbon dioxide, propane, xenon, ethane, propylene, methane, ethylene, ethanol), carbon dioxide, chloroform, ethanol, ethyl acetate, heptane, hexane, isopropanol, methanol, methylene chloride, octane, tetrahydrofuran (THF), cyclohexane, isobutyl acetate, methyl ketone, ethyl ketone, toluene, cyclohexanone, benzene, propylene glycol, vegetable oils (e.g. soybeen soybean oil, rapeseed oil, corn oil, cottonseed oil, canola oil, etc.) and combinations thereof (e.g. hexane:ethyl acetate, combination of a polar and non-polar solvent, combination of an alcohol with either hexane or ethyl acetate). Particular solvents may be selected, for example, based on their ability to solubilize particular carotenoid compounds and/or retinolic compounds, or sets of carotenoid compounds (e.g., all carotenoids) and/or retinolic compounds (e.g., all retinolic compounds), and/or based on regulatory or other considerations (e.g., toxicity, cost, ease of handling, ease of removal, ease of disposal, etc.). For example, more polar carotenoids (e.g., xanthophylls) are known to be extracted more efficiently into extraction solvents with increased polarity. Craft (1992) J. Agric. Food Chem 40, 431-434 which is herein incorporated by reference discusses the relative solubility of two carotenoids, lutein and β-carotene in different solvents. In some embodiments, combinations of solvents may be utilized. In some embodiments, combinations of a relatively polar solvent (e.g., alcohols, acetone, chloroform, methylene chloride, ethyl acetate, etc.) and a relatively non-polar solvent (e.g., hexane, cyclohexane, oils, etc.) are utilized for extraction. Those of ordinary skill in the art will readily appreciate that different ratios of polar to non-polar solvent may be employed as appropriate in a particular situation. Just to give a few examples, common ratios include 1:1, 2:1, 3:1, 3:2, 95:5, 90:10, 85:15, 80:20, 75:25, 70:30, 65:45, 60:40, 55:45, and 50:50. It will be appreciated that solvents or solvent mixtures of different polarities may be more effective at extracting particular carotenoids (e.g., based on their polarities and/or as a function of other attributes of the host cell material from which they are being extracted). Those of ordinary skill in the art are well able to adjust the overall polarity of the extracting solvent, for instance by adjusting the relative amounts of polar and non-polar solvents in a solvent blend, in order to achieve more efficient extraction. Extraction may be performed under any of a variety of environmental conditions, including any of a variety of temperatures. For example, extraction may be performed on ice (for example at 4° C., 0° C., less than 0° C.), at room temperature, or at any of a variety of other temperatures. For example, a solvent may be maintained at a selected temperature (e.g., about less than 0, 0, 4, 25, 28, 30, 37, 68, 70, 75, 80, 85, 90, 95, or 100° C.) in order to improve or adjust extraction of a particular desired carotenoid. Extraction typically yields a crude oil suspension. In some embodiments, the crude oil suspension contains some intact host cells but is at least about 95% free of intact host cells. In some embodiments, the crude oil suspension is at least about 96%, 97%, 98%, or 99% or more free of intact host cells. In some embodiments, the suspension is substantially free of water-soluble cell components (e.g., nucleic acids, cell wall or storage carbohydrates, etc.). In some embodiments, the suspension contains less than about 5%, 4%, 3%, 2%, or 1% or less water-soluble cell components. Extraction conditions that yield a crude oil suspension will enrich for lipophilic components that accumulate in the lipid bodies within oleaginous organisms. In general, the major components of the lipid bodies consist of triacylglycerols, ergosteryl esters, other steryl esters, free ergosterol, phospholipids, and some proteins, which often function in the synthesis or regulation of the levels of other lipid body components. C16 and C18 (e.g. C16:0, C16:1, C18:0, C18:1, and C18:2) are generally the major fatty acids present in lipid bodies, mainly as components of triacylglycerol and steryl esters. In some embodiments of the invention, the crude oil suspension contains at least about 2.5% by weight carotenoid compound(s) and/or retinolic compound(s); in some embodiments, the crude oil suspension contains at least about 5% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 10% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 20% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 30% by weight carotenoid compound(s) and/or retinolic compound(s), at least about 40% by weight carotenoid compound(s) and/or retinolic compound(s), or at least about 50% by weight carotenoid compound(s) and/or retinolic compound(s). The crude oil suspension may optionally be refined as known in the art. Refined oils may be used directly as feed or food additives. Alternatively or additionally, carotenoids and/or retinolic compound can be isolated from the oil using conventional techniques. Given the sensitivity of carotenoids and retinolic compounds generally to oxidation, many embodiments of the invention employ oxidative stabilizers (e.g., ascorbyl palmitate, tocopherols, vitamin C (e.g. sodium ascorbate), ethoxyquin, vitamin E, BHT, BHA, TBHQ, etc., or combinations thereof) during and/or after carotenoid isolation. Alternatively or additionally, nitrogen or an inert gas can be utilized to purge oxygen from the process lines of any tanks or equipment. Alternatively or additionally, microencapsulation, (for example with a microencapsulation ingredients such as proteins, carbohydrates (e.g. maltodextrin, gum acacia, xanthan gum, starches/sugars like sucrose), or gelatins, or any other substance which creates a physical barrier to air and/or light) may be employed to add a physical barrier to oxidation and/or to improve handling (see, for example, U.S. Patent Applications 2004/0191365 and 2005/0169999). For example, carotenoids and/or retinolic compounds produced according to the present invention may be microencapsulated after isolation during the formulation of commercial products (e.g. pharmaceuticals, food supplements, electro-optic applications, animal feed additives, cosmetics, etc.) to minimize or eliminate oxidation during production, storage, transport, etc. Extracted carotenoids and/or retinolic compounds may be further isolated and/or purified, for example, by crystallization, washing, recrystallization, and/or other purification strategies. In some embodiments, carotenoid and/or retinolic compound crystals are collected by filtration and/or centrifugation. Isolated or purified carotenoids and/or retinolic compound may be dried and/or formulated for storage, transport, sale, and/or ultimate use. To give but a few specific examples, carotenoids and/or retinolic compounds may be prepared as a water (e.g. cold water) dispersible powder (e.g. 1%-20% carotenoid: microencapsulation ingredient), as a suspension of crystals in oil (e.g., vegetable oil, e.g., about 1%-30%, 5%-30%, 10%-30% w/w), etc. Uses Carotenoids and/or retinolic compounds produced according to the present invention can be utilized in any of a variety of applications, for example exploiting their biological or nutritional properties (e.g., anti-oxidant, anti-proliferative, etc.) and/or their pigment properties. For example, according to the present invention, carotenoids may be used in pharmaceuticals (see, for example, Bertram, Nutr. Rev. 57:182, 1999; Singh et al., Oncology 12:1643, 1998; Rock, Pharmacol. Ther. 75:185, 1997; Edge et al, J. Photochem Photobiol 41:189, 1997; U.S. Patent Application 2004/0116514; U.S. Patent Application 2004/0259959), food supplements (see, for example, Koyama et al, J. Photochem Photobiol 9:265, 1991; Bauernfeind, Carotenoids as colorants and vitamin A precursors , Academic Press, NY, 1981; U.S. Patent Application 2004/0115309; U.S. Patent Application 2004/0234579), electro-optic applications, animal feed additives (see, for example, Krinski, Pure Appl. Chem. 66:1003, 1994; Polazza et al., Meth. Enzymol. 213:403, 1992), cosmetics (as anti-oxidants and/or as cosmetics, including fragrances; see for example U.S. Patent Application 2004/0127554), etc. Carotenoids produced in accordance with the present invention may also be used as intermediates in the production of other compounds (e.g., steroids, etc.). For example, astaxanthin and/or esters thereof may be useful in a variety of pharmaceutical applications and health foods including treatment of inflammatory diseases, asthma, atopic dermatitis, allergies, multiple myeloma, arteriosclerosis, cardiovascular disease, liver disease, cerebrovascular disease, thrombosis, neoangiogenesis-related diseases, including cancer, rheumatism, diabetic retinopathy; macular degeneration and brain disorder, hyperlipidemia, kidney ischemia, diabetes, hypertension, tumor proliferation and metastasis; and metabolic disorders. Additionally, carotenoids and astaxanthin may be useful in the prevention and treatment of fatigue, for improving kidney function in nephropathy from inflammatory diseases, as well as prevention and treatment of other life habit-related diseases. Still further, astaxanthin has been found to play a role as inhibitors of various biological processes, including interleukin inhibitors, phosphodiesterase inhibitors, phospholipase A2 inhibitors, cyclooxygenase-2 inhibitors, matrix metalloproteinase inhibitors, capillary endothelium cell proliferation inhibitors, lipoxygenase inhibitors. See, e.g., Japanese Publication No. 2006022121, published 2006 Jan. 26 (JP Appl No. 2005-301156 filed 2005 Oct. 17); Japanese Publication No. 2006016408, published 2006 Jan. 19 (JP Appl No. 2005-301155 filed 2005 Oct. 17); Japanese Publication No. 2006016409, published 2006 Jan. 19 (JP Appl No. 2005-301157 filed 2005 Oct. 17); Japanese Publication No. 2006016407, published 2006 Jan. 19 (JP Appl No. 2005-301153 filed 2005 Oct. 17); Japanese Publication No. 2006008717, published 2006 Jan. 12 (JP Appl No. 2005-301151 filed 2005 Oct. 17); Japanese Publication No. 2006008716, published 2006 Jan. 12 (JP Appl No. 2005-301150 filed 2005 Oct. 17); Japanese Publication No. 2006008720, published 2006 Jan. 12 (JP Appl No. 2005-301158 filed 2005 Oct. 17); Japanese Publication No. 2006008719, published 2006 Jan. 12 (JP Appl No. 2005-301154 filed 2005 Oct. 17); Japanese Publication No. 2006008718, published 2006 Jan. 12 (JP Appl No. 2005-301152 filed 2005 Oct. 17); Japanese Publication No. 2006008713, published 2006 Jan. 12 (JP Appl No. 2005-301147 filed 2005 Oct. 17); Japanese Publication No. 2006008715, published 2006 Jan. 12 (JP Appl No. 2005-301149 filed 2005 Oct. 17); Japanese Publication No. 2006008714, published 2006 Jan. 12 (JP Appl No. 2005-301148 filed 2005 Oct. 17); and Japanese Publication No. 2006008712, published 2006 Jan. 12 (JP Appl No. 2005-301146 filed 2005 Oct. 17). As other non-limiting examples, retinolic compounds produced according to the present invention may be used in pharmaceuticals, foodstuff, dietary supplements, electro-optic applications, animal feed additives, cosmetics, etc. It will be appreciated that, in some embodiments of the invention, carotenoids and/or retinolic compounds produced by manipulated host cells as described herein are incorporated into a final product (e.g., food or feed supplement, pharmaceutical, cosmetic, dye-containing item, etc.) in the context of the host cell. For example, host cells may be lyophilized, freeze dried, frozen or otherwise inactivated, and then whole cells may be incorporated into or used as the final product. The host cell may also be processed prior to incorporation in the product to increase bioavailability (e.g., via lysis). Alternatively or additionally, a final product may incorporate only a portion of the host cell (e.g., fractionated by size, solubility), separated from the whole. For example, in some embodiments of the invention, lipid droplets are isolated from the host cells and are incorporated into or used as the final product. For instance, inventive carotenoid-containing and/or retinolic compound-containing lipid bodies (e.g., from engineered cells, and particularly from engineered fungal cells) may be substituted for the plant oil bodies described in U.S. Pat. No. 6,599,513 (the entire contents of which are hereby incorporated by reference) and incorporated into emulsion or emulsion formulations, as described therein. In other embodiments, the carotenoids and/or retinolic compounds themselves, or individual carotenoid and/or retinolic compounds are isolated and reformulated into a final product. As stated above, fatty acid and glucoside esters are the predominant carotenoid esters found in nature, whereas additional esters (e.g. with organic acids or inorganic phosphate) can be synthesized to generate useful product forms. For delivery, carotenoid esters can also be formulated as salts of the ester form. See, e.g., US Publication No. 20050096477. The amount of carotenoid and/or retinolic compound incorporated into a given product may vary dramatically depending on the product, and the particular carotenoid(s) and/or retinolic compound(s) involved. Amounts may range, for example, from less than 0.01% by weight of the product, to more than 1%, 10%, 20%, 30% or more; in some cases the carotenoid and/or retinolic compound may comprise 100% of the product. Thus, amount of carotenoid and/or retinolic compound incorporated into a given product may be, for example, 0.01%, 0.02%, 0.03%, 0.04%, 0.05%, 0.06%, 0.07%, 0.08%, 0.09%, 0.1%, 0.2%, 0.3%, 0.4%, 0.5%, 0.6%, 0.7%, 0.8%, 0.9%, 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 100%. In some embodiments of the invention, one or more produced carotenoids and/or retinolic compounds is incorporated into a component of food or feed (e.g., a food supplement). Types of food products into which carotenoids and/or retinolic compounds can be incorporated according to the present invention are not particularly limited, and include beverages such as milk, water, sports drinks, energy drinks, teas, juices, and liquors; confections such as jellies and biscuits; fat-containing foods and beverages such as dairy products; processed food products such as rice and soft rice (or porridge); infant formulas; breakfast cereals; or the like. In some embodiments, one or more produced carotenoids and/or retinolic compounds is incorporated into a dietary supplements, such as for example a multivitamin. In certain embodiments, beta-carotene produced according to the present invention is included in a dietary supplement. In certain embodiments, lutein produced according to the present invention is included in a dietary supplement. In certain embodiments, retinol, retinal, retinyl palmitate, retinyl acetate, and/or retinoic acid produced according to the present invention is included in a dietary supplement. In some embodiments of this aspect of the invention, it may be useful to incorporate the carotenoids and/or retinolic compounds within bodies of edible lipids as it may facilitate incorporation into certain fat-containing food products. Thus, for example, when the edible fungus, Candida utilis is used as a host, its' carotenoid and/or retinolic compound containing lipids may be directly incorporated into a component of food or feed (e.g., a food supplement). Examples of feedstuffs into which carotenoids and/or retinolic compounds produced in accordance with the present invention may be incorporated include, for instance, pet foods such as cat foods, dog foods and the like, feeds for aquarium fish, cultured fish or crustaceans, etc., feed for farm-raised animals (including livestock and further including fish or crustaceans raised in aquaculture). Food or feed material into which the carotenoid(s) and/or retinolic compound(s) produced in accordance with the present invention is incorporated is preferably palatable to the organism which is the intended recipient. This food or feed material may have any physical properties currently known for a food material (e.g., solid, liquid, soft). In some embodiments, feedstuffs containing carotenoids and/or retinolic compounds produced in accordance with the present invention are substantially free of intact host cells. For example, feedstuffs of the present invention may be at least about 95% free of intact host cells. In some embodiments, feedstuffs of the present invention are at least about 96%, 97%, 98%, or 99% or more free of intact host cells. Such embodiments are typical when the carotenoids and/or retinolic compounds are highly purified away from the host cell in which they were produced (see section entitled “Production and Isolation of Carotenoids and/or Retinolic Compounds”). In some embodiments, feedstuffs containing carotenoids and/or retinolic compounds produced in accordance with the present invention are not substantially free of intact host cells. For example, feedstuffs of the present invention may comprise greater than about 95% intact host cells. In certain embodiments, feedstuffs of the present invention comprise greater than about 70%, 75%, 85%, or 90% intact host cells. In certain embodiments, feedstuffs of the present invention comprise nearly intact host cells. For example, feedstuffs of the present invention may comprise greater than about 70%, 75%, 85%, 90%, or 95% nearly intact host cells. As will be appreciated by those of ordinary skill in the art, carotenoid and/or retinolic compound-containing feedstuffs of the present invention that contain intact cells and/or nearly intact cells will have great utility in providing the carotenoids and/or retinolic compounds of interest present in such host cells to an animal. Such embodiments are advantageous when host cells that produce the carotenoids and/or retinolic compounds of interest contain additional vitamins, nutrients, etc. that benefit the animal. In some embodiments of the invention, one or more produced carotenoids and/or retinolic compounds is incorporated into a cosmetic product. Examples of such cosmetics include, for instance, skin cosmetics (e.g., lotions, emulsions, creams and the like), lipsticks, anti-sunburn cosmetics, makeup cosmetics, fragrances, products for daily use (e.g., toothpastes, mouthwashes, bad breath preventive agents, solid soaps, liquid soaps, shampoos, conditioners), etc. In some embodiments, one or more produced carotenoids and/or retinolic compounds is incorporated into a pharmaceutical. Examples of such pharmaceuticals include, for instance, various types of tablets, capsules, drinkable agents, troches, gargles, etc. In some embodiments, the pharmaceutical is suitable for topical application. Dosage forms are not particularly limited, and include capsules, oils, granula, granula subtilae, pulveres, tabellae, pilulae, trochisci, or the like. Oils and oil-filled capsules may provide additional advantages both because of their lack of ingredient decomposition during manufacturing, and because inventive carotenoid-containing and/or retinolic compound-containing lipid droplets may be readily incorporated into oil-based formulations. Pharmaceuticals according to the present invention may be prepared according to techniques established in the art including, for example, the common procedure as described in the United States Pharmacopoeia, for example. Carotenoids and/or retinolic compounds produced according to the present invention may be incorporated into any pigment-containing product including, for example, fabric, paint, etc. They may also be incorporated into a product which is an environmental indicator, or an instrument such as a biosensor for use as a detection agent. Carotenoids and/or retinolic compounds produced according to the present invention (whether isolated or in the context of lipid droplets or of cells, e.g., fungal cells) may be incorporated into products as described herein by combinations with any of a variety of agents. For instance, such carotenoids and/or retinolic compounds may be combined with one or more binders or fillers. In some embodiments, inventive products will include one or more chelating agents, pigments, salts, surfactants, moisturizers, viscosity modifiers, thickeners, emollients, fragrances, preservatives, etc., and combinations thereof. Useful surfactants include, for example, anionic surfactants such as branched and unbranched alkyl and acyl hydrocarbon compounds, sodium dodecyl sulfate (SDS); sodium lauryl sulfate (SLS); sodium lauryl ether sulfate (SLES); sarconisate; fatty alcohol sulfates, including sodium, potassium, ammonium or triethanolamine salts of C 10 to C 18 saturated or unsaturated forms thereof; ethoxylated fatty alcohol sulfates, including alkyl ether sulfates; alkyl glyceryl ether sulfonate, alpha sulpho fatty acids and esters; fatty acid esters of isethionic acid, including Igepon A; acyl (fatty) N-methyltaurides, including Igepon T; dialkylsulfo succinate esters, including C 8 , C 10 and C 12 forms thereof; Miranot BT also referred to as lauroamphocarboxyglycinate and sodium tridecath sulfate; N-acylated amino acids, such as sodium N-lauroyl sarconisate or gluconate; sodium coconut monoglyceride sulfonate; and fatty acid soaps, including sodium, potassium, DEA or TEA soaps. Among the cationic surfactants that are useful are monoalkyl trimethyl quartenary salts; dialkyl dimethyl quartenary salts; ethoxylated or propoxylated alkyl quaternary ammonium salts, also referred to in the art as ethoquats and propoquats; cetyl benzylmethylalkyl ammonium chloride; quaternized imidazolines, which are generally prepared by reacting a fat or fatty acid with diethylenetriamine followed by quaternization, and non-fat derived cationic polymers such as the cellulosic polymer, Polymer JR (Union Carbide). Further useful cationic surfactants include lauryl trimethyl ammonium chloride; cetyl pyridinium chloride; and alkyltrimethylammonium bromide. Cationic surfactants are particularly useful in the formulation of hair care products, such as shampoos, rinses and conditioners. Useful nonionic surfactants include polyethoxylated compounds and polypropoxylated products. Examples of ethoxylated and propoxylated non-ionic surfactants include ethoxylated anhydrohexitol fatty esters, for example Tween 20; mono- and diethanolamides; Steareth-20, also known as Volpo20; polyethylene glycol fatty esters (PEGs), such as PEG-8-stearate, PEG-8 distearate; block co-polymers, which are essentially combinations of hydrophylic polyethoxy chains and lipophilic polypropoxy chains and generically known as Poloaxamers. Still other useful non-ionic surfactants include fatty esters of polyglycols or polyhydric alcohols, such as mono and diglyceride esters; mono- and di-ethylene glycol esters; diethylene glycol esters; sorbitol esters also referred to as Spans; sucrose esters; glucose esters; sorbitan monooleate, also referred to as Span80; glyceryl monostearate; and sorbitan monolaurate, Span20 or Arlacel 20. Yet other useful nonionic surfactants include polyethylene oxide condensates of alkyl phenols and polyhydroxy fatty acid amide surfactants which may be prepared as for example disclosed in U.S. Pat. No. 2,965,576. Examples of amphoteric surfactants which can be used in accordance with the present invention include betaines, which can be prepared by reacting an alkyldimethyl tertiary amine, for example lauryl dimethylamine with chloroacetic acid. Betaines and betaine derivatives include higher alkyl betaine derivatives including coco dimethyl carboxymethyl betaine; sulfopropyl betaine; alkyl amido betaines; and cocoamido propyl betaine. Sulfosultaines which may be used include for example, cocoamidopropyl hydroxy sultaine. Still other amphoteric surfactants include imidazoline derivatives and include the products sold under the trade name “Miranol” described in U.S. Pat. No. 2,528,378 which is incorporated herein by reference in its entirety. Still other amphoterics include phosphates for example, cocamidopropyl PG-dimonium chloride phosphate and alkyldimethyl amine oxides. Suitable moisturizers include, for example, polyhydroxy alcohols, including butylene glycol, hexylene glycol, propylene glycol, sorbitol and the like; lactic acid and lactate salts, such as sodium or ammonium salts; C 3 and C 6 diols and triols including hexylene glycol, 1,4 dihydroxyhexane, 1,2,6-hexane triol; aloe vera in any of its forms, for example aloe vera gel; sugars and starches; sugar and starch derivatives, for example alkoxylated glucose; hyaluronic acid; lactamide monoethanolamine; acetamide monoethanolamine; glycolic acid; alpha and beta hydroxy acids (e.g. lactic, glycolic salicylic acid); glycerine; pantheol; urea; vaseline; natural oils; oils and waxes (see: the emollients section herein) and mixtures thereof.) Viscosity modifiers that may be used in accordance with the present invention include, for example, cetyl alcohol; glycerol, polyethylene glycol (PEG); PEG-stearate; and/or Keltrol. Appropriate thickeners for use in inventive products include, for example, gelling agents such as cellulose and derivatives; Carbopol and derivatives; carob; carregeenans and derivatives; xanthane gum; sclerane gum; long chain alkanolamides; bentone and derivatives; Kaolin USP; Veegum Ultra; Green Clay; Bentonite NFBC; etc. Suitable emollients include, for example, natural oils, esters, silicone oils, polyunsaturated fatty acids (PUFAs), lanoline and its derivatives and petrochemicals. Natural oils which may be used in accordance with the present invention may be obtained from sesame; soybean; apricot kernel; palm; peanut; safflower; coconut; olive; cocoa butter; palm kernel; shea butter; sunflower; almond; avocado; borage; carnauba; hazel nut; castor; cotton seed; evening primrose; orange roughy; rapeseed; rice bran; walnut; wheat germ; peach kernel; babassu; mango seed; black current seed; jojoba; macademia nut; sea buckthorn; sasquana; tsubaki; mallow; meadowfoam seed; coffee; emu; mink; grape seed; thistle; tea tree; pumpkin seed; kukui nut; and mixtures thereof. Esters which may be used include, for example, C 8 -C 30 alklyl esters of C 8 -C 30 carboxylic acids; C 1 -C 6 diol monoesters and diesters of C 8 -C 30 carboxylic acids; C 10 -C 20 alcohol monosorbitan esters, C 10 -C 20 alcohol sorbitan di- and tri-esters; C 10 -C 20 alcohol sucrose mono-, di-, and tri-esters and C 10 -C 20 fatty alcohol esters of C 2 -C 6 2-hydroxy acids and mixtures thereof. Examples of these materials include isopropyl palmitate; isopropyl myristate; isopropyl isononate; C 12 /C 14 benzoate ester (also known as Finesolve); sorbitan palmitate, sorbitan oleate; sucrose palmitate; sucrose oleate; isostearyl lactate; sorbitan laurate; lauryl pyrrolidone carboxylic acid; panthenyl triacetate; and mixtures thereof. Further useful emollients include silicone oils, including non-volatile and volatile silicones. Examples of silicone oils that may be used in the compositions of the present invention are dimethicone; cyclomethycone; dimethycone-copolyol; aminofunctional silicones; phenyl modified silicones; alkyl modified silicones; dimethyl and diethyl polysiloxane; mixed C 1 -C 30 alkyl polysiloxane; and mixtures thereof. Additionally useful silicones are described in U.S. Pat. No. 5,011,681 to Ciotti et al., incorporated by reference herein. A yet further useful group of emollients includes lanoline and lanoline derivatives, for example lanoline esters. Petrochemicals which may be used as emollients in the compositions of the present invention include mineral oil; petrolatum; isohexdecane; permethyl 101; isododecanol; C 11 -C 12 Isoparrafin, also known as Isopar H. Among the waxes which may be included in inventive products are animal waxes such as beeswax; plant waxes such as carnauba wax, candelilla wax, ouricurry wax, Japan wax or waxes from cork fibres or sugar cane. Mineral waxes, for example paraffin wax, lignite wax, microcrystalline waxes or ozokerites and synthetic waxes may also be included. Exemplary fragrances for use in inventive products include, for instance, linear and cyclic alkenes (i.e. terpenes); primary, secondary and tertiary alcohols; ethers; esters; ketones; nitrites; and saturated and unsaturated aldehydes; etc. Examples of synthetic fragrances that may be used in accordance with the present invention include without limitation acetanisole; acetophenone; acetyl cedrene; methyl nonyl acetaldehyde; musk anbrette; heliotropin; citronellol; sandella; methoxycitranellal; hydroxycitranellal; phenyl ethyl acetate; phenylethylisobutarate; gamma methyl ionone; geraniol; anethole; benzaldehyde; benzyl acetate; benzyl salicate; linalool; cinnamic alcohol; phenyl acetaldehyde; amyl cinnamic aldehyde; caphore; p-tertiairy butyl cyclohexyl acetate; citral; cinnamyl acetate; citral diethyl acetal; coumarin; ethylene brasslate; eugenol; 1-menthol; vanillin; etc. Examples of natural fragrances of use herein include without limitation lavandin; heliotropin; sandlewood oil; oak moss; pathouly; ambergris tincture; ambrette seed absolute; angelic root oil; bergamont oil; benzoin Siam resin; buchu leaf oil; cassia oil; cedarwood oil; cassia oil; castoreum; civet absolute; chamomile oil; geranium oil; lemon oil; lavender oil; Ylang Ylang oil; etc. A list of generally used fragrance materials can be found in various reference sources, for example, “Perfume and Flavor Chemicals”, Vols. I and II; Steffen Arctander Allured Pub. Co. (1994) and “Perfumes: Art, Science and Technology”; Muller, P. M. and Lamparsky, D., Blackie Academic and Professional (1994) both incorporated herein by reference. Suitable preservatives include, among others, (e.g., sodium metabisulfite; Glydant Plus; Phenonip; methylparaben; Germall 115; Germaben II; phytic acid; sodium lauryl sulfate (SLS); sodium lauryl ether sulfate (SLES); Neolone; Kathon; Euxyl and combinations thereof), anti-oxidants (e.g., butylated hydroxytoluened (BHT); butylated hydroxyanisol (BHA); ascorbic acid (vitamin C); tocopherol; tocopherol acetate; phytic acid; citric acid; pro-vitamin A. In some embodiments, inventive products will comprise an emulsion (e.g., containing inventive lipid bodies), and may include one or more emulsifying agents (e.g., Arlacel, such as Alacel 165; Glucamate; and combinations thereof) and/or emulsion stabilizing agents. In some embodiments, inventive products will include one or more biologically active agents other than the carotenoid(s). To give but a few examples, inventive cosmetic or pharmaceutical products may include one or more biologically active agents such as, for example, sunscreen actives, anti-wrinkle actives, anti-aging actives, whitening actives, bleaching actives, sunless tanning actives, anti-microbial actives, anti-acne actives, anti-psoriasis actices, anti-eczema actives, antioxidants, anesthetics, vitamins, protein actives, etc. EXEMPLIFICATION Table 26 below describes certain Yarrowia lipolytica strains used in the following exemplification: TABLE 26Yarrowia lipolytica strains.NRRL Y-1095Wild type diploidATCC76861MATB ura2-21 lyc1-5 LYS1-5BATCC76982MATB ade1 leu2-35 lyc1-5 xpr2ATCC201249MATA ura3-302 leu2-270 lys8-11 PEX17-HAMF346MATA ura2-21ATCC76861 x ATCC201249MF350MATB ura2-21 leu2-35 ade1ATCC76982 x MF346 (The genotypes at LYC1, LYS1, XPR2, and PEX17 were not determined in crosses nor verified for ATCC strains.) All basic molecular biology and DNA manipulation procedures described herein are generally performed according to Sambrook et al. or Ausubel et al. (Sambrook J, Fritsch E F, Maniatis T (eds). 1989 . Molecular Cloning: A Laboratory Manual . Cold Spring Harbor Laboratory Press: New York; Ausubel F M, Brent R, Kingston R E, Moore D D, Seidman J G, Smith J A, Struhl K (eds). 1998. Current Protocols in Molecular Biology . Wiley: New York). Example 1 Production of Plasmids for Carotenoid Strain Construction Plasmids were generated for construction of carotenoid producing strains. The following subparts describe production of plasmids encoding carotenogenic polypeptides. Plasmids used in these studies and details of their construction are described in Table 27. Additional plasmid construction details and descriptions of their use are found in the text of the relevant subsection. All PCR amplifications used NRRL Y-1095 genomic DNA as template unless otherwise specified. The URA5 gene described below is allelic with the ura2-21 auxotrophy above. The GPD1 and TEF1 promoters are from Y. lipolytica as is the XPR2 terminator. GGS1 is the gene encoding the Y. lipolytica gene encoding geranylgeranylpyrophosphate synthase. The nucleic acid coding sequence, and encoded Ggs1 protein of pMB4591 and pMB4683 are as follows: (SED ID NO: 1)atggattataacagcgcggatttcaaggagatatggggcaaggccgccgacaccgcgctgctgggaccgtacaactacctcgccaacaaccggggccacaacatcagagaacacttgatcgcagcgttcggagcggttatcaaggtggacaagagcgatctcgagaccatttcgcacatcaccaagattttgcataactcgtcgctgcttgttgatgacgtggaagacaactcgatgctccgacgaggcctgccggcagcccattgtctgtttggagtcccccaaaccatcaactccgccaactacatgtactttgtggctctgcaggaggtgctcaagctcaagtcttatgatgccgtctccattttcaccgaggaaatgatcaacttgcatagaggtcagggtatggatctctactggagagaaacactcacttgcccctcggaagacgagtatctggagatggtggtgcacaagaccggtggactgtttcggctggctctgagacttatgctgtcggtggcatcgaaacaggaggaccatgaaaagatcaactttgatctcacacaccttaccgacacactgggagtcatttaccagattctggatgattacctcaacctgcagtccacggaattgaccgagaacaagggattctgcgaagatatcagcgaaggaaagttttcgtttccgctgattcacagcatacgcaccaacccggataaccacgagattctcaacattctcaaacagcgaacaagcgacgcttcactcaaaaagtacgccgtggactacatgagaacagaaaccaagagtttcgactactgcctcaagaggatacaggccatgtcactcaaggcaagttcgtacattgatgatctagcagcagctggccacgatgtctccaagctacgagccattttgcattattttgtgtccacctctgactgtgaggagagaaagtactttgaggatgcgcagtga(SEQ ID NO: 2)mdynsadfkeiwgkaadtallgpynylannrghnirehliaafgavikvdksdletishitkilhnssllvddvednsmlrrglpaahclfgvpqtinsanymyfvalqevlklksydavsifteeminlhrgqgmdlywretltcpsedeylemvvhktgglfrlalrlmlsvaskqedhekinfdlthltdtlgviyqilddylnlqsteltenkgfcedisegkfsfplihsirtnpdnheilnilkqrtsdaslkkyavdymrtetksfdyclkriqamslkassyiddlaaaghdvsklrailhyfvstsdceerkyfedaq TABLE 27PlasmidsPlasmidBackboneInsertOligos or sourcepMB4529PCR2.13.4 kb ADE1 PCRMO4475 &productMO4476pMB4534PCR2.12.1 kb LEU2 PCRMO4477 &productMO4478pMB4535PCR2.11.2 kb URA5 PCRMO4471 &productMO4472pMB4589pMB4535 (KpnI + SpeI)1.2 kb GPD1 promoterMO4568 &(KpnI + NotI); 0.14 kbMO4591;XPR2 terminator (NotI +MO4566 &SpeI)MO4593pMB4590pMB4535 (KpnI + SpeI)0.4 kb TEF1 promoterMO4571 &(KpnI + NotI); 0.14 kbMO4592;XPR2 terminator (NotI +MO4566 &SpeI)MO4593pMB4591pMB4590 (NheI + MluI)1.0 kb GGS1 ORF (XbaI +MO4534 &MluI)MO4544pMB4597pMB4534 (Acc65I +GPD1 promoter & XPR2From pMB4589SpeI)terminator (Acc65I +SpeI)pMB4603pMB4597 (RsrII + MluI)Residual backboneFrom pMB4590& TEF1 promoter (RsrII +MluI)pMB4616pMB4529 (RsrII + SpeI)Residual backboneFrom pMB4589& GPD1 promoter &XPR2 terminator (RsrII +SpeI)pMB4629pMB4616 (RsrII + MluI)Residual backboneFrom pMB4590& TEF1 promoter (RsrII +MluI)pMB4631pMB4603 (KpnI + NheI)1.2 kb GPD1 promoterMO4568 &(KpnI + NheI);MO4659pMB4628pMB4603carRPSee 1ApMB4637pMB4629 (NheI + MluI)1.5 kb hmg1 trunc ORFSee 1D(XbaI + MluI)pMB4714pMB4691 (Nhel + MluI)1.5 kb hmg1 trunc ORFSee 1D(XbaI + MluI)pMB4638pMB4629carB(i − )See 1BpMB4660pMB4638 (+URA3)carB(i − )See 1CpMB4662pMB4631 (SpeI + XhoI)1.8 kb URA3 fragmentSee 1C(SpeI + BsaIpMB4683pMB4662 (Acc65I +1.4 kb tef1p-GGS1From pMB4591MluI)fragment (Acc65I +MluI)pMB4692pMB4662 (Acc65I +0.4 kb TEF1 promoterSee 1EMluI)(Acc65I + NheI); 0.55 kbcrtZ ORF (XbaI + MluI)pMB4698pMB4629 (NheI + MluI)0.9 kb crtW ORF (XbaI +See 1FMluI)pMB4599pBluescriptSKII-1.9 kb carRP geneSee 1A(EcoRV)pMB4606pBluescriptSKII-1.9 kb carB geneSee 1A(EcoRV)pMB4613pMB4599 (Acc65I +carRP(i − )See 1APpuMI)pMB4619pBluescriptSKII-(BamHI +carB(i − )See 1AAcc65I))pMB4705pMB4603 (NheI + MluI)carRP(i − )See 1ApMB4691pMB4662 (Acc65I +0.4 kb TEF1 promoterFrom pMB4629MluI)(Acc65I + MluI)pMB4751pMB46910.75 kb YALI0D12903gInserted betweenpromoter + 0.45 Y.TEF1p/XPRt andlipoltyica HIS3URA3terminatorpMB4719pMB4691 (NheI + MluI)crtZ ( E. litoralis )See 1JpMB4778pMB4751 (NheI + MluI)crtZ ( P. bermudensis )See 1IpMB4741pMB4629 (NheI + MluI)crtW ( Aurantimonas )See 1GpMB4735pMB4629 (NheI + MluI)crtW ( P. bermudensis )See 1HpMB4812pMB4603 (NheI + MluI)al-2 ( N. crassa )See 1KpMB4846pMB4691 (NheI + MluI)crtZ ( Erythrobacter sp.See 1LNAP1)pMB4835pMB4691 (NheI + MluI)S. alaskensis )See 1MpMB4845pMB4691 (NheI + MluI)crtZ (R. biformata )See 1NpMB4837pMB4691 (NheI + MluI)crtZ (X. autrophicus )See 1OpMB4850pMB4691 (NheI + MluI)crtZ ( P. putida )See 1P Certain oligonucleotides referred to in Table 27 above are as follows: (SEQ ID NO: 3)MO44715′-CTGGGTGACCTGGAAGCCTT(SEQ ID NO: 4)MO44725′-AAGATCAATCCGTAGAAGTTCAG(SEQ ID NO: 5)MO44755′-AAGCGATTACAATCTTCCTTTGG(SEQ ID NO: 6)MO44765′-CCAGTCCATCAACTCAGTCTCA(SEQ ID NO: 7)MO44775′-GCATTGCTTATTACGAAGACTAC(SEQ ID NO: 8)MO44785′-CCACTGTCCTCCACTACAAACAC(SEQ ID NO: 9)MO45345′-CACAAACGCGTTCACTGCGCATCCTCAAAGT(SEQ ID NO: 10)MO45445′-CACAATCTAGACACAAATGGATTATAACAGCGCGGAT(SEQ ID NO: 11)MO45665′-CACAAACTAGTTTGCCACCTACAAGCCAGAT(SEQ ID NO: 12)MO45685′-CACAAGGTACCAATGTGAAAGTGCGCGTGAT(SEQ ID NO: 13)MO45715′-CACAAGGTACCAGAGACCGGGTTGGCGG(SEQ ID NO: 14)MO45915′-CACAAGCGGCCGCGCTAGCATGGGGATCGATCTCTTATAT(SEQ ID NO: 15)MO45925′-CACAAGCGGCCGCGCTAGCGAATGATTCTTATACTCAGAAG(SEQ ID NO: 16)MO45935′-CACAAGCGGCCGCACGCGTGCAATTAACAGATAGTTTGCC(SEQ ID NO: 17)MO46595′-CACAAGCTAGCTGGGGATGCGATCTCTTATATC 1A: Production of pMB4628 (tef1p-carRP LEU2) and pMB4705 (tef1p-carRP[i − ] LEU2) Encoding Phytoene Synthase/Lycopene Cyclase: Intron-containing carRP was amplified from M. circinelloides (ATCC 90680) genomic DNA using MO4525 and MO4541: (SEQ ID NO: 18)MO45255′-CACAAACGCGTTTAAATGGTATTTAGATTTCTCATT(SEQ ID NO: 19)MO45415′-CACAATCTAGACACAAATGCTGCTCACCTACATGGA and the resulting 1.9 kb fragment was phosphorylated with T4 polynucleotide kinase. The resulting fragment was blunt-end ligated into pBluescriptSKII− cleaved with EcoRV, yielding pMB4599. The 1.9 kb XbaI-MluI fragment from pMB4599 was inserted into NheI- and MluI-cleaved pMB4603, yielding pMB4628. The intron containing nucleic acid coding sequence, and encoded CarRP protein (assuming correctly predicted splicing) of pMB4628 are as follows: (SEQ ID NO: 20)atgctgctcacctacatggaagtccacctctactacacgctgcctgtgctgggcgtcctgtcctggctgtcgcggccgtactacacagccaccgatgcgctcaaattcaaatttctgacactggttgccttcacgaccgcctccgcctgggacaactacattgtctaccacaaggcgtggtcctactgccccacctgcgtcaccgctgtcattggctacgtgcccttggaggagtacatgttcttcatcatcatgactctgttgaccgtggcattcaccaatctggtgatgcgctggcacctgcacagcttctttatcaggcctgaaacgcccgtcatgcagtccgtcctggtccgtcttgtccccataacagccttattaatcactgcatacaaggcttgggtaagcaaacaaacaaatgatgtgccgcatcgcattttaatattaaccattgcatacacagcatttggcggtccctggaaagccactgttctacggatcatgcattttgtggtacgcctgtccggttttggccttattgtggtttggtgctggcgagtacatgatgcgtcgtccgctggcggtgctcgtctccattgcgctgcccacgctgtttctctgctgggtcgatgtcgtcgctattggcgccggcacatgggacatttcgctggccacaagcaccggcaagttcgtcgtgccccacctgcccgtggaggaattcatgttctttgcgctaattaataccgttttggtatttggtacgtgtgcgatcgatcgcacgatggcgatcctccacctgttcaaaaacaagagtccttatcagcgcccataccagcacagcaagtcgttcctccaccagatcctcgagatgacctgggccttctgtttacccgaccaagtgctgcattcagacacattccacgacctgtccgtcagctgggacatcctgcgcaaggcctccaagtccttttacacggcctctgctgtctttcccggcgacgtgcgccaagagctcggtgtgctatacgccttttgcagagccacggacgatctctgcgacaacgagcaggtccctgtgcagacgcgaaaggagcagctgatactgacacatcagttcgtcagcgatctgtttggccaaaagacaagcgcgccgactgccattgactgggacttttacaacgaccaactgcctgcctcgtgcatctctgccttcaagtcgttcacccgtttgcgccatgtgctggaagctggagccatcaaggaactgctcgacgggtacaagtgggatttggagcgtcgctccatcagggatcaggaggatctcagatattactcagcttgtgtcgccagcagtgttggtgaaatgtgcactcgcatcatactggcccacgccgacaagcccgcctcccgccagcaaacacagtggatcattcagcgtgcgcgtgaaatgggtctggtactccaatatacaaacattgcaagagacattgtcaccgacagcgaggaactgggcagatgctacctgcctcaggattggcttaccgagaaggaggtggcgctgattcaaggcggccttgcccgagaaattggcgaggagcgattgctctcactgtcgcatcgcctcatctaccaggcagacgagctcatggtggttgccaacaagggcatcgacaagctgcccagccattgtcaaggcggcgtgcgtgcggcctgcaacgtctatgcttccattggcaccaagctcaagtcttacaagcaccactatcccagcagagcacatgtcggcaattcgaaacgagtggaaattgctcttcttagcgtatacaacctttacaccgcgccaattgcgactagtagtaccacacattgcagacagggaaaaatgagaaatctaaataccatttaa(SEQ ID NO: 21)mlltymevhlyytlpvlgvlswlsrpyytatdalkfkfltlvafttasawdnyivyhkawsycptcvtavigyvpleeymffiimtlltvaftnlvmrwhlhsffirpetpvmqsvlvrlvpitallitaykawhlavpgkplfygscilwyacpvlallwfgageymmrrplavlvsialptlflcwvdvvaigagtwdislatstgkfvvphlpveefmffalintvlvfgtcaidrtmailhlfknkspyqrpyqhsksflhqilemtwafclpdqvlhsdtfhdlsvswdilrkasksfytasavfpgdvrqelgvlyafcratddlcdneqvpvqtrkeqlilthqfvsdlfgqktsaptaidwdfyndqlpascisafksftrlrhvleagaikelldgykwdlerrsirdqedlryysacvassvgemctriilahadkpasrqqtqwiiqraremglvlqytniardivtdseelgrcylpqdwltekevaliqgglareigeerllslshrliyqadelmvvankgidklpshcqggvraacnvyasigtklksykhhypsrahvgnskrveiallsvynlytapiatsstthcrqgkmrnlnti Alternatively, pMB4599 was also used as a template for PCR amplification using MO4318, MO4643, MO4644, and MO4639: (SEQ ID NO: 22)MO43185′-GTAAAACGACGGCCAGT(SEQ ID NO: 23)MO46435′-CACACGGTCTCATGCCAAGCCTTGTATGCAGTGATTAA(SEQ ID NO: 24)MO46395′-CCACTGTGTTTGCTGGCGG(SEQ ID NO: 25)MO46445′-CACACGGTCTCTGGCATTTGGCGGTCCCTGGAAA producing fragments of 0.5 and 0.95 kb, that were subsequently cleaved with Acc65I and BsaI, and BsaI and PpuMI, respectively. These fragments were ligated to pMB4599 that had been digested with Acc65I and PpuMI, yielding pMB4613, harboring intronless carRP. The 1.85 kb XbaI-MluI fragment from pMB4613 was inserted into NheI- and MluI-cleaved pMB4603 to yield pMB4705. The intronless nucleic acid coding sequence of pMB4705 is as follows, and encodes the same CarRP protein as above: (SEQ ID NO: 26)atgctgctcacctacatggaagtccacctctactacacgctgcctgtgctgggcgtcctgtcctggctgtcgcggccgtactacacagccaccgatgcgctcaaattcaaatttctgacactggttgccttcacgaccgcctccgcctgggacaactacattgtctaccacaaggcgtggtcctactgccccacctgcgtcaccgctgtcattggctacgtgcccttggaggagtacatgttcttcatcatcatgactctgttgaccgtggcattcaccaatctggtgatgcgctggcacctgcacagcttctttatcaggcctgaaacgcccgtcatgcagtccgtcctggtccgtcttgtccccataacagccttattaatcactgcatacaaggcttggcatttggcggtccctggaaagccactgttctacggatcatgcattttgtggtacgcctgtccggttttggccttattgtggtttggtgctggcgagtacatgatgcgtcgtccgctggcggtgctcgtctccattgcgctgcccacgctgtttctctgctgggtcgatgtcgtcgctattggcgccggcacatgggacatttcgctggccacaagcaccggcaagttcgtcgtgccccacctgcccgtggaggaattcatgttctttgcgctaattaataccgttttggtatttggtacgtgtgcgatcgatcgcacgatggcgatcctccacctgttcaaaaacaagagtccttatcagcgcccataccagcacagcaagtcgttcctccaccagatcctcgagatgacctgggccttctgtttacccgaccaagtgctgcattcagacacattccacgacctgtccgtcagctgggacatcctgcgcaaggcctccaagtccttttacacggcctctgctgtctttcccggcgacgtgcgccaagagctcggtgtgctatacgccttttgcagagccacggacgatctctgcgacaacgagcaggtccctgtgcagacgcgaaaggagcagctgatactgacacatcagttcgtcagcgatctgtttggccaaaagacaagcgcgccgactgccattgactgggacttttacaacgaccaactgcctgcctcgtgcatctctgccttcaagtcgttcacccgtttgcgccatgtgctggaagctggagccatcaaggaactgctcgacgggtacaagtgggatttggagcgtcgctccatcagggatcaggaggatctcagatattactcagcttgtgtcgccagcagtgttggtgaaatgtgcactcgcatcatactggcccacgccgacaagcccgcctcccgccagcaaacacagtggatcattcagcgtgcgcgtgaaatgggtctggtactccaatatacaaacattgcaagagacattgtcaccgacagcgaggaactgggcagatgctacctgcctcaggattggcttaccgagaaggaggtggcgctgattcaaggcggccttgcccgagaaattggcgaggagcgattgctctcactgtcgcatcgcctcatctaccaggcagacgagctcatggtggttgccaacaagggcatcgacaagctgcccagccattgtcaaggcggcgtgcgtgcggcctgcaacgtctatgcttccattggcaccaagctcaagtcttacaagcaccactatcccagcagagcacatgtcggcaattcgaaacgagtggaaattgctcttcttagcgtatacaacctttacaccgcgccaattgcgactagtagtaccacacattgcagacagggaaaaatgagaaatctaaataccatttaa 1B: Production of pMB4638 (tef1p-carB ADE1), Encoding Phytoene Dehydrogenase: Intron-containing carB was amplified from M. circinelloides (ATCC 90680) genomic DNA using MO4530 and MO4542: (SEQ ID NO: 27)MO45305′-CACAAACGCGTTTAAATGACATTAGAGTTATGAAC(SEQ ID NO: 28)MO45425′-CACAATCTAGACACAAATGTCCAAGAAACACATTGTC and the resulting 1.9 kb fragment was phosphorylated with T4 polynucleotide kinase and blunt-end ligated into pBS-SKII− cleaved with EcoRV, yielding pMB4606. pMB4606 was then used as a template for PCR amplification using MO4318 and MO4648, and MO4646 and MO4647, and MO4343 and MO4645: (SEQ ID NO: 29)MO43185′-GTAAAACGACGGCCAGT(SEQ ID NO: 30)MO46485′-CACAAGGTCTCAAGCACGCATCCCGGAACTG(SEQ ID NO: 31)MO46465′-CACACGGTCTCAGGCATGTCGCCCTACGATGC(SEQ ID NO: 32)MO46475′-CACACGGTCTCATGCTTGCACCCACAAAGAATAGG(SEQ ID NO: 33)MO43435′-CAGGAAACAGCTATGAC(SEQ ID NO: 34)MO46455′-CACACGGTCTCTTGCCCATATACATGGTCTGAAACG producing fragments of 0.4 and 0.85 and 0.7 kb, that were subsequently cleaved with Acc65I and BsaI, and BsaI, and BsaI and BamHI, respectively. These fragments were ligated to pBS-SKII− that had been cut with Acc65I and BamHI, yielding pMB4619, harboring intronless carB. The 1.75 kb XbaI-MluI fragment from pMB4619 was inserted into NheI- and MluI-cleaved pMB4629, yielding pMB4638. The resulting nucleic acid coding sequence and encoded CarB protein of pMB4638 are as follows: (SEQ ID NO: 35)atgtccaagaaacacattgtcattatcggtgctggcgtgggtggcacggctacagctgctcgtttggcccgcgaaggcttcaaggtcactgtggtggagaaaaacgactttggtggcggccgctgctccttgatccatcaccagggccatcgctttgatcagggcccgtcgctctacctgatgcccaagtactttgaggacgcctttgccgatctggacgagcgcattcaagaccacctggagctgctgcgatgcgacaacaactacaaggtgcactttgacgacggtgagtcgatccagctgtcgtctgacttgacacgcatgaaggctgaattggaccgcgtggagggcccccttggttttggccgattcctggatttcatgaaagagacacacatccactacgaaagcggcaccctgattgcgctcaagaagaatttcgaatccatctgggacctgattcgcatcaagtacgctccagagatctttcgcttgcacctgtttggcaagatctacgaccgcgcttccaagtacttcaagaccaagaagatgcgcatggcattcacgtttcagaccatgtatatgggcatgtcgccctacgatgcgcctgctgtctacagcctgttgcagtacaccgagttcgctgaaggcatctggtatccccgtggcggcttcaacatggtggttcagaagctagaggcgattgcaaagcaaaagtacgatgccgagtttatctacaatgcgcctgttgccaagattaacaccgatgatgccaccaaacaagtgacaggtgtaaccttggaaaatggccacatcatcgatgccgatgcggttgtgtgtaacgcagatctggtctatgcttatcacaatctgttgcctccctgccgatggacgcaaaacacactggcttccaagaaattgacgtcttcttccatttccttctactggtccatgtccaccaaggtgcctcaattggacgtgcacaacatctttttggccgaggcttatcaggagagctttgacgaaatcttcaaggactttggcctgccttctgaagcctccttctacgtcaatgtgccctctcgcatcgatccttctgctgctcccgacggcaaggactctgtcattgtcttggtgcctattggtcatatgaagagcaagacgggcgatgcttccaccgagaactacccggccatggtggacaaggcacgcaagatggtgctggctgtgattgagcgtcgtctgggcatgtcgaatttcgccgacttgattgagcatgagcaagtcaatgatcccgctgtatggcagagcaagttcaatctgtggagaggctcaattctgggtttgtctcatgatgtgcttcaggtgctgtggttccgtcccagcacaaaggattctaccggtcgttatgataacctattctttgtgggtgcaagcacgcatcccggaactggtgttcccattgtccttgcaggaagcaagctcacctctgaccaagttgtcaagagctttggaaagacgcccaagccaagaaagatcgagatggagaacacgcaagcacctttggaggagcctgatgctgaatcgacattccctgtgtggttctggttgcgcgctgccttttgggtcatgtttatgttcttttacttcttccctcaatccaatggccaaacgcccgcatcttttatcaataatttgttacctgaagtattccgcgttcataactctaatgtcatttaa(SEQ ID NO: 36)mskkhiviigagvggtataarlaregfkvtvvekndfgggrcslihhqghrfdqgpslylmpkyfedafadlderiqdhlellrcdnnykvhfddgesiqlssdltrmkaeldrvegplgfgrfldfmkethihyesgtlialkknfesiwdlirikyapeifrlhlfgkiydraskyfktkkmrmaftfqtmymgmspydapavysllqytefaegiwyprggfnmvvqkleaiakqkydaefiynapvakintddatkqvtgvtlenghiidadavvcnadlvyayhnllppcrwtqntlaskkltsssisfywsmstkvpqldvhniflaeayqesfdeifkdfglpseasfyvnvpsridpsaapdgkdsvivlvpighmksktgdastenypamvdkarkmvlavierrlgmsnfadlieheqvndpavwqskfnlwrgsilglshdvlqvlwfrpstkdstgrydnlffvgasthpgtgvpivlagskltsdqvvksfgktpkprkiementqapleepdaestfpvwfwlraafwvmfmffyffpqsngqtpasfinnllpevfrvhnsnvi 1C. Production of pMB4660 (tef1p-carB URA3) Encoding Phytoene Dehydrogenase: The 4.3 kb XhoI-NotI fragment and the 1.8 kb NotI-SpeI fragment from pMB4638 were ligated to the 1.9 kb BsaI- and SpeI-cleaved URA3 gene generated by PCR amplification of Y. lipolytica genomic DNA using MO4684 and MO4685 to create pMB4660: (SEQ ID NO: 37)MO46845′-CATTCACTAGTGGTGTGTTCTGTGGAGCATTC(SEQ ID NO: 38)MO46855′-CACACGGTCTCATCGAGGTGTAGTGGTAGTGCAGTG The resulting nucleic acid coding sequence and encoded CarB(i) protein of pMB4660 are as follows: (SEQ ID NO: 39)atgtccaagaaacacattgtcattatcggtgctggcgtgggtggcacggctacagctgctcgtttggcccgcgaaggcttcaaggtcactgtggtggagaaaaacgactttggtggcggccgctgctccttgatccatcaccagggccatcgctttgatcagggcccgtcgctctacctgatgcccaagtactttgaggacgcctttgccgatctggacgagcgcattcaagaccacctggagctgctgcgatgcgacaacaactacaaggtgcactttgacgacggtgagtcgatccagctgtcgtctgacttgacacgcatgaaggctgaattggaccgcgtggagggcccccttggttttggccgattcctggatttcatgaaagagacacacatccactacgaaagcggcaccctgattgcgctcaagaagaatttcgaatccatctgggacctgattcgcatcaagtacgctccagagatctttcgcttgcacctgtttggcaagatctacgaccgcgcttccaagtacttcaagaccaagaagatgcgcatggcattcacgtttcagaccatgtatatgggcatgtcgccctacgatgcgcctgctgtctacagcctgttgcagtacaccgagttcgctgaaggcatctggtatccccgtggcggatcaacatggtggttcagaagctagaggcgattgcaaagcaaaagtacgatgccgagtttatctacaatgcgcctgttgccaagattaacaccgatgatgccaccaaacaagtgacaggtgtaaccttggaaaatggccacatcatcgatgccgatgcggttgtgtgtaacgcagatctggtctatgcttatcacaatctgttgcctccctgccgatggacgcaaaacacactggcttccaagaaattgacgtcttcttccatttccttctactggtccatgtccaccaaggtgcctcaattggacgtgcacaacattctttttggccgaggcttatcaggagagctttgacgaaatcttcaaggactttggcctgccttctgaagcctccttctacgtcaatgtgccctctcgcatcgatccttctgctgctcccgacggcaaggactctgtcattgtcttggtgcctattggtcatatgaagagcaagacgggcgatgcttccaccgagaactacccggccatggtggacaaggcacgcaagatggtgctggctgtgattgagcgtcgtctgggcatgtcgaatttcgccgacttgattgagcatgagcaagtcaatgatcccgctgtatggcagagcaagttcaatctgtggagaggctcaattctgggtttgtctcatgatgtgcttcaggtgctgtggttccgtcccagcacaaaggattctaccggtcgttatgataacctattctttgtgggtgcaagcacgcatcccggaactggtgttcccattgtccttgcaggaagcaagctcacctctgaccaagttgtcaagagctttggaaagacgcccaagccaagaaagatcgagatggagaacacgcaagcacctttggaggagcctgatgctgaatcgacattccctgtgtggttctggttgcgcgctgccttttgggtcatgtttatgttcttttacttcttccctcaatccaatggccaaacgcccgcatcttttatcaataatttgttacctgaagtattccgcgttcataactctaatgtcatttaa(SEQ ID NO: 40)mskkhiviigagvggtataarlaregfkvtvvekndfgggrcslihhqghrfdqgpslylmpkyfedafadlderiqdhlellrcdnnykvhfddgesiqlssdltrmkaeldrvegplgfgrfldfmkethihyesgtlialkknfesiwdlirikyapeifrlhlfgkiydraskyfktkkmrmaftfqtmymgmspydapavysllqytefaegiwyprggfnmvvqkleaiakqkydaefiynapvakintddatkqvtgvtlenghiidadavvcnadlvyayhnllppcrwtqntlaskkltsssisfywsmstkvpqldvhniflaeayqesfdeifkdfglpseasfyvnvpsridpsaapdgkdsvivlvpighmksktgdastenypamvdkarkmvlavierrlgmsnfadlieheqvndpavwqskfnlwrgsilglshdvlqvlwfrpstkdstgrydnlffvgasthpgtgvpivlagskltsdqvvksfgktpkprkiementqapleepdaestfpvwfwlraafwvmfmffyffpqsngqtpasfinnllpevfrvhnsnvi 1D. Production of pMB4637, pMB4714 and pTef-HMG Encoding a Truncated HMG1. For production of a truncated variant of the HMG-CoA reductase gene, which also encodes a 77 amino acid leader sequence derived from S. cerevisiae , the following oligonucleotides are synthesized: (SEQ ID NO: 41)PRIMER O 5′-TTCTAGACACAAAAATGGCTGCAGACCAATTGGTGA(SEQ ID NO: 42)PRIMER P 5′-CATTAATTCTTCTAAAGGACGTATTTTCTTATC(SEQ ID NO: 43)PRIMER Q 5′-GTTCTCTGGACGACCTAGAGG(SEQ ID NO: 44)MO4658 5′-CACACACGCGTACACCTATGACCGTATGCAAAT Primers O and P are used to amplify a 0.23 kb fragment encoding Met-Ala followed by residues 530 to 604 of the Hmg1 protein of S. cerevisiae , using genomic DNA as template. Primers Q and MO4658 are used to amplify a 1.4 kb fragment encoding the C-terminal 448 residues of the Hmg1 protein of Y. lipolytica , using genomic DNA as template. These fragments are ligated to the appropriate cloning vector, and the resultant plasmids, designated pOP and pQMO4658, are verified by sequencing. The OP fragment is liberated with XbaI and AseI, and the QMO4658 fragment is liberated with MaeI and MluI. These fragments are then ligated to the ADE1 TEF1p expression vector pMB4629 cut with XbaI and MluI to produce pTefHMG. Alternatively, the native HMG1 gene from Y. lipolytica was amplified without S. cerevisiae sequences using primers MO4658 (described above) and MO4657 (5′-CACACTCTAGACACAAAAATGACCCAGTCTGTGAAGGTGG (SEQ ID NO:45)). The 1.5 kb product was phosphorylated and ligated to pBluescriptSK − that had been cleaved with EcoRV to create pMB4623. The XbaI-MluI fragment containing hmg1 trunc was ligated both to NheI-MluI-cleaved MB4629 and to NheI-MluI-cleaved pMB4691 to create pMB4637 and pMB4714, respectively. The resulting nucleic acid coding sequence and encoded Hmg1 trunc protein of pMB4637 and pMB4714 are as follows: (SEQ ID NO: 46)atgacccagtctgtgaaggtggttgagaagcacgttcctatcgtcattgagaagcccagcgagaaggaggaggacacctcttctgaagactccattgagctgactgtcggaaagcagcccaagcccgtgaccgagacccgttctctggacgacctagaggctatcatgaaggcaggtaagaccaagcttctggaggaccacgaggttgtcaagctctctctcgagggcaagcttcctttgtatgctcttgagaagcagcttggtgacaacacccgagctgttggcatccgacgatctatcatctcccagcagtctaataccaagactttagagacctcaaagcttccttacctgcactacgactacgaccgtgtttttggagcctgttgcgagaacgttattggttacatgcctctccccgttggtgttgctggccccatgaacattgatggcaagaactaccacattcctatggccaccactgagggttgtcttgttgcctcaaccatgcgaggttgcaaggccatcaacgccggtggcggtgttaccactgtgcttactcaggacggtatgacacgaggtccttgtgtttccttcccctctctcaagcgggctggagccgctaagatctggcttgattccgaggagggtctcaagtccatgcgaaaggccttcaactccacctctcgatttgctcgtctccagtctcttcactctacccttgctggtaacctgctgtttattcgattccgaaccaccactggtgatgccatgggcatgaacatgatctccaagggcgtcgaacactctctggccgtcatggtcaaggagtacggcttccctgatatggacattgtgtctgtctcgggtaactactgcactgacaagaagcccgcagcgatcaactggatcgaaggccgaggcaagagtgttgttgccgaagccaccatccctgctcacattgtcaagtctgttctcaaaagtgaggttgacgctcttgttgagctcaacatcagcaagaatctgatcggtagtgccatggctggctctgtgggaggtttcaatgcacacgccgcaaacctggtgaccgccatctaccttgccactggccaggatcctgctcagaatgtcgagtcttccaactgcatcacgctgatgagcaacgtcgacggtaacctgctcatctccgtttccatgccttctatcgaggtcggtaccattggtggaggtactattttggagccccagggggctatgctggagatgcttggcgtgcgaggtcctcacatcgagacccccggtgccaacgcccaacagcttgctcgcatcattgcttctggagttcttgcagcggagctttcgctgtgttctgctcttgctgccggccatcttgtgcaaagtcatatgacccacaaccggtcccaggctcctactccggccaagcagtctcaggccgatctgcagcgtctacaaaacggttcgaatatttgcatacggtcatag(SEQ ID NO: 47)mtqsvkvvekhvpiviekpsekeedtssedsieltvgkqpkpvtetrslddleaimkagktklledhevvklslegklplyalekqlgdntravgirrsiisqqsntktletsklpylhydydrvfgaccenvigymplpvgvagpmnidgknyhipmattegclvastmrgckainagggvttvltqdgmtrgpcvsfpslkragaakiwldseeglksmrkafnstsrfarlqslhstlagnllfirfrtttgdamgmnmiskgvehslavmvkeygfpdmdivsvsgnyctdkkpaainwiegrgksvvaeatipahivksvlksevdalvelnisknligsamagsvggfnahaanlvtaiylatgqdpaqnvessncitlmsnvdgnllisvsmpsievgtigggtilepqgamlemlgvrgphietpganaqqlariiasgvlaaelslcsalaaghlvqshmthnrsqaptpakqsqadlqrlqngsnicirs 1E. Production of pMB4692 (URA3 tef1p-crtZ) Encoding N. aromaticovans Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Novosphingobium aromaticivorans , using Y. lipolytica codon bias: (SEQ ID NO: 48)5′-ttctagacacaaaa atgggtggagccatgcagaccctcgctgctatcctgatcgtcctcggtacagtgctcgctatggagtttgtcgcttggtcttctcataagtatatcatgcatggcttcggatggggatggcatagagaccatcacgagccccatgagggatttcttgagaagaatgacttatacgccatcgttggcgctgccctctcgatactcatgtttgccctcggctctcccatgatcatgggcgctgacgcctggtggcccggaacctggatcggactcggtgtcctcttctatggtgtcatctataccctcgtgcacgacggtctggtgcaccaacgatggtttagatgggtgcctaaacgaggttacgccaaacgactcgtgcaggcccataagctgcaccacgccaccattggcaaggaaggaggcgtctcattcggtttcgtgttcgcccgagatcccgccgttctgaagcaggagcttcgagctcaacgagaagcaggtatcgccgtgctgcgagaggctgtggacggctag acgcgt This sequence was cleaved using XbaI and MluI and ligated, along with an Acc65I-NheI TEF1 promoter fragment from pMB4629, to pMB4662 cut with Acc65I and MIA to produce pMB4692. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4692 is as follows: (SEQ ID NO: 49)mggamqtlaailivlgtvlamefvawsshkyimhgfgwgwhrdhhephegflekndlyaivgaalsilmfalgspmimgadawwpgtwiglgvlfygviytlvhdglvhqrwfrwvpkrgyakrlvqahklhhatigkeggvsfgfvfardpavlkqelraqreagiavlreavdg 1F. Production of pMB4698 (ADE1 tef1p-crtW), Encoding Carotene Ketolase Derived from an Environmental Sample. The following carotene ketolase (CrtW) ORF sequence was synthesized de novo, based on protein sequence of an environmental sequence isolated from the Sargasso Sea (Genbank accession AACY01034193.1): (SEQ ID NO: 50)5′-ttctagacacaaaa atgactcgatctatttcctggccttccacctactggcacctccagccctcctgttcttcttgggtcgcaaacgaattctctcctcaagcccgaaaaggtctcgtcctcgctggtctcattggttccgcttggctgcttactctcggacttggcttttcccttcccctccatcaaacgagctggcttctcatcggttgtctcgttctccttagatctttcctgcacaccggactttttatcgttgcccatgacgctatgcacgcttctcttgttcctgaccaccctggccttaaccgttggattggacgtgtctgtcttctcatgtatgctggactctcctacaaaagatgctgccgaaatcaccgtcgacaccaccaagcccctgaaacagttgaagaccctgactaccaacgatgcactaacaacaatatcctcgactggtacgttcactttatgggaaattacctcggatggcaacaattgcttaatctctcttgcgtttggctcgctctcaccttccgtgtttctgactactctgctcaattcttccacctgctccttttctctgtccttcctctcatcgtctcctcctgtcaactcttcctcgtgggaacctggctgccacaccgacgaggcgctactactcgacccggcgttaccactcgatccctgaacttccaccctgctctttccttcgctgcttgctaccacttcggttaccaccgtgaacaccatgaatctccctctactccttggttccaacttcctaaactccgagaaggttctctcatctaa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4698. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4698 is as follows: (SEQ ID NO: 51)mtrsiswpstywhlqpscsswvanefspqarkglvlagligsawlltlglgfslplhqtswlligclvllrsflhtglfivahdamhaslvpdhpglnrwigrvcllmyaglsykrccrnhrrhhqapetvedpdyqrctnnnildwyvhfmgnylgwqqllnlscvwlaltfrvsdysaqffhlllfsvlplivsscqlflvgtwlphrrgattrpgvttrslnfhpalsfaacyhfgyhrehhespstpwfqlpklregsli Mutant alleles of this protein (e.g. L200M, F238L/I/V, including combinations thereof) can also be constructed and tested. 1G. Production of pMB4741 (ADE1 tef-crtW), Encoding Aurantimonas Carotene Ketolase. The following carotene ketolase (CrtW) ORF sequence was synthesized de novo based on protein sequence of Aurantimonas sp. 5185-9A1, using Y. lipolytica codon bias: (SEQ ID NO: 52)ctctagacacaaaa atgtcttcctttgcccctatgaatgatgttgctattcctgccggtcaagctcctttctctgcctgtactagaaaacctgtcctgagaccttttcaagctgccatcggtcttacactcgccggatgtgttatctctgcttggattgcaatccacgttggagctgtctttttcctcgatgtcggttggcgaacccttcctgttgttcctgtcctcattgccgttcagtgctggctcacggtcggtctttttattgtcgcacacgatgctatgcacggctccctcgctcctggttggccacgacttaacgctcgaattggtgccttcatcctcaccatctacgctggattcgcttggagacgtgtccgaggagctcacatggcccatcacgacgcccctggtactgccgatgaccctgacttctttgttgatgaacctgaccgattttggccttggtttcgagctttcttccttagatattttggacgtcgatctattctctttgtttgcacagttgtcaccgtttacattctggtccttggagcccctgttcttaatgttgttctcttttacggtcttccttcccttctgtcttctcttcaactcttttactttggaacttttcgtcctcaccgtcatgaagaagatgatttcgttgacgcccataatgcccgatctaatgaatttggttacatcgcctccctcctttcttgctttcactttggataccatcacgaacatcatgccgagccgtgggtcccttggtggggtcttccttctcaatggcgccagagacaagcctcttcttcccgacaggtcccgggcggccgagacgctgctgacgccgctggagcatctcgacaacctgccggacgataccgatctgtttcttctcgaggtcgaaatcaggcccgttctcccgcttctggtcgaaacgaacaaatgagataa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4741. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4741 is as follows: (SEQ ID NO: 53)mssfapmndvaipagqapfsactrkpvlrpfqaaigltlagcvisawiaihvgavffldvgwrtlpvvpvliavqcwltvglfivahdamhgslapgwprlnarigafiltiyagfawrrvrgahmahhdapgtaddpdffvdepdrfwpwfrafflryfgrrsilfvctvvtvyilvlgapvlnvvlfyglpsllsslqlfyfgtfrphrheeddfvdahnarsnefgyiasllscfhfgyhhehhaepwvpwwglpsqwrqrqasssrqvpggrdaadaagasrqpagryrsvssrgrnqarspasgrneqmr Mutant alleles of this protein (e.g. L201M, A232V/I/L, F240L/I/V, including combinations thereof) can also be constructed and tested. 1H. Production of pMB4735 (ADE1 tef-crtW), Encoding P. bermudensis Carotene Ketolase. The following carotene ketolase (CrtW) ORF sequence was synthesized de novo based on protein sequence of Parvularcula bermudensis , using Y. lipolytica codon bias: (SEQ ID NO: 54)ctctagacacaaaa atggaccctaccggagacgttactgctagccctcgacctcaaaccaccattcctgtccgacaagcactctggggacttagccttgctggagccatcatcgccgcatgggtttttatgcacattggtttcgttttttttgccccccttgatcctatcgttctcgccctcgccccagttattattcttcttcaatcctggctttctgttggtctttttattatttctcacgacgcaattctccctcgcccctggacgacccgcctttaatagagccatgggacgactctgcatgacactttacgccggtttcgactttgaccgtatggccgctgcacatcaccgacatcacagatcccctggaaccgccgctgaccccgatttttctgttgactcccctgatcgacctctcccttggtttggagctttcttccgacctactttggctggagaccttttcttaccgttaacgctgtcgtctttacctactggcttgttcttggagctaaccctgttaatattgttctcttttatggcgttcctgcactcctttccgccggacagctattttactttggtacatttctccctcaccgacacgaacgacaaggctttgctgatcaccaccgagcacgatccgtccgatccccttacatgctttctcttgttacttctaccactttggaggctatcatcacgaacatcatctctttccacacgaaccctggtggcgcctgcctcaacgaggaggttgggaacgtgacagacgaaagagaaccggcccttaa cgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4629 cut with NheI and MluI to produce pMB4735. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtW protein of pMB4735 is as follows: (SEQ ID NO: 55)mdptgdvtasprpqttipvrqalwglslagaiiaawvfmhigfvffapldpivlalapviillqswlsvglfiishdaihgslapgrpafnramgrlcmtlyagfdfdrmaaahhrhhrspgtaadpdfsvdspdrplpwfgaffrryfgwrpfltvnavvftywlvlganpvnivlfygvpallsagqlfyfgtflphrherqgfadhhrarsvrspymlslvtcyhfggyhhehhlfphepwwrlpqrggwerdrrkrtgp Mutant alleles of this protein (e.g. L190M, M110I/V/L, F229L/I/V, including combinations thereof) can also be constructed and tested. 1I. Production of pMB4778 (URA3 tef-crtZ), Encoding P. bermudensis Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Parvularcula bermudensis , using Y. lipolytica codon bias: (SEQ ID NO: 56)ctctagacacaaaa atgactctcgctctctggcaaagatcaccctcgtccttggttccgctgctctgatggaaggatttgcttggtgggcccatagatatattatgcacggttggggatgggcttggcatagagatcatcatgaacctcacgacaaagtttttgaaaaaaatgacctgtttgctgtggtttttggctcgttcgcatttggtttgttcatcgtcggttacctttattggccacctgtttggtacgttgctgctggcatcactctttacggacttctttacgcatttgttcatgacggtttggttcatcaacgttggccctggcatttcatgcctaaacgaggatacctccgaagactggttcaagctcacaaacttcatcatgctgttacaacacaaggcggaaatgtttcgtttggattcgtccttgcccctgaccctagacatcttagagaaaaacttagacaatttcgtgctgaaagacatcgtgcccttgccgccgaaggtgcttcctcctctgaccctcgtgttccccattttcgaaaagttcaagacgtttaa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4751 cut with NheI and MluI to produce pMB4778. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4778 is as follows: (SEQ ID NO: 57)mtlalwqkitlvlgsaalmegfawwahryimhgwgwawhrdhhephdkvfekndlfavvfgsfafglfivgylywppywyvaagitlygllyafvhdglvhqrwpwhfmpkrgylrrlvqahklhhavttqggnvsfgfvlapdprhlreklrqfraerhralaaegasssdprvppfrkvqdv 1J. Production of pMB4719 (URA3 tef-crtZ), Encoding E. litoralis Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Erythrobacter litoralis , using Y. lipolytica codon bias: (SEQ ID NO: 58)ctctagacacaaaa atgagctggtgggctatcgctcttattgtctttggtgctgtcgttggaatggaattttttgcttggttcgctcataagtacattatgcatggttggggatggagctggcaccgagatcatcacgaacctcacgataatactcttgaaaaaaacgaccttttcgccgttgtctttggctcggttgccgcacttctgtttgttattggagctctctggtctgatcctctctggtgggcagcagttggtattacattgtatggcgtcatttacactctggttcacgacggacttgttcatcaacgttactggcgttggacccctaagcgaggttatgctaagagacttgtccaggcccatcgacttcatcacgctactgttggaaaggaaggaggtgtttcttttggttttgtgttcgcccgagatcctgctaagttgaaagccgaattgaaacaacaaagagaacagggacttgccgtcgttcgagattctatgggagcataa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4719. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4719 is as follows: (SEQ ID NO: 59)mswwaialivfgavvgmeffawfahkyimhgwgwswhrdhhephdntlekndlfavvfgsvaallfvigalwsdplwwaavgitlygviytlvhdglvhqrywrwtpkrgyakrlvqahrlhhatvgkeggvsfgfvfardpaklkaelkqqreqglavvrdsmga 1K. Production of pMB4812, Encoding N. crassa Phytoene Synthase/Lycopene Cyclase, al-2. Exon 1 of al-2 was synthesized by annealing the following oligonucleotides: (SEQ ID NO: 60)MO5017: 5′-CTAGACACAAAAATGTACGACTACGCCTTCGT;(SEQ ID NO: 61)MO5018: 5′-GCACCTGAAGTTCACCGTGCCCGCGGTTCCAA;(SEQ ID NO: 62)MO5019: 5′-GTGCACGAAGGCGTAGTCGTACATTTTTGTGT;(SEQ ID NO: 63)MO5020: 5′-CGCGTTGGAACCGCGGGCACGGTGAACTTCAG, and ligating them to pMB4603 that had been cleaved with NheI and MluI, to create pMB4811. Exon2 was amplified from N. crassa (Fungal Genetic Stock Center #3200) genomic DNA, using MO5016 (5′-CCCGCGGCGGTACTTCT (SEQ ID NO:64)) and MO5013 (5′-CCGTCTCTACAGCAGGATCAGGTCAATGC (SEQ ID NO:65)), and inserted into pCR-TOPO (Invitrogen), to create pMB4809. Exon 3 was similarly amplified with MO5014 (5′-CCGTCTCACTGTACTCCTTCTGTCGCCTG (SEQ ID NO:66)) and MO5015 (5′-CACGCGTCTACTGCTCATACAACGCCCT (SEQ ID NO:67)), and cloned into the same vector to create pMB4810. The 0.9 kb SacII-BsmBI fragment from pMB4809 was ligated together with the 0.9 kb BsmBI-MluI fragment from pMB4810 into SacII-MluI-cleaved pMB4811, to create pMB4812, which expresses al-2 from the TEF1 promoter. The resulting nucleic acid coding sequence and encoded al-2 protein of pMB4812 are as follows: (SEQ ID NO: 68)atgtacgactacgccttcgtgcacctgaagttcaccgtgcccgcggcggtacttctcaccgctatcgcctaccccattctcaacaggatacatctcatccaaacaggcttcctcgtcgtcgtcgcctttaccgccgctctgccatgggatgcctacttgattaagcacaaagtatggtcttacccaccagaagccattgttgggccgcgtttgcttggaattccctttgaagagctgttcttctttgtgatacagacttacatcacggcgctcgtatacatcctcttcaacaagccggtgctgcacgcgttgcacctcaacaatcaacaaaacccgccagcatggatgagggttgtcaaggttaccggccaggtagtcctcgtagccttgtcggtatggggatggaatgccgctcaggttcatcaggaaacaagctatctcggcttgatccttgtttgggcttgtccgttcttactggctatctggaccctcgctgggcgcttcattctcagcctaccctggtacgcgacggtgctcccgatgttcctacccaccttctatctttgggcggtagacgagtttgccttgcacaggggtacttggtccatcggatcggggacgaagctcgatttttgtctgtttggcaagttggacattgaagaagccacgttcttcctggtgaccaacatgctcatcgttggcggtatggccgcgttcgatcaatatctggccgtcatttacgctttcccaactctgttccccaaggtcaaccggtatccgacaactcatatgcttcttcaaagccgtcttatcaacacttccaggtacgatcttgagcgcattgagggcctgagagaagcggtcgagagactgcgcctgaagagcaggagtttttacctggccaattcgctcttttctggtcgactccgcattgacctgatcctgctgtactccttctgtcgcctggctgatgatctagtcgacgacgccaaatctcgccgtgaggtcttgtcctggaccgcgaagctgaaccacttccttgatctgcactacaaggacgcggacgccaccgaggaccccaagaaaaaggcggagcgaatcgacgcctacatcaagacagcgttccctccctgtgcctaccaagccctccacctcctgcccactcacattcttcctcccaagcctctttacgatctcatcaagggtttcgagatggactctcaattcaccttccacggtacttccgactctacggatctccaataccccatcgccgacgacaaggaccttgagaactacgctatctatgtcgccggtaccgtcggcgagctctgcatcgccctcatcatctaccactgcctgccagacatgtcggacactcagaagcgcgagctcgagaccgccgcgtgccggatgggcatcgcgctgcagtacgtcaacatcgctcgtgacatcgtcgtcgacgcacgtatcgggcgcgtttacttgcctaccacctggctcaagaaggaagggttgacgcacaagatggtcttggagaaccccgagggtcccgaggtcattgagcggatgagaagacggcttttggaaaatgcgtttgagctgtatgggggcgcgaggcctgagatgcaacggataccgagcgaggctaggggcccgatgattggtgccgttgaaaattacatggcgattggaagggtgttgagggagaggaaggaggggacggtgtttgtgaggatggaggggagggctacggtcccgaagcgaaggaggttgagcacgctgttgagggcgttgtatgagcagtag;(SEQ ID NO: 69)mydyafvhlkftvpaavlltaiaypilnrihliqtgflvvvaftaalpwdaylikhkvwsyppeaivgprllgipfeelfffviqtyitalvyilfnkpvlhalhlnnqqnppawmrvvkvtgqvvlvalsvwgwnaaqvhqetsylglilvwacpfllaiwtlagrfilslpwyatvlpmflptfylwavdefalhrgtwsigsgtkldfclfgkldieeatfflvtnmlivggmaafdqylaviyafptlfpkvnryptthmllqsrlintsrydlerieglreaverlrlksrsfylanslfsgrlridlillysfcrladdlvddaksrrevlswtaklnhfldlhykdadatedpkkkaeridayiktafppcayqalhllpthilppkplydlikgfemdsqftfhgtsdstdlqypiaddkdlenyaiyvagtvgelcialiiyhclpdmsdtqkreletaacrmgialqyvniardivvdarigrvylpttwlkkeglthkmvlenpegpeviermrrrllenafelyggarpemqripseargpmigavenymaigrvlrerkegtvfvrmegratvpkrrrlstllralyeq 1L. Production of pMB4846 (URA3 tef-crtZ), Encoding an Erythrobacter Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Erythrobacter sp. NAP1, using Y. lipolytica codon bias: (SEQ ID NO: 70)ctctagacacaaaa atgtcttggcctgccgctattgcagttacacttggtgcccttatttttatggaattctttgcttggtacgctcacaaatacattatgcatggatggggatggggttggcacagagaccatcacgaacctcacgacaacaaactggaaaaaaatgacctgttcgctgtggttttcggaacaattaacgctggtatgtatatttttggtgctctttattgggatgctttgtggtgggctgcacttggagttaatctttacggagtgatttacgcccttgttcatgacggactggttcatcaaagatttggaagatacgtccctaaaaacgcatacgctaaacgacttgttcaagcacacagattgcatcacgctactatcggtaaagaaggaggagtgtccttcggattcgttcttgctcgagaccctgctaaacttaaagccgaacttaaacgacaatctcaatccggagaagctattgttcgagaatccgccggagcctaa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4846. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4846 is as follows: (SEQ ID NO: 71)mswpaaiavtlgalifmeffawyahkyimhgwgwgwhrdhhephdnklekndlfavvfgtinagmyifgalywdalwwaalgvnlygviyalvhdglvhqrfgryvpknayakrlvqahrlhhatigkeggvsfgfvlardpaklkaelkrqsqsgeaivresaga 1M. Production of pMB4835 (URA3 tef-crtZ), Encoding an S. alaskensis Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was synthesized de novo based on protein sequence of Sphingopyxis alaskensis , using Y. lipolytica codon bias: (SEQ ID NO: 72)ctctagacacaaaa atgagccaccgaagagatccaggacttagaagagacgacgcacgatctatggcctcctgtctcagacgagcttacaacccccacatgtccctgcctgcaattttgtttttggttcttgctactgtcattgcaatggaaggagtcgcctgggcatcccacaaatacatcatgcacggatttggatgggcctggcacagagaccaccatgaaccccacgacaatcgactcgagaaaaacgacctgtttgccctgttcggagccgctatgtctatttctgccttcgctattggttctcctatgattatgggtgcagctgcctggaagcctggaacttggattggacttggtattcttctttacggtattatctacacactcgttcacgacggccttgtgcaccaaagatactttcgatgggtcccacgacgaggttacgcaaaacgacttgttcaagcacacaaacttcatcacgctacaatcggaaaagagggaggagtttctttcggatttgtttttgctcgtgaccctgctaaacttaaagccgaactgaaagcacaacgagaagctggtattgcagtcgtcagagaagcccttgctgactaa acgcgt This sequence was cleaved using XbaI and MluI and ligated to pMB4691 cut with NheI and MluI to produce pMB4835. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4835 is as follows: mshrrdpglrrddarsmasclrraynphmslpailflylatviamegvawashkyimhgfgwawhrdhhephdnr lekndlfalfgaamsisafaigspmimgaaawkpgtwiglgillygiiytivhdglvhqryfrwvprrgyakrlvqahklhhatigkeggvsfg fvfardpaklkaelkaqreagiavvrealad (SEQ ID NO:73) 1N. Production of pMB4845 (URA3 tef-crtZ), Encoding an R. biformata Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Robiginitalea biformata : (SEQ ID NO: 74)cacaatctagacacaaaa atgacagtcttgatttggatcgcaattttcctggccaccttctgcttcatggaattcatggcctggtttacgcataaatatatcatgcacggtttcctctggagccttcataaggaccaccataaaaaggaccacgacagttggtttgagcgaaacgacgccttctttctattttatgcgatagtctccatgtcctttatcggggccgccgtgaacacgggattctggcaggggtggcccatcggcctgggcatcctcgcttacgggattgcctactttatcgtacacgatatctttatccatcagcggttcaagctctttcgcaatgcgaataactggtacgcgcggggtatccgcagggcccataaaatccaccacaagcacctgggaaaagaggaaggggaatgcttcgggatgctgtttgtcccatttaagtacttccggaagacctga acgcgtttgtg This sequence was phosphorylated and ligated to pBluescriptSK − that had been cleaved with EcoRV and dephosphorylated, to create pMB4824. The XbaI-MluI fragment from pMB4824 that contains crtZ was ligated to pMB4691 cut with NheI and MluI to produce pMB4845. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4845 is as follows: (SEQ ID NO: 75)mtvliwiaiflatfcfmefmawfthkyimhgflwslhkdhhkkdhdswferndafflfyaivsmsfigaavntgfwqgwpiglgilaygiayfivhdifihqrfklfrnannwyargirrahkihhkhlgkeegecfgmlfvpfkyfrkt 1O. Production of pMB4837 (URA3 tef-crtZ), Encoding an X. autotrophicus Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Xanthobacter autotrophicus : (SEQ ID NO: 76)cacaatctagacacaaaa atgtccaccagcctcgccttcctcgtcaacgcgctcatcgtgatcgccacggtcgccgccatggaaggggtggcctgggccgcgcacaaatatgtcatgcacggcttcggctggggctggcacaagtcccaccacgagccgcgcgagggcgtgttcgagcgcaacgacctttatgcgctgctgttcgcaggcatcgccatcgccctcatctacgcgttccgcaatggcggcgcgctgctgtgggtgggcgtggggatgacggtctacggcttcctttatttcttcgtgcacgacggcatcacccaccagcgctggccgttccgctacgtgccgcgcaacggctatctcaagcgcctggtgcaggcccaccggctgcaccatgcggtggatggcaaggagggctgcgtctccttcggcttcatctatgccccgccgcctgccgacctgaaggccaagctgaagaagctgcacggcagcctgaacagaacgaggcggcggaatag acgcgtttgtg This sequence was phosphorylated and ligated to pBluescriptSK − that had been cleaved with EcoRV and dephosphorylated, to create pMB4823. The XbaI-HindIII (filled in with Klenow) fragment from pMB4823 that contains crtZ was ligated to pMB4691 cut with NheI and MluI (filled in with Klenow) to produce pMB4837. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4837 is as follows: mstslaflvnaliviatvaamegvawaahkyvmhgfgwgwhkshhepregvferndlyallfagiaialiyafrngg allwvgvgmtvygflyffvhdgithqrwpfryvprngylkrlvqahrlhhavdgkegcvsfgfiyapppadlkaklkklhggslkqneaae (SEQ ID NO:77) 1P. Production of pMB4850 (URA3 tef-crtZ), Encoding a P. putida Carotene Hydroxylase. The following carotene hydroxylase (CrtZ) ORF sequence was amplified from genomic DNA extracted from Pseudomonas putida (this sequence encodes a valine rather than a leucine at the second position, due to N-end rule considerations): (SEQ ID NO: 78)tctctctagacacaaaa atggtgttcaatctcgccatattgttcggcaccctggtggccatggagggcgttggtacgctggctcacaagtacatcatgcatggctggggctggtggctgcaccgatcgcaccatgagccacacctgggcatgctcgaaaccaacgacctgtacctggtggccctggggctgatcgccacggcgctggtggcgctgggcaaaagtggttatgcgcctttgcagtgggtgggcggtggtgtggcaggctatggagcactgtatgtactggcccacgacggtttctttcaccggcactggccgcgcaagccgcggccggtcaaccgctacctgaaacgcttgcaccgcgcgcaccgcttgcaccatgcggtgaaggggcgcacggggagcgtgtcgttcgggttcttctatgcgccgccgctgaaggtgttgaagcagcaattgcgcagcaggcgcagccaatcgtga acgcgtgagacgttgtg This sequence was phosphorylated and ligated to pBluescriptSK − that had been cleaved with EcoRV and dephosphorylated, to create pMB4847. The XbaI-MluI fragment from pMB4847 that contains crtZ was ligated to pMB4691 cut with NheI and MluI to produce pMB4850. The nucleic acid coding sequence is depicted in bold underline above. The resulting encoded CrtZ protein of pMB4850 is as follows: (SEQ ID NO: 79)mvfnlailfgtlvamegvgtlahkyimhgwgwwlhrshhephlgmletndlylvalgliatalvalgksgyaplqwvgggvagygalyvlahdgffhrhwprkprpvnrylkrlhrahrlhhavkgrtgsvsfgffyapplkvlkqqlrsrrsqs Example 2 Engineering Yarrowia lipolytica for Increased Carotenoid Production 2A. Production of Y. lipolytica Expressing Geranylgeranylpyrophosphate Synthase and Phytoene Dehydrogenase: MF350 (MATB ura2-21 leu2-35 ade1) was transformed with pMB4591 (tef1p-GGS1) that had been cleaved upstream of URA5 with SspI; a Ura + transformant carrying the plasmid at the ura2 locus was identified and named MF364. It was subsequently transformed with pMB4638 (tef1p-carB) that had been cleaved at ADE1 with SspI and a prototrophic transformant was chosen that harbored the plasmid at the ade1 locus. This strain was named MF502. 2B. Production of Y. lipolytica Expressing Geranylgeranylpyrophosphate Synthase, Phytoene Dehydrogenase and Phytoene Synthase/Lycopene Cyclase MF502 was transformed with pMB4705 (tef1p-carRP[i − ]) that had been treated with SspI. Ninety percent of the prototrophic transformants were very orange on YPD agar plates, and one, MF719, produced greater than 10 mg carotene per g dry cell weight (DCW) after four days of growth in YPD at 30° C. 2C. Production of Y. lipolytica Expressing Phytoene Synthase/Lycopene Cyclase and Phytoene Dehydrogenase: ATCC201249 (MATA ura3-302 leu2-270 lys8-11) was transformed with SspI-cleaved pMB4628. Hundreds of Leu + colonies were pooled, re-grown, and transformed with pMB4660 (tef1p-carB) that had been cleaved upstream of URA3 with SalI. One colony that was noticeably yellow after 5 days at 30° C. on YNBglut media (per liter: 1.7 g yeast nitrogen base, 1 g monosodium glutamate, 1% glucose) plus 0.6 mM lysine was selected, named MF447, and found to produce 0.2 mg carotene per gram dry cell weight after 4 days of growth in YPD. MF447 was challenged with 1 g/L 5-fluoroorotic acid and Ura − segregants selected. Surprisingly, they were all found to retain the identical yellow appearance of their parent, implying that the loss of a functional URA3 gene did not coincide with the loss of a functional CarB enzyme. Southern analysis demonstrates that two fragments from a KpnI-HindIII digest of MF447 DNA contain URA3p-hybridizing sequences, only one of which also hybridizes to carB. The other is absent in MF578, the Ura3 − segregant chosen for further manipulation. Plasmid rescue and analysis of the DNA sequence surrounding tef-carB in MF578 confirmed the absence of nearby URA3 sequences. Plasmid rescue and analysis of the DNA sequence encompassing the carRP intron in MF447 revealed that exons 1 and 2 were contiguous and were each separated by an intron sequence that lacked the original internal SspI site (present in pMB4628). The sequence of this region shows a seven-base pair deletion (AATATTA) that would restore the proper frame to an unspliced message. Partial intron sequence comprising the sequence where the deletion occurred is shown as follows: (SEQ ID NO: 80)ACAAACAAATGATGTGCCGCATCGCATTTTAATATTAACCATTGCATACACAG . Predicted partial amino acid sequence comprising this intron, if unspliced, is as follows: (SEQ ID NO: 219)KAW VSKQTNDVPHRILIPLHTQ HLA ....(VSKQTNDVPHRILIPLHTQ is intron encoded) 2D. Production of Y. lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase: MF578 was transformed with pMB4683 (tef1p-GGS1) that had been cleaved with SalI (upstream of URA3) or with StuI (within the GGS1 ORF). Ura + Leu + colonies in both cases appeared bright orange on YNBglut+Lysine and on YPD, and several produced greater than 4 mg carotene per gram of dry cell weight when grown as above. One, MF633, contained a single copy of the plasmid at the GGS1 locus, as inferred from Southern analysis. The others arose by non-homologous or more complex integrations. 2E. Production of Y. lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase: MF364 was crossed with MF578, and spores from the resulting diploid were plated on YPD for two to three days at 30° C. White Leu − Ade − Ura − colonies were screened for the presence of tefp-carB and tefp-GGS1 and for the absence of tefp-carRP by PCR. Thirteen colonies meeting these criteria, as well as displaying resistance to 5-fluorootic acid, an indication that they harbor the ura3-302 allele, were chosen as hosts for further modifications. One such strain, MF731, was transformed with pMB4705 cut with BbvCI, and one Leu + orange colony, MF740, produced 6 mg of β-carotene per g DCW after four days of growth in YPD at 30° C. Another tefp-carB tefp-GGS1 strain from the same cross, MF739, was transformed with pMB4705 cut with BbvCI, and one Leu + orange colony, MF746, produced 8 mg of β-carotene per g DCW after four days of growth in YPD at 30° C. When this strain was transformed with pMB4812 (expressing N. crassa al-2 protein) treated with SspI, the Leu + transformants were less orange than parallel pMB4705 Leu + transformants, and after 4 days of growth in YPD, produced about half the amount of β-carotene as pMB4705 transformants. In addition, the pMB4812 transformants produced significant amounts of γ-carotene (˜40% of total carotene.). 2F. Expression of a Truncated Form of HMG-CoA Reductase Results in Increased Carotenoid Production in Y. lipolytica Expressing Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase, and Geranylgeranylpyrophosphate Synthase: In order to increase carotenoid production, carbon flow through the isoprenoid pathway is enhanced by introducing a truncated variant of the HMG-CoA reductase gene. MF740 was transformed with pMB4637 treated with SnaBI, and Ade + colonies were selected. One such colony, MF760, was shown to produce about 20 mg β-carotene per g DCW after four days of growth in YPD at 30° C. This strain was also the subject of several fermentor studies outlined in Example 5. In addition, MF740 was also transformed with MB4714 treated with AflII and Ura + colonies, were selected. One such colony was designated MF779 (see Example 2G). MF746 was also transformed with pMB4637 treated with SnaBI, and Ade + colonies were selected. One such colony, MF946, was shown to produce greater than 35 mg β-carotene per g DCW after four days of growth in YPD at 30° C. MF760 was also transformed with pMB4691 (empty vector) cut with SalI, creating the prototroph MF858. 2G. Production of Y. lipolytica Expressing Carotene Ketolase, a Truncated Form of HMG-CoA Reductase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase: MF779 was transformed with either pMB4735 or pMB4741 cleaved with SnaBI, and a red prototrophic colony was chosen from each transformation: MF838 (pMB4735) and MF840 (pMB4741). After 4 days of growth in YPD, MF838 produced 25 mg canthaxanthin per g DCW, and MF840 produced 14 mg canthaxanthin and 30 mg echinenone per g DCW. Only trace levels of β-carotene were produced. These strains are the subject of fermentor studies described in Example 5. In addition, MF740 was transformed with pMB4735 cleaved with SnaBI, and a red Ade + colony was chosen for further manipulation and designated MF889 (See example 2I). 2H. Manipulation of the Y. lipolytica ERG9 Gene to Enhance Carotenoid Production. In order to decrease the expression of Erg9 (squalene synthase) in a carotenoid-producing yeast, pMB4789, containing the following cassette, was constructed using standard molecular techniques. The 4.8 kb fragment contains the Y. lipolytica URA3 gene flanked by the ERG9 ORF and the ERG9 terminator. Thus this fragment comprises the sequence: GATCtcgttctgctcgggtagatc (SEQ ID NO: 82)-ERG9 (promoter and ORF)-gtgctctgcggtaagatcgACTAGTggtgtgttctgtggagcattc (SEQ ID NO:83)-URA3 (promoter, ORF, and terminator)-ccaccactgcactaccactacacCTCGAGCATGCATcaggaaggactctccctgtggt (SEQ ID NO:84)-ERG9 terminator-gtgttatggctctacgtgaagGGGCCC (SEQ ID NO:85). (Capital letters: restriction sites [engineered for assembly]) In addition, it was found that a mutation was generated during cloning that changed the coding sequence of ERG9 as follows: (cccgacgttAtccagaagaac (SEQ ID NO:86); F317I in the encoded protein). Two overlapping fragments from this cassette, a 2.4 kb AlwNI-SmaI fragment and a 1.9 kb AlwNI-AflII fragment, were cotransformed into MF760 and Ura + colonies were selected. PCR analysis showed that one, designated MF921, contains the erg9::URA3 cassette replacing the wild type ERG9 gene. MF921 produced greater than 30 mg β-carotene per g DCW after 4 days of growth at 30° C. in YPD. 2I. Production of Y. lipolytica Expressing Carotene Hydroxylase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase: MF740 was transformed with pMB4837 cleaved with SalI, and a Ura + colony was selected and designated MF1011. MF1011 produced 6 mg of zeaxanthin and 1.5 mg of β-carotene per g DCW after 4 days of growth at 30° C. in YPD. 2J. Production of Y. lipolytica Expressing Carotene Hydroxylase, Carotene Ketolase, Phytoene Synthase/Lycopene Cyclase, Phytoene Dehydrogenase and Geranylgeranylpyrophosphate Synthase: MF889 was transformed with pMB4837 cleaved with SalI, and a prototrophic colony was selected and designated MF1016. MF1016 produced 1.5 mg of astaxanthin and 3 mg of canthaxanthin per g DCW after 4 days of growth at 30° C. in YPD. Example 3 Extraction of Carotenoids 3a: Total Extraction of Carotenoids from Yarrowia lipolytica Cells Yarrowia lipolytica cultures to be tested for carotenoid production were grown in 20 ml YPD medium (1% yeast extract, 2% peptone, 2% glucose) in 125 flasks at 30° C. Following incubation for 72-96 hr, the cultures were harvested by centrifugation and the solvent extractions were performed to determine carotenoid form and quantity. Dry cell weights were determined by transferring 1.8 ml of each culture to an Eppendorf tube, which was then centrifuged to pellet the cells, and then the pellet washed twice with 1 ml water. After the second wash, the cells were resuspended in water and transferred to a pre-weighed snap-cap tube with a hole poked in the top, frozen, and then lyophilized overnight. After drying to constant weight, the tube was weighed in order to calculate dry cell weight (mg dry cell weight/ml). The carotenoid content of the culture was calculated by solvent extraction from 0.25 ml of culture from the same shake flask culture. This 0.25 ml culture sample was transferred to a 2 ml screw-cap tube, the cells pelleted, and the supernatant aspirated. Such pelleted cells may be extracted immediately or frozen at −80° C. and stored. An equal volume of cubic zirconia beads was added to cell pellets, along with 1 ml ice-cold extraction solvent (a 50/50 v/v mix of hexane and ethyl acetate containing 0.01% butylhydroxytoluene (BHT)). The mixture was then agitated (Mini-BeadBeater-8, BioSpec Products, Inc.) at maximum speed for 5 minutes at 4° C. The mixture was then spun at maximum speed for 1 minute, and the supernatant was collected and deposited in a cold 16 ml glass vial. The remaining cell debris was re-extracted at least three times, without the addition of zirconia beads; all supernatants were pooled in the 16 ml glass vial. Following extraction, the glass vial was spun for 5 minutes at 2000 rpm at 4° C. in a Sorvall tabletop centrifuge, and the supernatant was transferred to a new cold 16 ml glass vial. A Speed Vac was used to concentrate the supernatant (room temperature in dark), and the samples were stored at −20° C. or −80° C. until immediately before HPLC analysis. Prior to HPLC analysis, the samples were resuspended in 1 ml ice-cold solvent and then transferred to a cold amber vial. Throughout the protocol, care was taken to avoid contact with oxygen, light, heat, and acids. The use of a hexane:ethyl acetate (50:50) mixture to extract carotenoids efficiently extracted all carotenoids analyzed from Yarrowia even though the carotenoids possessed different polarity levels. For instance, in a strain containing β-carotene, γ-carotene, echinenone, and canthaxanthin, a hexane:ethyl acetate (50:50) mixture efficiently extracted all carotenoids even though echinenone and canthaxanthin, respectively, are progressively more polar than either β-carotene or γ-carotene. Given the high efficiency of extraction observed for all carotenoids with 50:50 hexane:ethyl acetate, these conditions were chosen as a “100%” standard against which the extraction efficiency of other conditions could be compared. 3B. Extraction of β-carotene from Y. lipolytica MF858. Y. lipolytica strain MF858 was grown as described in Example 3a and found to contain β-carotene as the dominant carotenoid. Extraction and breakage with hexane yielded an equal amount of β-carotene as was observed with a 50:50 hexane:ethyl acetate mixture. 3C. Extraction of Mixed Carotenoids from Y. lipolytica MF838. Y. lipolytica strain MF838 (example 2g) had previously been found to contain the following types carotenoids when extracted as described in Example 3a: β-carotene, γ-carotene, echinenone, and canthaxanthin. Extraction with 750 μl of hexane resulted in the following extraction efficiencies for each of the carotenoids (extraction efficiency is reported independently for each of the carotenoid species based on the total amount found by hexane:ethyl acetate extraction): β-carotene (79.3%), γ-carotene (82.4%), echinenone (42.6%), and canthaxanthin (8.0%). When an identical aliquot of MF838 was extracted with 1 ml of ethanol (95%), the extraction efficiency of the same four carotenoids was as follows: β-carotene (53.6%), γ-carotene (71.3%), echinenone (39.9%), and canthaxanthin (28.0%). Thus ethanol can be used to extract both polar and nonpolar carotenoids from fungi (e.g. Y. lipolytica ). Example 4 Quantification of Carotenoid Production by HPLC For carotenoid analysis, samples were resuspended in ice-cold extraction solvent (a 50/50 v/v mix of hexane and ethyl acetate containing 0.01% butylhydroxytoluene (BHT)). An Alliance 2795 HPLC (Waters) equipped with a Waters XBridge C18 column (3.5 pa, 2.1×50 mm) and Thermo Basic 8 guard column (2.1×10 mm) was used to resolve carotenoid at 25° C.; authentic carotenoid samples were used as standards. The mobile phases and flow rates are shown below (Solvent A=Ethyl Acetate; Solvent B=Water; Solvent C=Methanol; Solvent D=Acetonitrile). The injection volume was 10 μL. The detector is a Waters 996 photodiode array detector. The retention times for lipophilic molecules include astaxanthin (1.159 min), zeaxanthin (1.335), β-apo-8′-carotenal (2.86 min), ergosterol (3.11 min), lycopene (3.69 min), β-carotene (4.02 min), Canthaxanthin (2.50 min), Echinenone (3.38 min), and phytoene (4.13 min). Astaxanthin, zeaxanthin, β-apo-8′-carotenal, lycopene, β-carotene, canthaxanthin, and echinenone are detected at 475 nm, whereas ergosterol and phytoene were detected at 286 nm. TABLE 28Retention Times for Lipophilic MoleculesTime (min)Flow (mL/min)% A% B% C% DCurve0.500.020.00.080.03.001.0020.00.00.080.064.501.0080.00.020.00.065.001.000.00.0100.00.066.001.000.00.0100.00.066.501.000.020.00.080.067.000.500.0200.080.06 Example 5A 2 Liter Fed-Batch Fermentation of β-Carotene Producing Strain MF760 FIG. 9A depicts the production and intracellular accumulation of phytoene and β-carotene by strain MF760 (Example 2F) when grown in fed-batch fermentation on various carbon sources. Fermentation medium and process parameters are described below. Carbon sources used were glucose, glycerol, or olive oil. Feeding was initiated during the early exponential growth phase at a rate of 15.2 ml/hr. This feed rate either continued until feed exhaustion or, when the dissolved oxygen (dO2) level of the culture reached 20% saturation, feed was added to maintain the dO2 at 20% (DO controlled feed). As seen in FIG. 9 a , β-carotene accumulates in all fermentations from 1.5 to 2.2% of DCW weight. Substantial phytoene accumulation was observed in the constant feed fermentations but not in the DO controlled feed fermentations. FIG. 9B depicts dry cell weight accumulation during the course of the fermentations. For each carbon source examined, constant feeding resulted in greater biomass production relative to the DO controlled feed fermentation. This was especially true for the olive oil fed-batch fermentations where the constant feed fermentation reached greater than 150 g/L DCW. This was expected as Y. lipolytica has been reported to accumulate greater than 40% its biomass as lipid when grown on oils under conditions of excess carbon and oxygen limitation (Pananikolaou et al., Appl. Microbiol. Biotechnol. 58:p308, 2002) and was independent of nitrogen concentration. Batch Medium—1 L Carbon Source (one of the following):Glucose60gGlycerol75gOlive Oil50mlYeast Nitrogen Base4.1gw/o Amino Acids and (NH 4 ) 2 SO 4(NH 4 ) 2 SO 46gUracil72mgAntifoam 204 (Sigma catalog A6426)5ml Feed Medium—1 L Carbon Source (one of the following):Glucose500gGlycerol500gOlive Oil500ml(NH 4 ) 2 SO 472gKH 2 PO 413.5gMgSO 45gInositol70mgThiamine10mgUracil900mgTrace Metal Solution40mlFeCl 3 •6H 2 O2.7g/LZnCl 2 •4H 2 O2.0g/LCaCl 2 •2H 2 O2.0g/LNa 2 MoO 4 •2H 2 O2.0g/LCuSO 4 •5H 2 O1.9g/LH 3 BO 30.5g/LMnSO 4 •H 2 O2.23g/LConcentrated HCl10ml/LVitamins Solution40mlPantothenic acid5.4g/LPyridoxine1.4g/LNiacin6.1g/LFolic acid0.04g/LBiotin0.06g/L Fermentation Parameters: pH 5.5, controlledTemp—30° C.Air Flow—1.4 lpmAgitation—1200 rpm Inoculum—200 ml overnight culture grown in YEP+5% glucose Example 5B 2 Liter Fed-Batch of β-Carotene Producing Strain MF760 FIG. 9 c depicts the production and intracellular accumulation of β-carotene by strain MF760 when grown in fed-batch fermentation. In this fermentation, additions of olive oil were combined with a glucose feeding protocol. Medium and process parameters are described below. Both glucose and olive oil were present in the batch medium. Feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 15.2 ml/hr, this feed rate continued until feed exhaustion. 25 ml of olive oil was added at 24, 48, and 72 hr. As shown in FIG. 9 c , this combined glucose and oil feeding protocol resulted in substantially higher DCW production when compared to glucose as the sole carbon source (example 5a). In addition, β-carotene accumulated to over 5% of the DCW at the end of the fermentation, higher then either the glucose or oil fermentations of example 5a. Batch Medium—1 L Glucose40gOlive Oil50mlYeast Nitrogen Base4.1gw/o Amino Acids and (NH 4 ) 2 SO 4(NH 4 ) 2 SO 46gUracil72mgAntifoam 2045ml Feed Medium—1 L Glucose500g(NH 4 ) 2 SO 472gKH 2 PO 413.5gMgSO 45gInositol70mgThiamine10mgUracil900mgTrace Metal Solution40mlVitamins Solution40mlOlive Oil Additions - 25 ml at 24, 48, and 72 hr Fermentation Parameters: pH 5.5, controlledTemp—30° C.Air Flow—1.4 lpmAgitation—1150 rpm Inoculum—200 ml overnight culture grown in YEP+5% glucose 2.5% olive oil Example 5C 2 Liter Fed-Batch of Canthaxanthin Producing Strain MF840 FIG. 9 d depicts the production and intracellular accumulation of canthaxanthin, echinenone and β-carotene by strain 840 (Example 2g) when grown in fed-batch fermentation. Medium and process parameters are described below. Both glucose and olive oil were present in the batch medium. Feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 15.2 ml/hr; this feed rate continued until the dissolved oxygen reached 20%, at which time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation. As seen in FIG. 9 d , the combined total amount of canthaxanthin, echinenone and β-carotene represented over 8% of the DCW at the end of the fermentation and demonstrates the ability of genetically engineered Y. lipolytica to produce and accumulate significant amounts of carotenoids. Batch Medium—1 L Glucose40gOlive Oil50mlYeast Nitrogen Base4.1gw/o Amino Acids and (NH 4 ) 2 SO 4(NH 4 ) 2 SO 46gAntifoam 2045ml Feed Medium—1 L Glucose500g(NH 4 ) 2 SO 472gKH 2 PO 413.5gMgSO 45gInositol70mgThiamine10mgTrace Metal Solution40mlVitamins Solution40ml Fermentation Parameters: pH 5.5, controlledTemp—30° C.Air Flow—1.4 lpmAgitation—1150 rpm Inoculum—200 ml overnight culture grown in YEP+5% glucose+2.5% olive oil. Example 5D 2 Liter Fed-Batch of Canthaxanthin Producing Strain MF838 FIG. 9 e depicts the production and intracellular accumulation of canthaxanthin and echinenone by strain MF838 (Example 2g) in fed-batch fermentation together with DCW levels. This example demonstrates the advantage of a two phase feeding protocol in which the first phase of feeding is designed to maintain excess carbon and oxygen limited conditions, while the second phase of feeding results in oxygen excess conditions via carbon limitation. Fermentations A and B are depicted on FIG. 9 e . Medium and process parameters are described below. In both fermentations, feeding of the glucose containing feed medium was initiated during the early exponential growth phase at a rate of 22.8 ml/hr. In fermentation A, this feed rate continued until the dissolved oxygen reached 20%, at which time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation. In fermentation B, the constant feed rate was maintained such that glucose was in excess, and dO2 level was essential zero, until approximately hour 40 of the fermentation. At that time feed was added to maintain the dO2 at 20% (DO controlled feed) for the remainder of the fermentation. As seen in FIG. 9 e , the extended period of carbon excess and oxygen limitation resulted in higher peak DCW, altered kinetics of canthaxanthin production, and produced a higher final level canthaxanthin—over 3.5% of DCW. Batch Medium—1 L Glucose40gYeast Nitrogen Base8.2gw/o Amino Acids and (NH 4 ) 2 SO 4(NH 4 ) 2 SO 46gAntifoam 2045ml Feed Medium—1 L Glucose500g(NH 4 ) 2 SO 472gKH 2 PO 413.5gMgSO 45gInositol70mgThiamine10mgTrace Metal Solution40mlVitamins Solution40ml Fermentation Parameters: pH 5.5, controlledTemp—30 CAir Flow—1.4 lpmAgitation—1150 rpm Inoculum—200 ml overnight culture grown in YEP+5% glucose Example 6 Introduction of Heterologous Carotene Hydroxylase and Carotene Ketolase Genes into Y. lipolytica Strains Producing Carotenoid for Production of Astaxanthin For introduction of carotene hydroxylase and carotene ketolase into carotenoid producing Y. lipolytica , pMB4692 and pMB4698, described as in Example 1E and 1F above, can be sequentially introduced into MF740 or MF746 (described in Example 2E). For the introduction of pMB4692, the plasmid may be cleaved with SalI or BsrGI to direct integration at the ura3 locus, or with XbaI to promote random integration, selecting for uracil prototrophy. Ura + transformants from MF740 or MF746 harboring pMB4692 are screened for zeaxanthin production in YPD. Zeaxanthin-producing cells are transformed with pMB4698 (which can be cleaved with PpuMI, SspI or BbvCI to direct integration at the ade1 locus, or with EcoRV to promote random integration) and prototrophic colonies are screened for astaxanthin production. Alternatively, the order of plasmid transformation may be reversed wherein pMB4698 is transformed first and transformants are selected for adenine prototrophy. Ade + transformants from MF740 or MF746 harboring pMB4698 are screened for canthaxanthin production. Canthaxanthin-producing MF740[pMB4698] or MF746[pMB4698] cells are transformed with pMB4692 and prototrophic colonies are screened for astaxanthin production. In another approach, the carotenoid ketolase and carotenoid hydroxylase genes from P. marcusii can be introduced into a Leu2 − version of MF740 or MF746, in order to convert β-carotene into astaxanthin. P. marcusii genomic DNA is amplified with two primers. (SEQ ID NO: 87)CrtZfwd: 5′ CACACCGTCTCAAatgaccaatttcctgatcgtcgtc(SEQ ID NO: 88)CrtZrev: 5′ CACACAGATCtcacgtgcgctcctgcgcc, and the resulting fragment is cleaved with BsmBI, modified with the Klenow fragment of DNA polymerase, and cleaved with BglII. This fragment is inserted into PmlI- and BamHI-cleaved pINA1269 (J. Mol. Microbiol. Biotechnol. 2 (2000): 207-216), containing the hp4d promoter, the XPR2 terminator, the selectable LEU2 gene, and sequences necessary for selection and propagation in E. coli . The resulting plasmid “pA” contains sequences encoding carotene hydroxylase from P. marcusii (crtZ gene) (Genbank accession: CAB56060.1) under the control of the hp4d promoter. “pYEG1TEF” is modified by substituting the LIP2 terminator for the XPR2 terminator as follows. pINA1291 is digested with AvrII, modified with the Klenow fragment of DNA polymerase, and cleaved with EcoRI, and the small LIP2t containing fragment is ligated to “pYEG1TEF” that has been digested with SacII, modified with T4 DNA polymerase in the presence of dNTP, and cleaved with EcoRI. The resulting plasmid is named “pYEG1TEF-LIP2t”. In order to amplify the carotenoid ketolase gene, P. marcusii genomic DNA is amplified with two primers. (SEQ ID NO: 89)CrtWfwd: 5′ CACACCCTAGGCCatgagcgcacatgccctgc(SEQ ID NO: 90)CrtWrev: 5′ CACACAAGCTTtcatgcggtgtcccccttg, and the resulting fragment is cleaved with AvrII and HindIII, and inserted into AvrII- and HindIII-cleaved “pYEG1TEF-LIP2t”. The resulting plasmid, “pBt”, contains sequences encoding the carotene ketolase (crtW gene) (Genbank accession: CAB56059.1) under the control of the constitutive TEF1 promoter. In order to combine the two expression cassettes into a single plasmid, “pBt” is cleaved with ClaI, modified with the Klenow fragment of DNA polymerase, and cleaved with EcoRI, and the crtW-containing fragment is isolated, mixed with the phosphorylated oligonucleotide adaptor pair: 5′ AATTCGCGGCCGCT(SEQ ID NO: 91)and5′ AGCGGCCGCG,(SEQ ID NO: 92) cleaved with NotI, and ligated to NotI-digested “pA”. The resulting plasmid, “pABt”, contains both the TEF1p/crtW/LIP2t cassette and the hp4d/crtZ/XPR2t cassette as well as the selectable LEU2 gene. “pABt” can be introduced into MF740 or MF746 and transformants selected for leucine prototrophy. Example 7 Partial Inactivation of Y. lipolytica ERG9 Gene Encoding Squalene Synthase Results in Increased Carotenoid Production 7A. In order to partially inactivate the ERG9 gene encoding squalene synthase, the neighboring FOL3 gene is disrupted, resulting in a folinic acid requirement. This strain is then transformed with a mutagenized fragment of DNA partially spanning the two genes, and Fol + transformants are screened for decreased squalene synthase activity. The following oligonucleotides are synthesized: (SEQ ID NO: 93)PRIMER K 5′-CCTTCTAGT CGTACG TAGTCAGC;(SEQ ID NO: 94)PRIMER L 5′-CCACTGA TCTAGA ATCTCTTTCTGG and used to amplify a 2.3 kb fragment from Y. lipolytica genomic DNA spanning most of the FOL3 gene, using Pfu polymerase. The resulting fragment is cleaved with XbaI and phosphorylated, then ligated into pBluescriptSK − that has been cleaved with KpnI, treated with T4 DNA polymerase (T4pol) in the presence of dNTPs, and subsequently cleaved with XbaI. The resultant plasmid, designated pBS-fol3, is then cleaved with Acc65I and EcoRI, treated with T4pol as above, and ligated to the 3.4 kb EcoRV-SpeI ADE1 fragment (treated with T4pol) from pMB4529. The resulting plasmid, pBSfol3Δade, can be cleaved with BsiWI and XbaI to liberate a 5.5 kb fragment that is used to transform MF740 or MF746 to adenine prototrophy. Resulting Ade + transformants are screened for a folinic acid requirement, and for homologous integration by PCR analysis. Strains that harbor the resultant fol3ΔADE1 allele can be transformed with a 3.5 kb DNA fragment generated by mutagenic PCR amplification using the primers: (SEQ ID NO: 95)PRIMER M 5′-GGCTCATTGCGCATGCTAACATCG;(SEQ ID NO: 96)PRIMER N 5′-CGACGATGCTATGAGCTTCTAGACG, and Y. lipolytica genomic DNA as template. The resulting fragment containing the N-terminal three-quarters of the FOL3 ORF and the C-terminal nine-tenths of the ERG9 ORF is used to transform strains. The resulting Fol + Ade − transformants are screened for decreased squalene synthase activity by sensitivity to agents such as zaragozic acid, itraconazole, or fluconazole. Additionally, the resulting transformants are screened for increased carotenoid production. 7B. Alternatively, the PCR fragment produced in 7A could be cloned and altered in such a way as to remove the 3′-untranslated region of ERG9 gene. Replacement of the fol3ΔADE1 disruption by this fragment results in decreased expression of squalene synthase [Schuldiner et al. (2005), Cell 123:507-519] [Muhlrad and Parker (1999), RNA 5:1299-1307], which can be confirmed as in 7A. This approach may also be used in a Fol + Ade − strain, using the ADE1 marker to disrupt the ERG9 3′-UTR. 7C. In still another approach, partially defective ERG9 alleles can be identified in S. cerevisiae using plasmid shuffling techniques [Boeke et al. (1987), Methods Enzymol. 154:164-175], and using drug sensitivities as a phenotype. Defective genes can be transferred to Y. lipolytica using standard molecular genetic techniques. Example 8 Treatment of Y. lipolytica Strains Producing Carotenoid with Inhibitor of an Isoprenoid Biosynthesis Competitor Polypeptide Results in Increased Carotenoid Production Cultures produced in Example 2 are treated with the squalene synthase inhibitor, zaragozic acid (zaragozic acid at 0.5 μM) and monitored for β-carotene production, as described above. Example 9 Constructing an Oleaginous Strain of Saccharomyces cerevisiae The genes encoding the two subunits of ATP-citrate lyase from N. crassa , the AMP deaminase from Saccharomyces cerevisiae , and the cytosolic malic enzyme from M. circinelloides are overexpressed in S. cereviseae strains in order to increase the total lipid content. Similar approaches to enhance lipid production could be employed in other host organisms such as Xanthophyllomyces dendrorhous ( Phaffia rhodozyma ), using the same, homologous, or functionally similar oleaginic polypeptides. Qiagen RNAEasy kits (Qiagen, Valencia, Calif.) are used to prepare messenger RNA from lyophilized biomass prepared from cultures of N. crassa . Subsequently, RT-PCR is performed in two reactions containing the mRNA template and either of the following primer pairs. acl1: (SEQ ID NO: 97)1fwd: 5′ CACACGGATCCTATAatgccttccgcaacgaccg(SEQ ID NO: 98)1rev: 5′ CACACACTAGttaaatttggacctcaacacgacccacl2:(SEQ ID NO: 99)2fwd: 5′ CACACGGATCCAATATAAatgtctgcgaagagcatcctcg(SEQ ID NO: 100)2rev: 5′ CACACGCATGCttaagcttggaactccaccgcac The resulting fragment from the acl1 reaction is cleaved with SpeI and BamHI, and that from the acl2 reaction is cleaved with BamHI and SphI, and both are ligated together into YEp24 that has been digested with NheI and SphI, creating the plasmid “p12”. The bi-directional GAL1-10 promoter is amplified from S. cerevisiae genomic DNA using the primers. (SEQ ID NO: 101)gal10: 5′ CACACGGATCCaattttcaaaaattcttactttttttttggatggac(SEQ ID NO: 102)gal1: 5′ CACACGGATCCttttttctccttgacgttaaagtatagagg, and the resulting 0.67 kb fragment is cleaved with BamHI and ligated in either orientation to BamHI-digested “p12” to create “p1gal2” and “p2gal1”, containing GAL1-acl1/GAL10-acl2 and GAL10-acl1/GAL1-acl2, respectively (Genbank accession: acl1: CAB91740.2; acl2: CAB91741.2). In order to amplify the S. cereviseae gene encoding AMP deaminase and a promoter suitable for expressing this gene, S. cerevisiae genomic DNA is amplified using two primer pairs in separate reactions: AMD1 ORF:(SEQ ID NO: 103)AMD1FWD: 5′ CACACGAGCTCAAAAatggacaatcaggctacacagag(SEQ ID NO: 104)AMD1rev: 5′ CACACCCTAGGtcacttttcttcaatggttctcttgaaattgGAL7p:(SEQ ID NO: 105)gal7prox: 5′ CACACGAGCTCggaatattcaactgtttttttttatcatgttgatg(SEQ ID NO: 106)gal7dist: 5′ CACACGGAtccttcttgaaaatatgcactctatatcttttag, and the resulting fragment from the AMD1 reaction (2.4 kb) is cleaved with SacI and AvrII, and that from the GAL7 reaction (0.7 kb) is cleaved with BamHI and SphI, and both are ligated together into YEp13 that has been digested with NheI and BamHI, creating the plasmid “pAMPD”. This plasmid carries the S. cerevisiae gene, AMD1, encoding AMP deaminase, under the control of the galactose-inducible GAL7 promoter. Messenger RNA is prepared from lyophilized biomass of M. circinelloides , as described above, and the mRNA template is used in a RT-PCR reaction with two primers: (SEQ ID NO: 107)MAEfwd: 5′ CACACGCTAGCTACAAAatgttgtcactcaaacgcatagcaac(SEQ ID NO: 108)MAErev: 5′ CACACGTCGACttaatgatctcggtatacgagaggaac, and the resulting fragment is cleaved with NheI and SalI, and ligated to XbaI- and XhoI-digested pRS413TEF (Mumberg, D. et al. (1995) Gene, 156:119-122), creating the plasmid “pTEFMAE”, which contains sequences encoding the cytosolic NADP + -dependant malic enzyme from M. circinelloides (E.C. 1.1.1.40; mce gene; Genbank accession: AY209191) under the control of the constitutive TEF1 promoter. The plasmids “p1gal2”, “pAMPD”, and “pTEFMAE” are sequentially transformed into a strain of S. cereviseae to restore prototrophy for uracil (“p1gal2”), leucine (“pAMPD”), and histidine (“pTEFMAE”) (Guthrie and Fink Methods in Enzymology 194:1-933, 1991). The resulting transformants are tested for total lipid content following shake flask testing in either synthetic complete (SC) medium lacking uracil, leucine and histidine, as described in Example 3, or in a 2-step fermentation process. In the 2-step process, 1.5 ml of cells from an overnight 2 ml roll tube culture containing SC medium lacking uracil, leucine and histidine are centrifuged, washed in distilled water, and resuspended in 20 ml of a nitrogen-limiting medium suitable for lipid accumulation (30 g/L glucose, 1.5 g/L yeast extract, 0.5 g/L NH 4 Cl, 7 g/L KH 2 PO 4 , 5 g/L Na 2 HPO 4 -12H 2 O, 1.5 g/L MgSO 4 -7H 2 O, 0.08 g/L FeCl 3 -6H 2 O, 0.01 g/L ZnSO 4 -7H 2 O, 0.1 g/L CaCl 2 -2H 2 O, 0.1 mg/L MnSO 4 -5H 2 O, 0.1 mg/L CuSO 4 -5H 2 O, 0.1 mg/L Co(NO 3 ) 2 -6H 2 O; pH 5.5 (J Am Oil Chem Soc 70:891-894 (1993)). Intracellular lipid content of the modified and control S. cerevisiae strains is analyzed using the fluorescent probe, Nile Red (J Microbiol Meth (2004) 56:331-338). In brief, cells diluted in buffer are stained with Nile Red, excited at 488 nm, and the fluorescent emission spectra in the wavelength region of 400-700 nm are acquired and compared to the corresponding spectra from cells not stained with Nile Red. To confirm results from the rapid estimation method, the total lipid content is determined by gas chromatographic analysis of the total fatty acids directly transmethylesterified from dried cells, as described (Appl Microbiol Biotechnol. 2002 November; 60(3):275-80). Non-transformed S. cerevisiae strains produce 6% and 10% total lipid (dry cell weight basis) after growth in YPD and lipid accumulation medium, respectively. Yeast strains expressing the multiple oleaginic polypeptides produce 17% and 25% total lipid following growth in YPD and lipid accumulation medium, respectively. Example 10 Introduction of Heterologous Carotene Hydroxylase into Y. lipolytica Strains Producing Carotenoid for Production of Zeaxanthin MF578 (tef-carRP tef-carB) was transformed with pMB4692 that had been cleaved with SalI. Several Ura + colonies inferred to contain tef-crtZ by PCR analysis were able to produce zeaxanthin in YPD shake flasks, and in one case, all of the β-carotene was depleted. Example 11 Regulatory Sequences Sequences which consist of, consist essentially of, and comprise the following regulatory sequences (e.g. promoters and terminator sequences, including functional fragments thereof) may be useful to control expression of endogenous and heterologous genes in engineered host cells, and particularly in engineered fungal cells described herein. Met2 promoter(SEQ ID NO: 109)5′cctctcactttgtgaatcgtgaaacatgaatcttcaagccaagaatgttaggcaggggaagctttctttcagactttttggaattggtcctcttttggacattattgacgatattattattttttccccgtccaatgttgacccttgtaagccattccggttctggagcgcatctcgtctgaaggagtcttcgtgtggctataactacaagcgttgtatggtggatcctatgaccgtctatatagggcaacttttgctcttgttcttccccctccttgagggacgtatggcaatggctatgacaactatcgtagtgagcctctataacccattgaagtacaagtcctccaccttgctgccaaactcgcgagaaaaaaagtccaccaactccgccgggaaatactggagaacacctctaagacgtgggcttctgcacctgtgtggcttgggtctgggttttgcgagctctgagccacaacctaaggacggtgtgattgggagataagtagtcgttggttttctaatcgcacgtgatatgcaagccacacttataacacaatgaagacaggccgatgaactgcatgtcattgtacaggtgcggagagcaagaaactctggggcggaggtgaaagatgagacaaaaagcctcaggtgcaaggtagggagttgatcaacgtcaaacacaaataatctaggttgttaggcagctaaacatgtatataactgggctgccaccgagtgttacttgtcattaacgtcgcattttcgcctacacaaaatttgggttactcgccactacactgctcaaatctttcagctgtgcaacaagctttcaggtcacacatagactcgcataaggacccgggtcatctgttattctccactggtaaaccaatagtcctagctgatttgggtacagaagctcactttcacatcttttcatcttcttctacaaccatcMet3 promoter(SEQ ID NO: 110)5′atctgtgaggagcccctggcgtcactgtcgactgtgccggcatttctgatggtatttccagccccgcagttctcgagacccccgaacaaatgtgccacacccttgccaaaatgacgaatacacggcgtcgcggccgggaatcgaactcttggcaccgccacaggagtgaaatttgaaatttgaaatttgaaaaataattcacattttgagtttcaataatatatcgatgaccctcccaaaagacccaagtcgagacgcaaaaaaacacccagacgacatggatgcggtcacgtgaccgcaaaaaccgccccggaaatccgtttgtgacgtgttcaattccatctctatgtttttctgcggtttctacgatgccgcaatggtggccaatgtgcgtttcactgccgtagtggctggaacaagccacagggggtcgtcgggccaatcagacggtccctgacatggttctgcgccctaacccgggaactctaacccccgtggtggcgcaatcgctgtcttcatgtgctttatctcacgtgacggctggaatctggcagaagacggagtatgtacattttgtcgttggtcacgttatccctaaaacgtggtgtttaaactggtcgaatgcttggcccagaacacaagaagaaaaaaacgagacaacttgatcagtttcaacgccacagcaagcttgtcttcactgtggttggtcttctccacgccacaagcaacacgtacatgtcaattacgtcagggtcttttaagttctgtggcttttgaaccagttataaagaaccaaccacccttttttcaaagctaatcaagacggggaaattttttttttgatatttttcgacaMet6 promoter(SEQ ID NO: 111)5′gatactgcagacggtgcattacttacccgtgtcgactgagagtctacttggtacttggccctgtggctaagcagtatttgagcaacaatgcaatgcagttgctgactcggttccagatccccttgccccgatgtgtggaagcgttgtttttggggcaagggcatgtgggggctgcatcatactgtggctggggccgttggaagagccgtcggcagcgagcctgagtcgcttctcggggccttattccccccgcctctaggtcagcggcggccgaagtgtcgtactcagctcgcctgtacagtatgacgtgaccgaatagcctctggaaggttggagaagtacagtgcaaaaaaaagttgcaaaatttcattttagcgttcgatccgacgtggcagttggacaatgaatcgatggagacatgatcatgggcagaaatagaaggtctccatgttcaatggcagtaccaattgagcaacagacgggtcgacaggcggcgggcacaccatccgccctccacatggcgcaatcgtcagtgcagcgattcgtactcggattgcatcatgttgcaccgaaagttggggcccgcacgttggagaggcgaggagccagggttagctttggtggggtcctttgttgtcacgtggcatcagcgaatggcgtcctccaatcagggccgtcagcgaagtcggcgtgtgatagtgcgtggggagcgaatagagtttctgggggggggcggcccaaaacgtgaaatccgagtacgcatgtagagtgtaaattgggtgtatagtgacattgtttgactctgaccctgagagtaatatataatgtgtacgtgtccccctccgttggtcttctttttttctcctttctcctaaccaacacccaaactaatcaatcMet25 promoter(SEQ ID NO: 112)5′aagtcgtattaacataactttccttacatttttttaaagcacgtcactatccacgtgacctagccacgcgataccaagtattcatccataatgacacactcatgacgtccggaggacgtcatcatcgtccagtcacgtgccaaggcacatgactaatcataacaccttatgactagcttctgaatcgctacacagttccaattcgcaaataaactcgaaatgacgaaatgccataataaaaatgacgaaactcgagattgagagcagcacatgcactgaagtggtggacaaccagcgtatccggagacacgacggatccagcaccatggaagctggccgaaaaagagatccccagcacattgagcaaccaagtcagctcaattgagtaacatcacacactcagatcgagtctgatggtggtccccttttgttccttcacttgaaaaataattgaaaataacaataacaataaaaataaaaacaaaataaaaataaaaataaaaataaaaataaaaaaataaaaaaaccttgccgcatttagcgtcagccaccccccgcattgacctgagtacgttggattgaccccgatcctgcacgtcgagcgtggtcggccaaaaagcgcccgtggctggtgagtcagaaatagcagggttgcaagagagagctgcgcaacgagcaataaacggtgtttttttcgcttctgtgctgcttagagtggagagccgaccctcgccatgctcacgtgaccattcacgtggttgcaaactccaccttagtatagccgtgtccctctcgctacccattatcgcatcgtactccagccacatttttttgttccccgctaaatccggaaccttatctgggtcacgtgaaattgcaatctcgacaggaggttatacttatagagtgagacactccacgcaaggtgttgcaagtcaattgacaccacctcacctcagactaacatccacaPox2 promoter(SEQ ID NO: 113)5′gaatctgcccccacattttatctccgcttttgactgtttttctcccccctttcacactctgcttttggctacataaaccccgcac cgtttggaactctgttggtccggggaagccgccgttaggtgtgtcagatggagagcgccagacgagcagaaccgagggacagcggatcgggggagggctgtcacgtgacgaagggcactgttgacgtggtgaatgtcgcccgttctcacgtgacccgtctcctctatatgtgtatccgcctctttgtttggttttttttctgcttccccccccccccccccaccccaatcacatgctcagaaagtagacatctgcatcgtcctgcatgccatcccacaagacgaacaagtgataggccgagagccgaggacgaggtggagtgcacaaggggtaggcgaatggtacgattccgccaagtgagactggcgatcgggagaagggttggtggtcatgggggatagaatttgtacaagtggaaaaaccactacgagtagcggatttgataccacaagtagcagagatatacagcaatggtgggagtgcaagtatcggaatgtactgtacctcctgtactcgtactcgtacggcactcgtagaaacggggcaatacgggggagaagcgatcgcccgtctgttcaatcgccacaagtccgagtaatgctcgagtatcgaagtcttgtacctccctgtcaatcatggcaccactggtcttgacttgtctattcatactggacaagcgccagagttaagcttgtagcgaatttcgccctcggacatcaccccatacgacggacacacatgcccgacaaacagcctctcttattgtagctgaaagtatattgaatgtgaacgtgtacaatatcaggtaccagcgggaggttacggccaaggtgataccggaataaccctggcttggagatggtcggtccattgtactgaagtgtccgtgtcgtttccgtcactgccccaattggacatgtttgtttttccgatctttcgggcgccctctccttgtctccttgtctgtctcctggactgttgctaccccatttctttggcctccattggttcctccccgtctttcacgtcgtctatggttgcatggtttcccttatacttttccccacagtcacatgttatggaggggtctagatggaggcctaattttgacgtgcaaggggcgaattggggcgagaaacacgtcgtggacatggtgcaaggcccgcagggttgattcgacgcttttccgcgaaaaaaacaagtccaaatacccccgtttattctccctcggctctcggtatttcacatgaaaactataacctagactacacgggcaaccttaaccccagagtatacttatataccaaagggatgggtcctcaaaaatcacacaagcaacgYef3 (YALI0E13277g) promoter(SEQ ID NO: 114)5′cgccattcggttccttccagaccattccagatcaatccacctcttcttatctcaggtgggtgtgctgacatcagaccccgtagcccttctcccagtggcgaacagcaggcataaaacagggccattgagcagagcaaacaaggtcggtgaaatcgtcgaaaaagtcggaaaacggttgcaagaaattggagcgtcacctgccaccctccaggctctatataaagcattgccccaattgctaacgcttcatatttacacctttggcaccccagtccatccctccaataaaatgtactacatgggacacaacaagagaggatgcgcgcccaaaccctaacctagcacatgcacgatgattctctttgtctgtgaaaaaatttttccaccaaaatttccccattgggatgaaaccctaaccgcaaccaaaagtttttaactatcatcttgtacgtcacggtttccgattcttctcttctctttcatcatcatcacttgtgaccCam1 (YALI0C24420g) promoter(SEQ ID NO: 115)5′aactaccataaagtaccgagaaatataggcaattgtacaaattgtccacctccttcacttacattaccgaaccatggccatatcaccaaaataccccgagtgctaaaacacctccctccaaatgttctcttaccttccaccgaaaaccgatcttattatcccaacgcttgttgtggcttgacgcgccgcacccgctgggcttgccatttcgataccaatccaagaggaaaagctcatgagaaacaatcggaatatcacgagaacggcctggcgaaccaacaggatatttttgaatataattacccctcgaatctagtcatatctatgtctactgtagacttgggcggcatcatgatgtacattattttagcgtctggaaccctaaagttcacgtacaatcatgtgacaaacgaggctaaaaaatgtcaatttcgtatattagtgttattacgtggctcacatttccgaatcatctaccaccccccacctaaaaaYALI0D16467g promoter(SEQ ID NO: 116)5′tttttttaattttcatatttattttcatatttattttcatatttattttcatttatttattcatgtatttatttattactttttaagtattttaaactcctcactaaaccgtcgattgcacaatattaaccttcattacacctgcagcgtggtttttgtggtcgttagccgaagtcttccaacgtgggtataagtaggaacaattgggccgattttttgagccgtctaaatctctcgactcaattgatctgctgtcgaaaatccggctctctagctccttttccccgtccgctggagctcctcttcattgtgccgtttttccaacatttaactttgccacccaccaccacccccactaccatcacccactcgatctctgttcgtgtcaccacgactttgtcttctcacacatactctgtttgtgcaccacacattgcgaaTef4 (YALI0B12562g) promoter(SEQ ID NO: 117)5′gctacaatagctttattggccctattgagcacgctacaattcggtccagtatgtacaacgtctatgcgcactaacggccatacagtgagttacagcacacccaaaagtaaccctgcctgacctgtctgcctgagacaggaagattaactcttgtagtgaccgagctcgataagactcaagccacacaatttttttatagccttgcttcaagagtcgccaaaatgacattacacaactccacggaccgtcggttccatgtccacacccttggatgggtaagcgctccacgcacgtaccacgtgcattgagtttaaccacaaacataggtctgtgtcccagagttaccctgctgcatcagccaagtcttgaaagcaaaatttattgcacaatttttcctcttcttttcttcactgatcgcagtccaaacacaaacaYALI0D12903g promoter(SEQ ID NO: 118)5′gcgctctgatccacttgtatggctccaagttcagtgtaccaagtagttggtgatgcagggagggatgtctctatccaccaataatgaactcatgggcgaaattgtttctgttaaacactccaactgtcgttttaaatctcattctctttgcatttggactccattcgcttccgttgggccaatataatccatcgtaacgtactttagatggaaatttagttacctgctacttgtctcaacaccccaacaggggctgttcgacagaggtaatagagcgtcaatgggttaataaaaacacactgtcgattttcactcattgtctttatgatattacctgttttccgctgttatcaatgccgagcatcgtgttatatcttccaccccaactacttgcatttacttaactattacctcaactatttacaccccgaattgttacctcccaataagtaactttatttcaaccaatgggacgagagcatctctgagaacatcgatctatctctgtcaatattgcccagaatcgttcgaaaaaaaacaccaaaaggtttacagcgccattataaatataaattcgttgtcaattcccccgcaatgtctgttgaaatctcattttgagaccttccaacattaccctctctcccgtctggtcacatgacgtgactgcttcttcccaaaacgaacactcccaactcttcccccccgtcagtgaaaagtatacatccgacctccaaatcttttcttcactcaacTef1 (YALI0C09141g) promoter(SEQ ID NO: 119)5′agagacgggttggcggcgtatttgtgtcccaaaaaacagccccaattgccccaattgaccccaaattgacccagtagcgggcccaaccccggcgagagcccccttcaccccacatatcaaacctcccccggttcccacacttgccgttaagggcgtagggtactgcagtctggaatctacgcttgttcagactttgtactagtttctttgtctggccatccgggtaacccatgccggacgcaaaatagactactgaaaatttttttgctttgtggttgggactttagccaagggtataaaagaccaccgtccccgaattacctttcctcttcttttctctctctccttgtcaactcacacccgaaatcgttaagcatttccttctgagtataagaatcattcFba1 (YALI0E26004g) promoter(SEQ ID NO: 120)5′gctgcgctgatctggacaccacagaggttccgagcactttaggttgcaccaaatgtcccaccaggtgcaggcagaaaacgctggaacagcgtgtacagtttgtcttagcaaaaagtgaaggcgctgaggtcgagcagggtggtgtgacttgttatagcctttagagctgcgaaagcgcgtatggatttggctcatcaggccagattgagggtctgtggacacatgtcatgttagtgtacttcaatcgccccctggatatagccccgacaataggccgtggcctcatttttttgccttccgcacatttccattgctcggtacccacaccttgcttctcctgcacttgccaaccttaatactggtttacattgaccaacatcttacaagcggggggcttgtctagggtatatataaacagtggctctcccaatcggttgccagtctcttttttcctttctttccccacagattcgaaatctaaactacacatcPox2 terminator:(SEQ ID NO: 121)5′gatgaggaatagacaagcgggtatttattgtatgaataaagattatgtattgattgcaaaaaagtgcatttgtagatgtggtttattgtagagagtacggtatgtactgtacgaacattaggagctacttctacaagtagattttcttaacaagggtgaaatttactaggaagtacatgcatatttcgttagtagaatcacaaaagaaatgtacaagcacgtactacttgtactccacaatgtggagtgggagcaaaaaaattggacgacaccggaatcgaaccggggacctcgcgcatgctaagcgcatgtgataaccaactacaccagacgcccaagaactttcttggtgattatggaatacgtggtctgctatatctcaattttgctgtaatgaatcattagaattaaaaaaaaaaccccatttttgtgtgattgtcggccaagagatggaacaggaagaatacgtgaacaagcgagcacgaatgccatatgctcttctgaacaaccgagtccgaatccgatttgtgggtatcacatgtctcaagtagctgaaatgtatttcgctagaataaaataaatgagattaagaattaaaaatattggaatatattttcctagaatagaaactttggattttttttcggctattacagtctgaactggacaaacggctgactatatataaatattattgggtctgttttcttgtttatgtcgaaattatctgggttttactactgtgtcgtcgagtatagagtggcctgactggagaaaatgcagtagtatggacagtaggtactgccagccagagaagtttttggaattgatacttgagtcatttttccattccccattccccattccaacacaatcaactgtttctgaacattttccaaaacgcggagatgtatgtcacttggcactgcaagtctcgattcaaaatgcatctctttcagaccaaagtgtcatcagctttgtttggccccaaattaccgcaaatacttgtcgaaattgaagtgcaatacggcctcgtctgccatgaaacctgcctattctcttcaaattggcgtcaggtttcacgtccagcattcctcgcccagacagagttgctatggttgaatcgtgtactgttaatatatgtatgtattatactcgtactacgatatactgttcaatagagtctcttataatcgtacgacgattctgggca Example 12 Y. lipolytica Oleaginic and Isoprenoid Biosynthesis Genes FIG. 10 is a list of Y. lipolytica genes representing various polypeptides (e.g. oleaginic and isoprenoid biosynthesis peptides) useful in the fungal strains and methods described herein. The Genbank accession number and GI number is given for each polypeptide in addition to oligo pairs which can be used to amplify the coding region for each gene from Y. lipolytica genomic DNA or cDNA. Resulting PCR fragments can be cleaved with restriction enzyme pairs (e.g. depending on what site is present within the oligo sequence, XbaI/MluI or NheI/MluI or XbaI/AscI or NheI/AscI) and inserted into expression vectors (e.g. fungal expression vectors including Y. lipolytica expression vectors such as MB4629 and MB4691 described herein). The DNA and proteins they encode of the Y. lipolytica genes represented in FIG. 10 are as follows (intron sequence is underlined): YALI0F30481gDNA:(SEQ ID NO: 122)atgtcgcaaccccagaacgttggaatcaaagccctcgagatctacgtgccttctcgaattgtcaaccaggctgagctcgagaagcacgacggtgtcgctgctggcaagtacaccattggtcttggtcagaccaacatggcctttgtcgacgacagagaggacatctattcctttgccctgaccgccgtctctcgactgctcaagaacaacaacatcgaccctgcatctattggtcgaatcgaggttggtactgaaacccttctggacaagtccaagtccgtcaagtctgtgctcatgcagctctttggcgagaacagcaacattgagggtgtggacaacgtcaacgcctgctacggaggaaccaacgccctgttcaacgctatcaactgggttgagggtcgatcttgggacggccgaaacgccatcgtcgttgccggtgacattgccctctacgcaaagggcgctgcccgacccaccggaggtgccggctgtgttgccatgctcattggccccgacgctcccctggttcttgacaacgtccacggatcttacttcgagcatgcctacgatttctacaagcctgatctgacctccgagtacccctatgttgatggccactactccctgacctgttacacaaaggccctcgacaaggcctacgctgcctacaacgcccgagccgagaaggtcggtctgttcaaggactccgacaagaagggtgctgaccgatttgactactctgccttccacgtgcccacctgcaagcttgtcaccaagtcttacgctcgacttctctacaacgactacctcaacgacaagagcctgtacgagggccaggtccccgaggaggttgctgccgtctcctacgatgcctctctcaccgacaagaccgtcgagaagaccttccttggtattgccaaggctcagtccgccgagcgaatggctccttctctccagggacccaccaacaccggtaacatgtacaccgcctctgtgtacgcttctctcatctctctgctgacttttgtccccgctgagcagctgcagggcaagcgaatctctctcttctcttacggatctggtcttgcttccactcttttctctctgaccgtcaagggagacatttctcccatcgtcaaggcctgcgacttcaaggctaagctcgatgaccgatccaccgagactcccgtcgactacgaggctgccaccgatctccgagagaaggcccacctcaagaagaactttgagccccagggagacatcaagcacatcaagtctggcgtctactacctcaccaacatcgatgacatgttccgacgaaagtacgagatcaagcagtagProtein:(SEQ ID NO: 123)MsqpqnvgikaleiyvpsrivnqaelekhdgvaagkytiglgqtnmafvddrediysfaltavsrllknnnidpasigrievgtetlldksksvksvlmqlfgensniegvdnvnacyggtnalfnainwvegrswdgrnaivvagdialyakgaarptggagcvamligpdaplvldnvhgsyfehaydfykpdltseypyvdghysltcytkaldkayaaynaraekvglfkdsdkkgadrfdysafhvptcklvtksyarllyndylndkslyegqvpeevaavsydasltdktvektflgiakaqsaermapslqgptntgnmytasvyaslislltfvpaeqlqgkrislfsygsglastlfsltvkgdispivkacdfkaklddrstetpvdyeaatdlrekahlkknfepqgdikhiksgvyyltniddmfrrkyeikqYALI0B16038gDNA:(SEQ ID NO: 124)atggactacatcatttcggcgccaggcaaagtgattctatttggtgaacatgccgctgtgtttggtaagcctgcgattgcagcagccatcgacttgcgaacatacctgcttgtcgaaaccacaacatccgacaccccgacagtcacgttggagtttccagacatccacttgaacttcaaggtccaggtggacaagctggcatctctcacagcccagaccaaggccgaccatctcaattggtcgactcccaaaactctggataagcacattttcgacagcttgtctagcttggcgcttctggaagaacctgggctcactaaggtccagcaggccgctgttgtgtcgttcttgtacctctacatccacctatgtcccccttctgtgtgcgaagattcatcaaactgggtagttcgatcaacgctgcctatcggcgcgggcctgggctcttccgcatccatttgtgtctgtttggctgcaggtcttctggttctcaacggccagctgagcattgaccaggcaagagatttcaagtccctgaccgagaagcagctgtctctggtggacgactggtccttcgtcggtgaaatgtgcattcacggcaacccgtcgggcatcgacaatgctgtggctactcagggaggtgctctgttgttccagcgacctaacaaccgagtccctcttgttgacattcccgagatgaagctgctgcttaccaatacgaagcatcctcgatctaccgcagacctggttggtggagtcggagttctcactaaagagtttggctccatcatggatcccatcatgacttcagtaggcgagatttccaaccaggccatggagatcatttctagaggcaagaagatggtggaccagtctaaccttgagattgagcagggtatcttgcctcaacccacctctgaggatgcctgcaacgtgatggaagatggagctactcttcaaaagttgagagatatcggttcggaaatgcagcatctagtgagaatcaatcacggcctgcttatcgctatgggtgtttcccacccgaagctcgaaatcattcgaactgcctccattgtccacaacctgggtgagaccaagctcactggtgctggaggaggaggttgcgccatcactctagtcacttctaaagacaagactgcgacccagctggaggaaaatgtcattgctttcacagaggagatggctacccatggcttcgaggtgcacgagactactattggtgccagaggagttggtatgtgcattgaccatccctctctcaagactgttgaagccttcaagaaggtggagcgggcggatctcaaaaacatcggtccctggacccattagProtein:(SEQ ID NO: 125)mdyiisapgkvilfgehaavfgkpaiaaaidlrtyllvetttsdtptvtlefpdihlnfkvqvdklasltaqtkadhlnwstpktldkhifdslsslalleepgltkvqqaavvsflylyihlcppsvcedssnwvvrstlpigaglgssasicyclaagllvlngqlsidqardfksltekqlslvddwsfvgemcihgnpsgidnavatqggallfqrpnnrvplvdipemkllltntkhprstadlvggvgvltkefgsimdpimtsvgeisnqameiisrgkkmvdqsnleieqgilpqptsedacnvmedgatlqklrdigsemqhlvrinhglliamgvshpkleiirtasivhnlgetkltgaggggcaitlvtskdktatqleenviafteemathgfevhettigargvgmcidhpslktveafkkveradlknigpwthYALI0E06193gDNA:(SEQ ID NO: 126)atgaccacctattcggctccgggaaaggccctcctttgcggcggttatttggttattgatccggcgtattcagcatacgtcgtgggcctctcggcgcgtatttacgcgacagtttcggcttccgaggcctccaccacctctgtccatgtcgtctctccgcagtttgacaagggtgaatggacctacaactacacgaacggccagctgacggccatcggacacaacccatttgctcacgcggccgtcaacaccgttctgcattacgttcctcctcgaaacctccacatcaacatcagcatcaaaagtgacaacgcgtaccactcgcaaattgacagcacgcagagaggccagtttgcataccacaaaaaggcgatccacgaggtgcctaaaacgggcctcggtagctccgctgctcttaccaccgttcttgtggcagctttgctcaagtcatacggcattgatcccttgcataacacccacctcgttcacaacctgtcccaggttgcacactgctcggcacagaagaagattgggtctggatttgacgtggcttcggccgtttgtggctctctagtctatagacgtttcccggcggagtccgtgaacatggtcattgcagctgaagggacctccgaatacggggctctgttgagaactaccgttaatcaaaagtggaaggtgactctggaaccatccttcttgccgccgggaatcagcctgcttatgggagacgtccagggaggatctgagactccaggtatggtggccaaggtgatggcatggcgaaaagcaaagccccgagaagccgagatggtgtggagagatctcaacgctgccaacatgctcatggtcaagttgttcaacgacctgcgcaagctctctctcactaacaacgaggcctacgaacaacttttggccgaggctgctcctctcaacgctctaaagatgataatgttgcagaaccctctcggagaactagcacgatgcattatcactattcgaaagcatctcaagaagatgacacgggagactggtgctgctattgagccggatgagcagtctgcattgctcaacaagtgcaacacttatagtggagtcattggaggtgttgtgcctggagcaggaggctacgatgctatttctcttctggtgatcagctctacggtgaacaatgtcaagcgagagagccagggagtccaatggatggagctcaaggaggagaacgagggtctgcggctcgagaaggggttcaagtagProtein:(SEQ ID NO: 127)mttysapgkalleggylvidpaysayvvglsariyatvsaseasttsvhvvspqfdkgewtynytngqltaighnpfahaavntvlhyvpprnlhinisiksdnayhsqidstqrgqfayhkkaihevpktglgssaalttvlvaallksygidplhnthlvhnlsqvahcsaqkkigsgfdvasavcgslvyrrfpaesvnmviaaegtseygallrttvnqkwkvtlepsflppgisllmgdvqggsetpgmvakvmawrkakpreaemvwrdlnaanmlmvklfildlrklsltnneayeqllaeaaplnalkmimlqnplgelarciitirkhlkkmtretgaaiepdeqsallnkcntysgviggvvpgaggydaisllvisstvnnvkresqgvqwmelkeeneglrlekgfkYALI0F05632gDNA:(SEQ ID NO: 128)atgatccaccaggcctccaccaccgctccggtgaacattgcgacactcaagtactggggcaagcgagaccctgctctcaatctgcccactaacaactccatctccgtgactttgtcgcaggatgatctgcggaccctcaccacagcctcgtgttcccctgatttcacccaggacgagctgtggctcaatggcaagcaggaggacgtgagcggcaaacgtctggttgcgtgtttccgagagctgcgggctctgcgacacaaaatggaggactccgactcttctctgcctaagctggccgatcagaagctcaagatcgtgtccgagaacaacttccccaccgccgctggtctcgcctcatcggctgctggctttgccgccctgatccgagccgttgcaaatctctacgagctccaggagacccccgagcagctgtccattgtggctcgacagggctctggatccgcctgtcgatctctctacggaggctacgtggcatgggaaatgggcaccgagtctgacggaagcgactcgcgagcggtccagatcgccaccgccgaccactggcccgagatgcgagccgccatcctcgttgtctctgccgacaagaaggacacgtcgtccactaccggtatgcaggtgactgtgcacacttctcccctcttcaaggagcgagtcaccactgtggttcccgagcggtttgcccagatgaagaagtcgattctggaccgagacttccccacctttgccgagctcaccatgcgagactcaaaccagttccacgccacctgtctggactcgtatcctcccattttctacctcaacgacgtgtcgcgagcctccattcgggtagttgaggccatcaacaaggctgccggagccaccattgccgcctacacctttgatgctggacccaactgtgtcatctactacgaggacaagaacgaggagctggttctgggtgctctcaaggccattctgggccgtgtggagggatgggagaagcaccagtctgtggacgccaagaagattgatgttgacgagcggtgggagtccgagctggccaacggaattcagcgggtgatccttaccaaggttggaggagatcccgtgaagaccgctgagtcgcttatcaacgaggatggttctctgaagaacagcaagtagProtein:(SEQ ID NO: 129)mihqasttapvniatlkywgkrdpalnlptnnsisvtlsqddlrtlttascspdftqdelwlngkqedvsgkrlvacfrelralrhkmedsdsslpkladqklkivsennfptaaglassaagfaaliravanlyelqetpeqlsivarqgsgsacrslyggyvawemgtesdgsdsravqiatadhwpemraailvvsadkkdtssttgmqvtvhtsplfkervttvvperfaqmkksildrdfptfaeltmrdsnqfhatcldsyppifylndvsrasirvveainkaagatiaaytfdagpncviyyedkneelvlgalkailgrvegwekhqsvdakkidvderweselangiqrviltkvggdpvktaeslinedgslknskYALI0F04015gDNA:(SEQ ID NO: 130)AtgacgacgtcttacagcgacaaaatcaagagtatcagcgtgagctctgtggctcagcagtttcctgaggtggcgccgattgcggacgtgtccaaggctagccggcccagcacggagtcgtcggactcgtcggccaagctatttgatggccacgacgaggagcagatcaagctgatggacgagatctgtgtggtgctggactgggacgacaagccgattggcggcgcgtccaaaaagtgctgtcatctgatggacaacatcaacgacggactggtgcatcgggccttttccgtgttcatgttcaacgaccgcggtgagctgcttctgcagcagcgggcggcggaaaaaatcacctttgccaacatgtggaccaacacgtgctgctcgcatcctctggcggtgcccagcgagatgggcgggctggatctggagtcccggatccagggcgccaaaaacgccgcggtccggaagcttgagcacgagctgggaatcgaccccaaggccgttccggcagacaagttccatttcctcacccggatccactacgccgcgccctcctcgggcccctggggcgagcacgagattgactacattctgtttgtccggggcgaccccgagctcaaggtggtggccaacgaggtccgcgataccgtgtgggtgtcgcagcagggactcaaggacatgatggccgatcccaagctggttttcaccccttggttccggctcatttgtgagcaggcgctgtttccctggtgggaccagttggacaatctgcccgcgggcgatgacgagattcggcggtggatcaagtagProtein:(SEQ ID NO: 131)mttsysdkiksisyssvaqqfpevapiadvskasrpstessdssaklfdghdeeqiklmdeicvvldwddkpiggaskkcchlmdnindglvhrafsvfmfndrgelllqqraaekitfanmwtntccshplavpsemggldlesriqgaknaavrklehelgidpkavpadkfhfltrihyaapssgpwgeheidyilfvrgdpelkvvanevrdtvwvsqqglkdmmadpklvftpwfrliceqalfpwwdqldnlpagddeirrwikYALI0E05753DNA:(SEQ ID NO: 132)atgtccaaggcgaaattcgaaagcgtgttcccccgaatctccgaggagctggtgcagctgctgcgagacgagggtctgccccaggatgccgtgcagtggttttccgactcacttcagtacaactgtgtgggtggaaagctcaaccgaggcctgtctgtggtcgacacctaccagctactgaccggcaagaaggagctcgatgacgaggagtactaccgactcgcgctgctcggctggctgattgagctgctgcaggcgtttttcctcgtgtcggacgacattatggatgagtccaagacccgacgaggccagccctgctggtacctcaagcccaaggtcggcatgattgccatcaacgatgctttcatgctagagagtggcatctacattctgcttaagaagcatttccgacaggagaagtactacattgaccttgtcgagctgttccacgacatttcgttcaagaccgagctgggccagctggtggatcttctgactgcccccgaggatgaggttgatctcaaccggttctctctggacaagcactcctttattgtgcgatacaagactgcttactactccttctacctgcccgttgttctagccatgtacgtggccggcattaccaaccccaaggacctgcagcaggccatggatgtgctgatccctctcggagagtacttccaggtccaggacgactaccttgacaactttggagaccccgagttcattggtaagatcggcaccgacatccaggacaacaagtgctcctggctcgttaacaaagcccttcagaaggccacccccgagcagcgacagatcctcgaggacaactacggcgtcaaggacaagtccaaggagctcgtcatcaagaaactgtatgatgacatgaagattgagcaggactaccttgactacgaggaggaggttgttggcgacatcaagaagaagatcgagcaggttgacgagagccgaggcttcaagaaggaggtgctcaacgctttcctcgccaagatttacaagcgacagaagtagProtein:(SEQ ID NO: 133)mskakfesvfpriseelvqllrdeglpqdavqwfsdslqyncvggklnrglsvvdtyqlltgkkelddeeyyrlallgwliellqafflvsddimdesktrrgqpcwylkpkvgmiaindafmlesgiyillkkhfrqekyyidlvelfhdisfktelgqlvdlltapedevdlnrfsldkhsfivryktayysfylpvvlamyvagitnpkdlqqamdvliplgeyfqvqddyldnfgdpefigkigtdiqdnkcswlvnkalqkatpeqrqilednygvkdkskelvikklyddmkieqdyldyeeevvgdikkkieqvdesrgfkkevlnaflakiykrqkYALI0E18634gDNA:(SEQ ID NO: 134)atgttacgactacgaaccatgcgacccacacagaccagcgtcagggcggcgcttgggcccaccgccgcggcccgaaacatgtcctcctccagcccctccagcttcgaatactcgtcctacgtcaagggcacgcgggaaatcggccaccgaaaggcgcccacaacccgtctgtcggttgagggccccatctacgtgggcttcgacggcattcgtcttctcaacctgccgcatctcaacaagggctcgggattccccctcaacgagcgacgggaattcagactcagtggtcttctgccctctgccgaagccaccctggaggaacaggtcgaccgagcataccaacaattcaaaaagtgtggcactcccttagccaaaaacgggttctgcacctcgctcaagttccaaaacgaggtgctctactacgccctgctgctcaagcacgttaaggaggtcttccccatcatctatacaccgactcagggagaagccattgaacagtactcgcggctgttccggcggcccgaaggctgcttcctcgacatcaccagtccctacgacgtggaggagcgtctgggagcgtttggagaccatgacgacattgactacattgtcgtgactgactccgagggtattctcggaattggagaccaaggagtgggcggtattggtatttccatcgccaagctggctctcatgactctatgtgctggagtcaacccctcacgagtcattcctgtggttctggatacgggaaccaacaaccaggagctgctgcacgaccccctgtatctcggccgacgaatgccccgagtgcgaggaaagcagtacgacgacttcatcgacaactttgtgcagtctgcccgaaggctgtatcccaaggcggtgatccatttcgaggactttgggctcgctaacgcacacaagatcctcgacaagtatcgaccggagatcccctgcttcaacgacgacatccagggcactggagccgtcactttggcctccatcacggccgctctcaaggtgctgggcaaaaatatcacagatactcgaattctcgtgtacggagctggttcggccggcatgggtattgctgaacaggtctatgataacctggttgcccagggtctcgacgacaagactgcgcgacaaaacatctttctcatggaccgaccgggtctactgaccaccgcacttaccgacgagcagatgagcgacgtgcagaagccgtttgccaaggacaaggccaattacgagggagtggacaccaagactctggagcacgtggttgctgccgtcaagccccatattctcattggatgttccactcagcccggcgcctttaacgagaaggtcgtcaaggagatgctcaaacacacccctcgacccatcattctccctctttccaaccccacacgtcttcatgaggctgtccctgcagatctgtacaagtggaccgacggcaaggctctggttgccaccggctcgccctttgacccagtcaacggcaaggagacgtctgagaacaataactgctttgttttccccggaatcgggctgggagccattctgtctcgatcaaagctcatcaccaacaccatgattgctgctgccatcgagtgcctcgccgaacaggcccccattctcaagaaccacgacgagggagtacttcccgacgtagctctcatccagatcatttcggcccgggtggccactgccgtggttcttcaggccaaggctgagggcctagccactgtcgaggaagagctcaagcccggcaccaaggaacatgtgcagattcccgacaactttgacgagtgtctcgcctgggtcgagactcagatgtggcggcccgtctaccggcctctcatccatgtgcgggattacgactagProtein:(SEQ ID NO: 135)mlrlrtmrptqtsvraalgptaaarnmsssspssfeyssyvkgtreighrkapttrlsvegpiyvgfdgirllnlphlnkgsgfplnerrefrlsgllpsaeatleeqvdrayqqfkkcgtplakngfctslkfqnevlyyalllkhvkevfpiiytptqgeaieqysrlfrrpegcflditspydveerlgafgdhddidyivvtdsegilgigdqgvggigisiaklalmtlcagvnpsrvipvvldtgtnnqellhdplylgrrmprvrgkqyddfidnfvqsarrlypkavihfedfglanahkildkyrpeipcfnddiqgtgavtlasitaalkvlgknitdtrilvygagsagmgiaeqvydnlvaqglddktarqniflmdrpgllttaltdeqmsdvqkpfakdkanyegvdtktlehvvaavkphiligcstqpgafnekvvkemlkhtprpiilplsnptrlheavpadlykwtdgkalvatgspfdpvngketsennncfvfpgiglgailsrsklitntmiaaaieclaeqapilknhdegvlpdvaliqiisarvatavvlqakaeglatveeelkpgtkehvqipdnfdeclawvetqmwrpvyrplihvrdydYALI0E11495gDNA:(SEQ ID NO: 136)atgccgcagcaagcaatggatatcaagggcaaggccaagtctgtgcccatgcccgaagaagacgacctggactcgcattttgtgggtcccatctctccccgacctcacggagcagacgagattgctggctacgtgggctgcgaagacgacgaagacgagcttgaagaactgggaatgctgggccgatctgcgtccacccacttctcttacgcggaagaacgccacctcatcgaggttgatgccaagtacagagctcttcatggccatctgcctcatcagcactctcagagtcccgtgtccagatcttcgtcatttgtgcgggccgaaatgaaccacccccctcccccaccctccagccacacccaccaacagccagaggacgatgacgcatcttccactcgatctcgatcgtcgtctcgagcttctggacgcaagttcaacagaaacagaaccaagtctggatcttcgctgagcaagggtctccagcagctcaacatgaccggatcgctcgaagaagagccctacgagagcgatgacgatgcccgactatctgcggaagacgacattgtctatgatgctacccagaaagacacctgcaagcccatatctcctactctcaaacgcacccgcaccaaggacgacatgaagaacatgtccatcaacgacgtcaaaatcaccaccaccacagaagatcctcttgtggcccaggagctgtccatgatgttcgaaaaggtgcagtactgccgagacctccgagacaagtaccaaaccgtgtcgctacagaaggacggagacaaccccaaggatgacaagacacactggaaaatttaccccgagcctccaccaccctcctggcacgagaccgaaaagcgattccgaggctcgtccaaaaaggagcaccaaaagaaagacccgacaatggatgaattcaaattcgaggactgcgaaatccccggacccaacgacatggtcttcaagcgagatcctacctgtgtctatcaggtctatgaggatgaaagctctctcaacgaaaataagccgtttgttgccatcccctcaatccgagattactacatggatctggaggatctcattgtggcttcgtctgacggacctgccaagtcttttgctttccgacgactgcaatatctagaagccaagtggaacctctactacctgctcaacgagtacacggagacaaccgagtccaagaccaacccccatcgagacttttacaacgtacgaaaggtcgacacccacgttcaccactctgcctgcatgaaccagaagcatctgctgcgattcatcaaatacaagatgaagaactgccctgatgaagttgtcatccaccgagacggtcgggagctgacactctcccaggtgtttgagtcacttaacttgactgcctacgacctgtctatcgatacccttgatatgcatgctcacaaggactcgttccatcgatttgacaagttcaacctcaagtacaaccctgtcggtgagtctcgactgcgagaaatcttcctaaagaccgacaactacatccagggtcgatacctagctgagatcacaaaggaggtgttccaggatctcgagaactcgaagtaccagatggcggagtaccgtatttccatctacggtcggtccaaggacgagtgggacaagctggctgcctgggtgctggacaacaaactgttttcgcccaatgttcggtggttgatccaggtgcctcgactgtacgacatttacaagaaggctggtctggttaacacctttgccgacattgtgcagaacgtctttgagcctcttttcgaggtcaccaaggatcccagtacccatcccaagctgcacgtgttcctgcagcgagttgtgggctttgactctgtcgatgacgagtcgaagctggaccgacgtttccaccgaaagttcccaactgcagcatactgggacagcgcacagaaccctccctactcgtactggcagtactatctatacgccaacatggcctccatcaacacctggagacagcgtttgggctataatacttttgagttgcgaccccatgctggagaggctggtgacccagagcatcttctgtgcacttatctggttgctcagggtatcaaccacggtattctgttgcgaaaggtgcccttcattcagtacctttactacctggaccagatccccattgccatgtctcctgtgtccaacaatgcgctgttcctcacgttcgacaagaaccccttctactcatacttcaagcggggtctcaacgtgtccttgtcatcggatgatcctctgcagtttgcttacactaaggaggctctgattgaggagtactctgtggctgcgctcatttacaagctttccaacgtggatatgtgtgagcttgctcgaaactcggtactgcaatctggctttgagcgaatcatcaaggagcattggatcggcgaaaactacgagatccatggccccgagggcaacaccatccagaagacaaacgtgcccaatgtgcgtctggccttccgagacgagactttgacccacgagcttgctctggtggacaagtacaccaatcttgaggagtttgagcggctgcatggttaaProtein:(SEQ ID NO: 137)mpqqamdikgkaksvpmpeeddldshfvgpisprphgadeiagyvgceddedeleelgmlgrsasthfsyaeerhlievdakyralhghlphqhsqspvsrsssfvraemnhpppppsshthqqpedddasstrsrsssrasgrkfnrnrtksgsslskglqqlnmtgsleeepyesdddarlsaeddivydatqkdtckpisptlkrtrtkddmknmsindvkittttedplvaqelsmmfekvqycrdlrdkyqtvslqkdgdnpkddkthwkiypeppppswhetekrfrgsskkehqkkdptmdefkfedceipgpndmvfkrdptcvyqvyedesslnenkpfvaipsirdyymdledlivassdgpaksfafrrlqyleakwnlyyllneytettesktnphrdfynvrkvdthvhhsacmnqkhllrfikykmkncpdevvihrdgreltlsqvfeslnltaydlsidtldmhahkdsfhrfdkfnlkynpvgesrlreiflktdnyiqgrylaeitkevfqdlenskyqmaeyrisiygrskdewdklaawvldnklfspnvrwliqvprlydiykkaglvntfadivqnvfeplfevtkdpsthpklhvflqrvvgfdsvddeskldrrfhrkfptaaywdsaqnppysywqyylyanmasintwrqrlgyntfelrphageagdpehllctylvaqginhgillrkvpfiqylyyldqipiamspvsnnalfltfdknpfysyfkrglnyslssddplqfaytkealieeysvaaliyklsnvdmcelarnsvlqsgferiikehwigenyeihgpegntiqktnvpnvrlafrdetlthelalvdkytnleeferlhgYALI0D16753gDNA:(SEQ ID NO: 138)atgttccgaacccgagttaccggctccaccctgcgatccttctccacctccgctgcccgacagcacaaggttgtcgtccttggcgccaacggaggcattggccagcccctgtctctgctgctcaagctcaacaagaacgtgaccgacctcggtctgtacgatctgcgaggcgcccccggcgttgctgccgatgtctcccacatccccaccaactccaccgtggccggctactctcccgacaacaacggcattgccgaggccctcaagggcgccaagctggtgctgatccccgccggtgtcccccgaaagcccggcatgacccgagacgatctgttcaacaccaacgcctccattgtgcgagacctggccaaggccgtcggtgagcacgcccccgacgcctttgtcggagtcattgctaaccccgtcaactccaccgtccccattgtcgccgaggtgctcaagtccaagggcaagtacgaccccaagaagctcttcggtgtcaccaccctcgacgtcatccgagccgagcgattcgtctcccagctcgagcacaccaaccccaccaaggagtacttccccgttgttggcggccactccggtgtcaccattgtccccctcgtgtcccagtccgaccaccccgacattgccggtgaggctcgagacaagcttgtccaccgaatccagtttggcggtgacgaggttgtcaaggccaaggacggtgccggatccgccaccctttccatggcccaggctgccgcccgattcgccgactctctcctccgaggtgtcaacggcgagaaggacgttgttgagcccactttcgtcgactctcctctgttcaagggtgagggcatcgacttcttctccaccaaggtcactcttggccctaacggtgttgaggagatccaccccatcggaaaggtcaacgagtacgaggagaagctcatcgaggctgccaaggccgatctcaagaagaacattgagaagggtgtcaactttgtcaagcagaacccttaaProtein:(SEQ ID NO: 139)mfrtrvtgstlrsfstsaarqhkvvvlganggigqplslllklnknvtdlglydlrgapgvaadvshiptnstvagyspdnngiaealkgaklvlipagvprkpgmtrddlfntnasivrdlakavgehapdafvgvianpvnstvpivaevlkskgkydpkklfgvttldviraerfvsqlehtnptkeyfpvvgghsgvtivplvsqsdhpdiageardklvhriqfggdevvkakdgagsatlsmaqaaarfadsllrgvngekdvveptfvdsplfkgegidffstkvtlgpngveeihpigkvneyeeklieaakadlkkniekgvnfvkqnpYALI0D16247gDNA:(SEQ ID NO: 140)atgacacaaacgcacaatctgttttcgccaatcaaagtgggctcttcggagctccagaaccggatcgttctcgcacccttgactcgaaccagagctctgcccggaaacgtgccctcggatcttgccacagagtactacgcacaaagagcagcatctccaggcactctcctcatcaccgaggccacatacatctcccccggatctgctggagtgcccattccaggagacggaatcgttccgggcatctggagtgacgagcagctcgaagcatggaaaaaggtgttcaaggccgtgcacgaccgaggatccaaaatctacgtccagctgtgggacattggacgtgtcgcatggtaccacaagctgcaggaactgggcaactacttccctacaggcccctcagctatccccatgaagggagaggagagcgagcatctcaaggctctgactcactgggagatcaagggcaaggtggccctctacgtcaacgctgccaagaacgccattgccgcaggcgctgatggcgtcgagatccactcggccaacggctaccttcccgacacatttctgagaagcgcctccaaccaacgaacagacgaatatggaggaagcatcgagaaccgggcccgattctcgctggagattgtcgacgctatcaccgaggccattggagcagacaaaaccgccatccgtctgtctccctggtccactttccaggacattgaggtgaatgacaccgagacccccgcacagttcacatacctgtttgagcagctgcagaagcgagccgacgagggaaagcagctggcctacgtgcatgtagttgagccccgactgtttggtccccccgagccctgggccaccaatgagcattcagaaaaatttggaagggtaacttcattagagcaggtggatacgatagagagactgctcttgaggatgcagacaagtcagacaacaccctgattgcctttggtcgagacttcattgccaatcctgatctcgtccaacgcctcaagaataacgagccttggccaagtacgacagaacaaccttctacgttccaggtgccaagggctacactgattaccctgcgtacaagatgtaaProtein:(SEQ ID NO: 141)mtqthnlfspikvgsselqnrivlapltrtralpgnvpsdlateyyaqraaspgtlliteatyispgsagvpipgdgivpgiwsdeqleawkkvfkavhdrgskiyvqlwdigrvawyhklqelgnyfptgpsaipmkgeesehlkalthweikgkvalyvnaaknaiaagadgveihsangylpdtflrsasnqrtdeyggsienrarfsleivdaiteaigadktairlspwstfqdievndtetpaqftylfeqlqkradegkqlayvhvveprlfgppepwatnepfrkiwkgnfiraggydretaledadksdntliafgrdfianpdlvqrlknneplakydrttfyvpgakgytdypaykmYALI0A15972gDNA:(SEQ ID NO: 142)atggaagccaaccccgaagtccagaccgatatcatcacgctgacccggttcattctgcaggaacagaacaaggtgggcgcgtcgtccgcaatccccaccggagacttcactctgctgctcaactcgctgcagtttgccttcaagttcattgcccacaacatccgacgatcgaccctggtcaacctgattggcctgtcgggaaccgccaactccaccggcgacgaccagaagaagctggacgtgatcggagacgagatcttcatcaacgccatgaaggcctccggtaaggtcaagctggtggtgtccgaggagcaggaggacctcattgtgtttgagggcgacggccgatacgccgtggtctgcgaccccatcgacggatcctccaacctcgacgccggcgtctccgtcggcaccattttcggcgtctacaagctccccgagggctcctccggatccatcaaggacgtgctccgacccggaaaggagatggttgccgccggctacaccatgtacggtgcctccgccaacctggtgctgtccaccggaaacggctgcaacggcttcactctcgatgaccctctgggagagttcatcctgacccaccccgatctcaagctccccgatctgcgatccatctactccgtcaacgagggtaactcctccctgtggtccgacaacgtcaaggactacttcaaggccctcaagttccccgaggacggctccaagccctactcggcccgatacattggctccatggtcgccgacgtgcaccgaaccattctctacggaggtatgtttgcctaccccgccgactccaagtccaagaagggcaagctccgacttttgtacgagggtttccccatggcctacatcattgagcaggccggcggtcttgccatcaacgacaacggcgagcgaatcctcgatctggtccccaccgagatccacgagcgatccggcgtctggctgggctccaagggcgagattgagaaggccaagaagtaccttctgaaatgaProtein:(SEQ ID NO: 143)meanpevqtdiitltrfilqeqnkvgassaiptgdftlllnslqfafkfiahnirrstlvnliglsgtanstgddqkkldvigdeifinamkasgkvklvvseeqedlivfegdgryavvcdpidgssnldagvsvgtifgvyklpegssgsikdvlrpgkemvaagytmygasanlvlstgngcngftlddplgefilthpdlklpdlrsiysvnegnsslwsdnvkdyfkalkfpedgskpysaryigsmvadvhrtilyggmfaypadskskkgklrllyegfpmayiieqagglaindngerildlvpteihersgvwlgskgeiekakkyllkYALI0E11099gDNA:(SEQ ID NO: 144)atgcgactcactctgccccgacttaacgccgcctacattgtaggagccgcccgaactcctgtcggcaagttcaacggagccctcaagtccgtgtctgccattgacctcggtatcaccgctgccaaggccgctgtccagcgatccaaggtccccgccgaccagattgacgagtttctgtttggccaggtgctgaccgccaactccggccaggcccccgcccgacaggtggttatcaagggtggtttccccgagtccgtcgaggccaccaccatcaacaaggtgtgctcttccggcctcaagaccgtggctctggctgcccaggccatcaaggccggcgaccgaaacgttatcgtggccggtggaatggagtccatgtccaacaccccctactactccggtcgaggtcttgttttcggcaaccagaagctcgaggactccatcgtcaaggacggtctctgggacccctacaacaacatccacatgggcaactgctgcgagaacaccaacaagcgagacggcatcacccgagagcagcaggacgagtacgccatcgagtcctaccgacgggccaacgagtccatcaagaacggcgccttcaaggatgagattgtccccgttgagatcaagacccgaaagggcaccgtgactgtctccgaggacgaggagcccaagggagccaacgccgagaagctcaagggcctcaagcctgtctttgacaagcagggctccgtcactgccggtaacgcctcccccatcaacgatggtgcttctgccgttgtcgttgcctctggcaccaaggccaaggagctcggtacccccgtgctcgccaagattgtctcttacgcagacgccgccaccgcccccattgactttaccattgctccctctctggccattcccgccgccctcaagaaggctggccttaccaaggacgacattgccctctgggagatcaacgaggccttctccggtgtcgctctcgccaacctcatgcgactcggaattgacaagtccaaggtcaacgtcaagggtggagctgttgctctcggccaccccattggtgcctccggtaaccgaatctttgtgactttggtcaacgccctcaaggagggcgagtacggagttgccgccatctgcaacggtggaggagcttccaccgccatcgtcatcaagaaggtctcttctgtcgagtagProtein:(SEQ ID NO: 145)mrltlprlnaayivgaartpvgkfngalksvsaidlgitaakaavqrskvpadqideflfgqvltansgqaparqvvikggfpesveattinkvcssglktvalaaqaikagdrnvivaggmesmsntpyysgrglvfgnqkledsivkdglwdpynnihmgnccentnkrdgitreqqdeyaiesyrranesikngafkdeivpveiktrkgtvtvsedeepkganaeklkglkpvfdkqgsvtagnaspindgasavvvasgtkakelgtpvlakivsyadaatapidftiapslaipaalkkagltkddialweineafsgvalanlmrlgidkskvnvkggavalghpigasgnrifvtlvnalkegeygvaaicngggastaivikkvssveYALI0E34793gDNA:(SEQ ID NO: 146)atgtctgccaacgagaacatctcccgattcgacgcccctgtgggcaaggagcaccccgcctacgagctcttccataaccacacacgatctttcgtctatggtctccagcctcgagcctgccagggtatgctggacttcgacttcatctgtaagcgagagaacccctccgtggccggtgtcatctatcccttcggcggccagttcgtcaccaagatgtactggggcaccaaggagactcttctccctgtctaccagcaggtcgagaaggccgctgccaagcaccccgaggtcgatgtcgtggtcaactttgcctcctctcgatccgtctactcctctaccatggagctgctcgagtacccccagttccgaaccatcgccattattgccgagggtgtccccgagcgacgagcccgagagatcctccacaaggcccagaagaagggtgtgaccatcattggtcccgctaccgtcggaggtatcaagcccggttgcttcaaggttggaaacaccggaggtatgatggacaacattgtcgcctccaagctctaccgacccggctccgttgcctacgtctccaagtccggaggaatgtccaacgagctgaacaacattatctctcacaccaccgacggtgtctacgagggtattgctattggtggtgaccgataccctggtactaccttcattgaccatatcctgcgatacgaggccgaccccaagtgtaagatcatcgtcctccttggtgaggttggtggtgttgaggagtaccgagtcatcgaggctgttaagaacggccagatcaagaagcccatcgtcgcttgggccattggtacttgtgcctccatgttcaagactgaggttcagttcggccacgccggctccatggccaactccgacctggagactgccaaggctaagaacgccgccatgaagtctgctggcttctacgtccccgataccttcgaggacatgcccgaggtccttgccgagctctacgagaagatggtcgccaagggcgagctgtctcgaatctctgagcctgaggtccccaagatccccattgactactcttgggcccaggagcttggtcttatccgaaagcccgctgctttcatctccactatttccgatgaccgaggccaggagcttctgtacgctggcatgcccatttccgaggttttcaaggaggacattggtatcggcggtgtcatgtctctgctgtggttccgacgacgactccccgactacgcctccaagtttcttgagatggttctcatgcttactgctgaccacggtcccgccgtatccggtgccatgaacaccattatcaccacccgagctggtaaggatctcatttcttccctggttgctggtctcctgaccattggtacccgattcggaggtgctcttgacggtgctgccaccgagttcaccactgcctacgacaagggtctgtccccccgacagttcgttgataccatgcgaaagcagaacaagctgattcctggtattggccatcgagtcaagtctcgaaacaaccccgatttccgagtcgagcttgtcaaggactttgttaagaagaacttcccctccacccagctgctcgactacgcccttgctgtcgaggaggtcaccacctccaagaaggacaacctgattctgaacgttgacggtgctattgctgtttcttttgtcgatctcatgcgatcttgcggtgcctttactgtggaggagactgaggactacctcaagaacggtgttctcaacggtctgttcgttctcggtcgatccattggtctcattgcccaccatctcgatcagaagcgactcaagaccggtctgtaccgacatccttgggacgatatcacctacctggttggccaggaggctatccagaagaagcgagtcgagatcagcgccggcgacgtttccaaggccaagactcgatcatagProtein:(SEQ ID NO: 147)msanenisrfdapvgkehpayelfhnhtrsfvyglqpracqgmldfdfickrenpsvagviypfggqfvtkmywgtketllpvyqqvekaaakhpevdvvvnfassrsvysstmelleypqfrtiaiiaegvperrareilhkaqkkgvtiigpatvggikpgcfkvgntggmmdnivasklyrpgsvayvsksggmsnelnniishttdgvyegiaiggdrypgttfidhilryeadpkckiivllgevggveeyrvieavkngqikkpivawaigtcasmfktevqfghagsmansdletakaknaamksagfyvpdtfedmpevlaelyekmvakgelsrisepevpkipidyswaqelglirkpaafistisddrgqellyagmpisevfkedigiggvmsllwfrrrlpdyaskflemvlmltadhgpavsgamntiittragkdlisslvaglltigtrfggaldgaatefttaydkglsprqfvdtmrkqnklipgighrvksrnnpdfrvelvkdfvkknfpstqlldyalaveevttskkdnlilnvdgaiavsfvdlmrscgaftveetedylkngvlnglfvlgrsigliahhldqkrlktglyrhpwdditylvgqeaiqkkrveisagdvskaktrsYALI0D24431gDNA:(SEQ ID NO: 148)atgtcagcgaaatccattcacgaggccgacggcaaggccctgctcgcacactttctgtccaaggcgcccgtgtgggccgagcagcagcccatcaacacgtttgaaatgggcacacccaagctggcgtctctgacgttcgaggacggcgtggcccccgagcagatcttcgccgccgctgaaaagacctacccctggctgctggagtccggcgccaagtttgtggccaagcccgaccagctcatcaagcgacgaggcaaggccggcctgctggtactcaacaagtcgtgggaggagtgcaagccctggatcgccgagcgggccgccaagcccatcaacgtggagggcattgacggagtgctgcgaacgttcctggtcgagccctttgtgccccacgaccagaagcacgagtactacatcaacatccactccgtgcgagagggcgactggatcctcttctaccacgagggaggagtcgacgtcggcgacgtggacgccaaggccgccaagatcctcatccccgttgacattgagaacgagtacccctccaacgccacgctcaccaaggagctgctggcacacgtgcccgaggaccagcaccagaccctgctcgacttcatcaaccggctctacgccgtctacgtcgatctgcagtttacgtatctggagatcaaccccctggtcgtgatccccaccgcccagggcgtcgaggtccactacctggatcttgccggcaagctcgaccagaccgcagagtttgagtgcggccccaagtgggctgctgcgcggtcccccgccgctctgggccaggtcgtcaccattgacgccggctccaccaaggtgtccatcgacgccggccccgccatggtcttccccgctcctttcggtcgagagctgtccaaggaggaggcgtacattgcggagctcgattccaagaccggagcttctctgaagctgactgttctcaatgccaagggccgaatctggacccttgtggctggtggaggagcctccgtcgtctacgccgacgccattgcgtctgccggctttgctgacgagctcgccaactacggcgagtactctggcgctcccaacgagacccagacctacgagtacgccaaaaccgtactggatctcatgacccggggcgacgctcaccccgagggcaaggtactgttcattggcggaggaatcgccaacttcacccaggttggatccaccttcaagggcatcatccgggccttccgggactaccagtcttctctgcacaaccacaaggtgaagatttacgtgcgacgaggcggtcccaactggcaggagggtctgcggttgatcaagtcggctggcgacgagctgaatctgcccatggagatttacggccccgacatgcacgtgtcgggtattgttcctttggctctgcttggaaagcggcccaagaatgtcaagccttttggcaccggaccttctactgaggcttccactcctctcggagtttaaProtein:(SEQ ID NO: 149)MsaksiheadgkallahflskapvwaeqqpintfemgtpklasltfedgvapeqifaaaektypwllesgakfvakpdqlikrrgkagllvlnksweeckpwiaeraakpinvegidgvlrtflvepfvphdqkheyyinihsvregdwilfyheggvdvgdvdakaakilipvdieneypsnatltkellahvpedqhqtlldfinrlyavyvdlqftyleinplvviptaqgvevhyldlagkldqtaefecgpkwaaarspaalgqvvtidagstkvsidagpamvfpapfgrelskeeayiaeldsktgaslkltvlnakgriwtlvagggasvvyadaiasagfadelanygeysgapnetqtyeyaktvldlmtrgdahpegkvlfigggianftqvgstfkgiirafrdyqsslhnhkvkiyvrrggpnwqeglrliksagdelnlpmeiygpdmhvsgivplallgkrpknvkpfgtgpsteastplgvYALI0E14190gDNA:(SEQ ID NO: 150)atggttattatgtgtgtgggacctcagcacacgcatcatcccaacacagggtgcagtatatatagacagacgtgttccttcgcaccgttcttcacatatcaaaacactaacaaattcaaaa gtgagtatcatggtgggagtcaattgattgctcggggagttgaacaggcaacaatggcatgcacagggccagtgaaggcagactgcagtcgctgcacatggatcgtggttctgaggcgttgctatcaaaagggtcaattacctcacgaaacacagctggatgttgtgcaatcgtcaattgaaaaacccgacacaatgcaagatctctttgcgcgcattgccatcgctgttgccatcgctgtcgccatcgccaatgccgctgcggattattatccctaccttgttccccgcttccgcacaaccggcgatgtctttgtatcatgaactctcgaaactaactcag tggttaaagctgtcgttgccggagccgctggtggtattggccagcccctttctcttctcctcaaactctctccttacgtgaccgagcttgctctctacgatgtcgtcaactcccccggtgttgccgctgacctctcccacatctccaccaaggctaaggtcactggctacctccccaaggatgacggtctcaagaacgctctgaccggcgccaacattgtcgttatccccgccggtatcccccgaaagcccggtatgacccgagacgatctgttcaagatcaacgctggtatcgtccgagatctcgtcaccggtgtcgcccagtacgcccctgacgcctttgtgctcatcatctccaaccccgtcaactctaccgtccctattgctgccgaggtcctcaagaagcacaacgtcttcaaccctaagaagctcttcggtgtcaccacccttgacgttgtccgagcccagaccttcaccgccgctgttgttggcgagtctgaccccaccaagctcaacatccccgtcgttggtggccactccggagacaccattgtccctctcctgtctctgaccaagcctaaggtcgagatccccgccgacaagctcgacgacctcgtcaagcgaatccagtttggtggtgacgaggttgtccaggctaaggacggtcttggatccgctaccctctccatggcccaggctggtttccgatttgccgaggctgtcctcaagggtgccgctggtgagaagggcatcatcgagcccgcctacatctaccttgacggtattgatggcacctccgacatcaagcgagaggtcggtgtcgccttcttctctgtccctgtcgagttcggccctgagggtgccgctaaggcttacaacatccttcccgaggccaacgactacgagaagaagcttctcaaggtctccatcgacggtctttacggcaacattgccaagggcgaggagttcattgttaaccctcctcctgccaagtaaProtein:(SEQ ID NO: 152)vvkavvagaaggigqplslllklspyvtelalydvvnspgvaadlshistkakvtgylpkddglknaltganivvipagiprkpgmtrddlfkinagivrdlvtgvaqyapdafvliisnpvnstvpiaaevlkkhnvfnpkklfgvttldvvraqtftaavvgesdptklnipvvgghsgdtivpllsltkpkveipadklddlvkriqfggdevvqakdglgsatlsmaqagfrfaeavlkgaagekgiiepayiyldgidgtsdikrevgvaffsvpvefgpegaakaynilpeandyekkllkvsidglygniakgeefivnpppakYALI0E22649gDNA:(SEQ ID NO: 151)atgactggcaccttacccaagttcggcgacggaaccaccattgtggttcttggagcctccggcgacctcgctaagaagaagacc gtgagtattgaaccagactgaggtcaattgaagagtaggagagtctgagaacattcgacggacctgattgtgctctggaccactcaattgactcgttgagagccccaatgggtcttggctagccgagtcgttgacttgttgacttgttgagcccagaacccccaacttttgccaccatacaccgccatcaccatgacacccagatgtgcgtgcgtatgtgagagtcaattgttccgtggcaaggcacagcttattccaccgtgttccttgcacaggtggtctttacgctctcccactctatccgagcaataaaagcggaaaaacagcagcaagtcccaacagacttctgctccgaataaggcgtctagcaagtgtgcccaaaactcaattcaaaaatgtcagaaacctgatatcaacccgtcttcaaaagctaaccccag ttccccgccctcttcggcctttaccgaaacggcctgctgcccaaaaatgttgaaatcatcggctacgcacggtcgaaaatgactcaggaggagtaccacgagcgaatcagccactacttcaagacccccgacgaccagtccaaggagcaggccaagaagttccttgagaacacctgctacgtccagggcccttacgacggtgccgagggctaccagcgactgaatgaaaagattgaggagtttgagaagaagaagcccgagccccactaccgtcttttctacctggctctgccccccagcgtatccttgaggctgccaacggtctgaagaagtatgtctaccccggcgagggcaaggcccgaatcatcatcgagaagccctttggccacgacctggcctcgtcacgagagctccaggacggccttgctcctctctggaaggagtctgagatcttccgaatcgaccactacctcggaaaggagatggtcaagaacctcaacattctgcgatttggcaaccagttcctgtccgccgtgtgggacaagaacaccatttccaacgtccagatctccttcaaggagccctttggcactgagggccgaggtggatacttcaacgacattggaatcatccgagacgttattcagaaccatctgttgcaggttctgtccattctagccatggagcgacccgtcactttcggcgccgaggacattcgagatgagaaggtcaaggtgctccgatgtgtcgacattctcaacattgacgacgtcattctcggccagtacggcccctctgaagacggaaagaagcccggatacaccgatgacgatggcgttcccgatgactcccgagctgtgacctttgctgctctccatctccagatccacaacgacagatgggagggtgttcctttcatcctccgagccggtaaggctctggacgagggcaaggtcgagatccgagtgcagttccgagacgtgaccaagggcgttgtggaccatctgcctcgaaatgagctcgtcatccgaatccagccctccgagtccatctacatgaagatgaactccaagctgcctggccttactgccaagaacattgtcaccgacctggatctgacctacaaccgacgatactcggacgtgcgaatccctgaggcttacgagtctctcattctggactgcctcaagggtgaccacaccaactttgtgcgaaacgacgagctggacatttcctggaagattttcaccgatctgctgcacaagattgacgaggacaagagcattgtgcccgagaagtacgcctacggctctcgtggccccgagcgactcaagcagtggctccgagaccgaggctacgtgcgaaacggcaccgagctgtaccaatggcctgtcaccaagggctcctcgtgaProtein:(SEQ ID NO: 153)mtgtlpkfgdgttivvlgasgdlakkktfpalfglyrngllpknveiigyarskmtqeeyherishyfktpddqskeqakkflentcyvqgpydgaegyqrlnekieefekkkpephyrlfylalppsvfleaanglkkyvypgegkariiiekpfghdlassrelqdglaplwkeseifridhylgkemvknlnilrfgnqflsavwdkntisnvqisfkepfgtegrggyfndigiirdviqnhllqvlsilamerpvtfgaedirdekvkvlrcvdilniddvilgqygpsedgkkpgytdddgvpddsravtfaalhlqihndrwegvpfilragkaldegkveirvqfrdvtkgvvdhlprnelviriqpsesiymkmnsklpgltaknivtdldltynrrysdvripeayeslildclkgdhtnfvrndeldiswkiftdllhkidedksivpekyaygsrgperlkqwlrdrgyvrngtelyqwpvtkgssYALI0B15598gDNA:(SEQ ID NO: 154)atgactgacacttcaaacatcaa gtgagtattgccgcacacaattgcaatcaccgccgggctctacctcctcagctctcgacgtcaatgggccagcagccgccatttgaccccaattacactggttgtgtaaaaccctcaaccacaatcgcttatgctcaccacagactacgacttaaccaagtcatgtcacaggtcaaagtaaagtcagcgcaacaccccctcaatctcaacacacttttgctaactcag gcctgtcgctgacattgccctcatcggtctcgccgtcatgggccagaacctgatcctcaacatggccgaccacg gtaagtatcaattgactcaagacgcaccagcaagatacagagcatacccagcaatcgctcctctgataatcgccattgtaacactacgttggttagattgatctaaggtcgttgctggttccatgcacttccacttgctcatatgaagggagtcaaactctattttgatagtgtcctctcccatccccgaaatgtcgcattgttgctaacaatagg ctacgaggttgttgcctacaaccgaaccacctccaaggtcgaccacttcctcgagaacgaggccaagg gtgagtatccgtccagctatgctgtttacagccattgaccccaccttcccccacaattgctacgtcaccattaaaaaacaaaattaccggtatcggcaagctagactttcatgcaacctacgcagggtaacaagttgagtttcagccgtgcaccttacaggaaaaccagtcatacgccgaggcagtgtgaaagcgaaagcacacagcctacggtgattgattgcatttttttgacataggagggaaacacgtgacatggcaagtgcccaacacgaatactaacaaacag gaaagtccattattggtgctcactctatcaaggagctgtgtgctctgctgaagcgaccccgacgaatcattctgctcgttaaggccggtgctgctgtcgattctttcatcgaacagctcctgccctatctcgataagggtgatatcatcattgacggtggtaactcccacttccccgactccaaccgacgatacgaggagcttaacgagaagggaatcctctttgttggttccggtgtttccggcggtgaggagggtgcccgatacggtccctccatcatgcccggtggaaacaaggaggcctggccccacattaagaagattttccaggacatctctgctaaggctgatggtgagccctgctgtgactgggtcggtgacgctggtgccggccactttgtcaagatggttcacaacggtattgagtatggtgacatgcagcttatctgcgaggcttacgacctcatgaagcgaggtgctggtttcaccaatgaggagattggagacgttttcgccaagtggaacaacggtatcctcgactccttcctcattgagatcacccgagacatcttcaagtacgacgacggctctggaactcctctcgttgagaagatctccgacactgctggccagaagggtactggaaagtggaccgctatcaacgctcttgaccttggtatgcccgtcaccctgatcggtgaggccgtcttcgctcgatgcattctgccctcaagcaggagcgtgtccgagcttccaaggttcttgatggccccgagcccgtcaagttcactggtgacaagaaggagtttgtcgaccagctcgagcaggccctttacgcctccaagatcatctcttacgcccagggtttcatgcttatccgagaggccgccaagacctacggctgggagctcaacaacgccggtattgccctcatgtggcgaggtggttgcatcatccgatccgtcttccttgctgacatcaccaaggcttaccgacaggaccccaacctcgagaacctgctgttcaacgacttcttcaagaacgccatctccaaggccaacccctcttggcgagctaccgtggccaaggctgtcacctggggtgttcccactcccgcattgcctcggctctggctttctacgacggttaccgatctgccaagctccccgctaacctgctccaggcccagcgagactacttcggcgcccacacctaccagctcctcgatggtgatggaaagtggatccacaccaactggaccggccgaggtggtgaggtttcttcttccacttacgatgcttaaProtein:(SEQ ID NO: 155)mtdtsnikpvadialiglavmgqnlilnmadhgyevvaynrttskvdhfleneakgksiigahsikelcallkrprriillvkagaavdsfieqllpyldkgdiiidggnshfpdsnrryeelnekgilfvgsgvsggeegarygpsimpggnkeawphikkifqdisakadgepccdwvgdagaghfvkmvhngieygdmqliceaydlmkrgagftneeigdvfakwnngildsflieitrdifkyddgsgtplvekisdtagqkgtgkwtainaldlgmpvtligeavfarclsalkqervraskvldgpepvkftgdkkefvdqleqalyaskiisyaqgfmlireaaktygwelnnagialmwrggciirsvfladitkayrqdpnlenllfndffknaiskanpswratvakavtwgvptpafasalafydgyrsaklpanllqaqrdyfgahtyqlldgdgkwihtnwtgrggevssstydaYALI0D06303gDNA:(SEQ ID NO: 156)atgctcaaccttagaaccgcccttcgagctgtgcgacccgtcactct ggtgagtatctcggagcccgggacggctaccaacacacaagcaagatgcaacagaaaccggactttttaaatgcggattgcggaaaatttgcatggcggcaacgactcggagaaggagcgggacaattgcaatggcaggatgccattgacgaactgagggtgatgagagaccgggcctccgatgacgtggtggtgacgacagcccggctggtgttgccgggactgtctctgaaaagcaatttctctatctccggtctcaacagactccccttctctagctcaattggcattgtcttcagaaggtgtcttagtggtatccccattgttatcttcttttccccaatgtcaatgtcaatgtcaatggctccgacctctttcacattaacacggcgcaaacacagataccacggaaccgactcaaacaaatccaaagagacgcagcggaataattggcatcaacgaacgatttgggatactctggcgagaatgccgaaatatttcgcttgtcttgttgtttctcttgagtgagttgtttgtgaagtcgtttggaagaaggttcccaatgtcacaaaccataccaactcgttacagccagcttgtaatcccccacctcttcaatacatactaacgcag acccgatcctacgccacttccgtggcctctttcaccggccagaagaactccaacggcaagtacactgtgtctctgattgagggagacggtatcggaaccgagatctccaaggctgtcaaggacatctaccatgccgccaaggtccccatcgactgggaggttgtcgacgtcacccccactctggtcaacggcaagaccaccatccccgacagcgccattgagtccatcaaccgaaacaaggttgccctcaagggtcccctcgccacccccatcggtaagggccacgtttccatgaacctgactctgcgacgaaccttcaacctgttcgccaacgtccgaccttgcaagtccgtcgtgggctacaagaccccttacgagaacgtcgacaccctgctcatccgagagaacactgagggtgagtactccggtatcgagcacaccgtcgtccccggtgtcgttcagtccatcaagctgatcacccgagaggcttccgagcgagtcatccggtacgcttacgagtacgccctgtcccgaggcatgaagaaggtccttgttgtccacaaggcctctattatgaaggtctccgatggtcttttccttgaggttgctcgagagctcgccaaggagtacccctccattgacctttccgtcgagctgatcgacaacacctgtctgcgaatggtccaggaccccgctctctaccgagatgtcgtcatggtcatgcccaacctttacggtgacattctgtccgatcttgcctccggtcttatcggtggtcttggtctgaccccctccggtaacatgggtgacgaggtctccatcttcgaggccgtccacggatccgctcccgacattgctggcaagggtcttgctaaccccactgctctgctgctctcctccgtgatgatgctgcgacacatgggtctcaacgacaacgccaccaacatcgagcaggccgtctttggcaccattgcttccggccccgagaaccgaaccaaggatcttaagggtaccgccaccacttctcactttgctgagcagattatcaagcgactcaagtagProtein:(SEQ ID NO: 157)mlnlrtalravrpvtltrsyatsvasftgqknsngkytvsliegdgigteiskavkdiyhaakvpidwevvdvtptlvngkttipdsaiesinrnkvalkgplatpigkghvsmnltlrrtfnlfanvrpcksvvgyktpyenvdtllirentegeysgiehtvvpgvvqsiklitreaserviryayeyalsrgmkkvlvvhkasimkvsdglflevarelakeypsidlsvelidntclrmvqdpalyrdvvmvmpnlygdilsdlasgligglgltpsgnmgdevsifeavhgsapdiagkglanptalllssvmmlrhmglndnatnieqavfgtiasgpenrtkdlkgtattshfaeqiikrlk Example 13 Determination of Lipid Levels of Y. lipolytica 12A. Determination of Lipid Levels of Y. lipolytica in Various Growth Conditions of Varying Carbon to Nitrogen Ratios. Shake flask testing was conducted using carbon to nitrogen (C/N) ratios of 160, 80, 60, 40, 30, 20, and 10 with yeast nitrogen base being the base medium providing vitamins, trace elements and salts. Ammonium sulfate (which contains 21% nitrogen) was used as the nitrogen source and glucose (which contains 40% carbon) was used as the carbon source at a concentration of 30 g/L. The concentrations of ammonium sulfate corresponding to these ratios are: 0.36, 0.71, 0.95, 1.43, 1.91, 2.86, and 4.6 g/L, respectively. Uracil was supplemented at 0.2 mM. As controls, strains were also grown in yeast extract-peptone with 50 g/L of glucose (media in which lipids do not accumulate at high levels) and yeast extract-peptone with 5% olive oil (v/v) (media in which lipids accumulate at high levels). Strain MF760 (10-14 ml of culture) was harvested after 4 days of growth at 30° C., during which time the cultures were shaking at 250 rpm. Following harvesting, cells were washed three times with water, with the exception of the oil-grown cells which were washed three times in 0.5% BSA and one time with water before lipid extractions. Lipids were extracted as described in Folch J, Lees, M, and Stanley, G. H. S. J. Biol. Chem. 226: 497-509, 1957. In brief, cell pellets were resuspended in 6 ml of water. A 1 ml aliquot was transferred to a pre-weighed tube with a hole on the lid, spun down and the cell pellet lyophilized overnight to determine the dry cell weight. The remaining 5 ml were placed in a 15 ml Falcon tube and spun down. Cell pellets were frozen at −20° C. until extractions were performed. Two to three volumes of a Zymolyase solution (2 mg/ml Zymolyase 100T in 1M Sorbitol, 50 mM EDTA and 0.01% β-mercaptoethanol) was added to each cell pellet and placed at 37° C. with constant agitation for 1 hr. Two volumes of cubic zirconia beads were added to each tube and vortexed for 15-20 min. Samples were viewed under a microscope to ensure cell breakage before continuing with extractions. After cell breakage was complete, 6 ml of extraction solvent was added (a 2:1 mix of chloroform and methanol) and mixed. The mixture was spun down for 5 min at 3000 rpm and the organic layer was transferred to a clean tube. NaCl was added to the remaining aqueous layer to make it a 0.29% NaCl solution. 6 ml of extraction solvent was added and mixed, and the mixture was spun down for 5 min. The organic layers were pooled and filtered through a 0.2 μm filter to get rid of any cell debris. The extract was washed with 0.2 volumes of 0.29% NaCl solution and another 6 ml of extraction solvent added and mixed. Mixtures were spun and the organic layer was placed in a pre-weighed glass vial, the solvent was evaporated under a flow on nitrogen and the vial was weighed again to determine the weight of the lipid extracted. The dry cell weight is used to determine the percentage of lipid per dry cell weight. The lipid accumulation results are in the Table 48 below: TABLE 48Lipid accumulation under various carbon:nitrogenratio growth conditionsC/N Ratio% lipidYNB160613% Glucose804960344017301620141015YEP5% Glucose225% olive oil38 Other nitrogen sources tested were proline (12% nitrogen), sodium glutamate (7% nitrogen), soy acid hydrolysate (12% nitrogen), and yeast extract-peptone (26.8% nitrogen). All nitrogen sources tested at C/N ratios of 80 (with glucose as a carbon source), had significantly larger lipid bodies than at C/N ratios of 10 (also with glucose as a carbon source). Strains MF858 and MF921 (example 2F and 2H) were harvested after 4 days of growth at 30° C. (3% glucose was used as the carbon source). Cells were washed three times with water and lipids extracted as described above. Lipid accumulation data for soy hydrolysate, yeast extract-peptone and yeast nitrogen base, used as a control, are listed in Table 49 below. TABLE 49Lipid accumulation under different carbon andnitrogen conditions with various nitrogen sources% lipidC/N RatioMF858MF921Soy hydrolysate803636603635101415Yeast Extract-803737Peptone101514Yeast Nitrogen803738Base101311 12b. Determination of Lipid Levels Under High Carbon and Phosphate or Magnesium Limiting Conditions. To test whether other nutrient limitations, under high carbon conditions, will allow for higher lipid accumulation, phosphate or magnesium limiting conditions were tested. For phosphate limiting conditions, yeast nitrogen base medium without phosphate was prepared. Shake flask testing was performed using carbon to phosphate ratios ranging from 5376 down to 42. This range corresponds to 7.8 mg/L up to 1 g/L, respectively, and the latter concentration corresponds to that are commonly used in yeast nitrogen base medium. Glucose, at 30 g/L, was used at the carbon source. Potassium phosphate monobasic (containing 28.7% phosphate) was used as the phosphate source. For magnesium limiting conditions, yeast nitrogen base medium without magnesium was prepared. Shake flask testing was conducted using carbon to magnesium ratios ranging from 31360 down to 245. This range corresponds to 0.375 mg/L up to 0.5 g/L, and the latter magnesium concentration corresponds to that commonly used in yeast nitrogen base. Glucose, at 30 g/L, was used as the carbon source. Magnesium sulfate (containing 9.8% magnesium) was used as the magnesium source. Strains MF858 and MF921 were harvested after 4 days of growth at 30° C., during which time the cultures were shaking at 250 rpm. Cells were washed three times with water before lipid extraction. Lipids were extracted as described above. Lipid accumulation data is listed in the Table 50 below: TABLE 50Lipid accumulation in phosphate or magnesiumlimiting growth conditions% Lipidg/LMF858MF921phosphate114140.062518200.031334410.015662630.00788376magnesium0.512110.0313NA160.0156NA250.0078NA420.00394848 Example 14 Effect of Temperature on Carotenoid Production MF740 was transformed with pMB4719 with SalI, and a Ura + colony was designated ML878. MF740 was transformed with pMB4629 cleaved with SalI, an Ade + colony was designated ML857, and subsequently transformed with pMB4719 cleaved with SalI, to create ML836. ML878 and ML836 were grown for 4 days in YPD at 20° C., 24° C., and 28° C., and carotenoids were extracted and analyzed by HPLC. β-carotene or zeaxanthin yield (% dry cell weight) at 20° C. was chosen as a standard against which yields at other temperatures were compared. In addition, the ratio of zeaxanthin/carotenoid (% dry cell weight) was calculated for each temperature. Whereas the β-carotene levels fell with decreasing temperatures, the ratio of zeaxanthin to β-carotene increased with lower temperatures (Table 51). TABLE 51Effect of Temperature on carotenoid productionZeaxanthin/β-caroteneTemperatureβ-caroteneZeaxanthinratioStrain(° C.)yield*yield**(% dry cell weight)***MF878201.01.02.4MF878241.31.01.9MF878283.21.51.1MF836201.01.01.0MF836241.91.20.7MF836283.41.10.4*β-carotene yield is calculated as % DCW β-carotene at 20° C. divided by % DCW β-carotene at each temperature**Zeaxanthin yield is calculated as % DCW zeaxanthin at 20° C. divided by % DCW zeaxanthin at each temperature***Zeaxanthin/β-carotene ratio is calculated as % DCW zeaxanthin divided by % DCW β-carotene Example 15 Construction of a Recyclable URA3 Marker Plasmid pMB5082 To create a selectively excisable (“recyclable”) URA3 marker, an 860 bp SpeI-SacI (blunt ended with T4 DNA ligase) fragment (containing the URA3 promoter and the first 121 nucleotides of the URA3 gene) from plasmid pMB4691 was inserted into the SpeI-NotI sites of plasmid pMB4534 to create pMB5055. The URA3 promoter was excised from pMB5055 as an 878 bp fragment by XbaI-SpeI digest, and was ligated into XbaI-cleaved pMB4691. Orientation of the promoter was verified by restriction digest. The resulting plasmid, designated pMB5082, contained the URA3 promoter both upstream of the URA3 gene and downstream of its terminator. This cassette, once integrated into the Yarrowia genome, permits excision of the URA3 marker by homologous recombination between the two copies of the URA3 promoter. Colonies containing the excision may be selected on 5-FOA. Example 16 Effects of Mutations in the Transcriptional Regulator, SPT8 on Carotenoid Production Y. Lipolytica strain ML1018 was isolated by plasmid insertion mutagenesis. ML1018 was darker in hue, shiny, exclusively yeast-form rather than partial mycelial morphology and exhibited increased carotenoid levels when compared to its sibling transformants. Sequence analysis identified the site of ML1018 plasmid insertion between base pairs 701 and 702 of the SPT8 coding sequence. Experiments were undertaken to examine carotenoid levels in a targeted SPT8 disruption strain. A 2.5 kb fragment containing the SPT8 gene (YALI0E23804g) with its endogenous promoter and terminator was amplified from genomic DNA isolated from Y. lipolytica strain NRRL Y-1095 using primers: MO5651 (5′-CACAAACTAGTGTCAGGAATATGAAACCAGG-3′) (SEQ ID NO:158) and MO5652 (5′-CACAAACTAGTGCATGTGATAGGAAGGAGGA-3′) (SEQ ID NO:159). Plasmid pMB5083 was constructed by phosphorylating the 2.5 kb SPT8 fragment with T4 polynucleotide kinase and ligating the phosphorylated fragment with desphosphorylated, EcoRV-digested pBluescriptSK−. A 3.4 kb fragment containing the TEF1 promoter, XPR terminator, and a recyclable URA3 marker was isolated from plasmid pMB5082 by Acc65I and XbaI (subsequently made blunt with Klenow) digestion. This fragment was cloned into the BsiWI and SmaI sites of pMB5083 to create pMB5086. BamHI-XbaI digestion of pMB5086 yields a 5.6 kb Y. Lipolytica SPT8 disruption fragment containing the TEF1 promoter and XPR terminators followed by a recyclable URA3 marker between base pairs 752 and 753 of the SPT8 coding sequence (SPT8::URA3 disruption cassette). A 3.6 kb fragment containing the XPR terminator and ADE1 gene was excised from plasmid pMB4629 by MluI and EcoRV digest and subsequently cloned into MulI-PmlI-digested pMB5086. The resulting plasmid, pMB5124, contains a 5.8 kb BamHI-XbaI SPT8 disruption cassette similar to that in pMB5086, with the distinction that the recyclable URA3 marker is replaced with a non-recyclable ADE1 marker (SPT8::ADE1 disruption cassette). Y. lipolytica strains MF740 and MF746 (both ade1 ura3) are transformed with a 5.8 kb BamHI-XbaI fragment from pMB5124 (spt8::ADE1). spt8 disruptants are distinguished from ectopic integrants by colony morphology, as spt8 strains are shinier, darker in hue, and less mycelial than SPT8 strains. Correct integration may be assayed by PCR or by Southern blotting. Carotenoid yield is assayed in spt8 disrupted and SPT8′ strains by harvesting carotenoids after a four-day fermentation in YPD shake flasks at 30° C. Example 17 Construction plasmid pMB4844 Encoding a Chimeric β-carotene Hydroxylase-Ketolase (crtZW) A β-carotene hydroxylase:β-carotene ketolase chimera is constructed as follows. First, a 0.5 kb fragment containing crtZ from Erythrobacter litoralis is amplified from pMB4715, a plasmid containing a copy of the crtZ gene, using primers MO4814: 5′-CACAACGTCTCTCTAGACACAAAAATGAGCT-3′ (SEQ ID NO:160) and MO4816: 5′-CACAACGTCTCAGCCGGCACCTGCTCCCATAGAATCTCG-3′ (SEQ ID NO:161) and the resulting fragment is digested with XbaI and BsmBI. Similarly, a 0.8 kb fragment containing crtW from Parvularcula bermudensis is amplified from pMB4731, a plasmid containing a copy of the crtW gene, with primers MO5060: 5′-CACAAGAAGACAACGGCGCAGGAGCCATGGACCCTACCGGAGACG-3′ (SEQ ID NO:162) and MO5061: 5′-CACAAGAAGACAACGCGTTTAAGGGCCGGTTCTCTTTC-3′ (SEQ ID NO:163) and the resulting fragment is digested with BbsI and MluI. The digested fragments containing the crtZ and crtW genes are then ligated in a three-piece reaction into NheI-MluI cleaved vector pMB4691 to create pMB4844. Sequence analysis confirms the creation of an in-frame fusion of crtZ and crtW placed under control of the TEF1 promoter and the XPR terminator. The chimeric sequence is designated crtZW. The amino acid sequence of crtZW is: (SEQ ID NO: 175)mswwaialivfgavvgmeffawfahkyimhgwgwswhrdhhephdntlekndlfavvfgsvaallfvigalwsdplwwaavgitlygviytlvhdglvhqrywrwtpkrgyakrlvqahrlhhatvgkeggvsfgfvfardpaklkaelkqqreqglavvrdsmgagagagamdptgdvtasprpqttipvrqalwglslagaiiaawvfmhigfvffapldpivlalapviillqswlsvglfiishdaihgslapgrpafnramgrlcmtlyagfdfdrmaaahhrhhrspgtaadpdfsvdspdrplpwfgaffrryfgwrpfltvnavvftywlvlganpvnivlfygvpallsagqlfyfgtflphrherqgfadhhrarsvrspymlslvtcyhfggyhhehhlfphepwwrlpqrggwerdrrkrtgp Example 18 pH Effects on Total Carotenoid Yield and Hydroxylation of Beta-Carotene The effect of altering pH on total carotenoid yield and relative amount of individual carotenoids was investigated. Strain ML1011 (MF740 transformed with multiple integrated copies of the X. autotrophicus crtZ gene) which accumulates a mixture of carotenoids comprising beta-carotene, beta-cryptoxanthin, and zeaxanthin was fermented under the following parameters. Batch medium: YPDTemperature setpoint: 30° C.Initial volume: 210 mlVessel volume: 400 mlAgitation rate: 1000 rpmFeed: 40% glucoseFeed rate: 2 ml/hour, starting at 24th hour after inoculation Four separate fermentor units were setup and the pH was controlled as follows: Unit 1: pH 5.5Unit 2: pH 7.0Unit 3: pH 7.0 at inoculation, continuously rising to a setpoint of pH 8.0 at 48 hours (change of 0.021 pH units/hour)Unit 4: pH 7.0 at inoculation, continuously rising to a setpoint of pH 9.0 at 48 hours (change of 0.042 pH units/hour Additionally, the glucose feed of unit 4 was halted at 64 hours (see below). FIG. 12 a depicts accumulation of total carotenoid (absorbance units per unit dry cell weight) throughout the fermentation. Excluding the last timepoint, units 1 and 2 accumulated similar amounts of carotenoid throughout the run. This result, consistent with previous experiments, suggests that varying the pH in the range of 5.5-7.0 does not affect total carotenoid yield. During this same period, fermentor unit 3 accumulated more carotenoid than units 1 and 2, suggesting setting pH to be within the range of 7.0-8.0 improves the rate of carotenoid biosynthesis. In unit 4, carbon dioxide evolution (indicating metabolic activity) and carotenoid accumulation started to fall precipitiously when the unit reached pH 8.3 at approximately 31 hours ( FIG. 12 d ), suggesting toxicity due to high pH. The feed to this unit was therefore stopped at 64 hours. Together, these results suggest that carotenoid yield may be maximized by maintaining pH within the range 7.0-8.0, while pH levels below or above this range were ineffective or toxic, respectively. FIG. 12 b depicts accumulation of zeaxanthin (absorbance units per dry cell weight; AU) over the course of the fermentation. As seen in FIG. 12 b , zeaxanthin accumulation improves with increasing pH. Unit 4, at highest pH, shows superior zeaxanthin accumulation compared to all other units until hour 64, when its feed was terminated. Likewise, unit 3, maintained at pH 8.0 after hour 48, shows significantly improved zeaxanthin accumulation over units 1 and 2, maintained at pH 5.5 and 7.0, respectively. These results indicate that hydroxylation of beta carotene to zeaxanthin is favored by higher pH. FIG. 12 c depicts the fraction of carotenoid as zeaxanthin (AU zeaxanthin/AU total carotenoid) throughout the course of the fermentation. Unit 3 hydroxylated a greater fraction of beta-carotene than units 1 and 2, in addition to producing more total carotenoid ( FIG. 12 a ) and more total zeaxanthin ( FIG. 12 b ). This result demonstrates that at pH 8.0, zeaxanthin accumulation outpaced the global increase in carotenoid biosynthesis also seen at this pH As seen in FIG. 12 e , biomass accumulated fastest in unit 3 and remained above all other units until the hundred-thirtieth or so hour of fermentation. This unit similarly was the most metabolically active, as shown by its increased rate of carbon dioxide evolution compared to the other units over the same time period ( FIG. 12 d ). The subsequent decline in biomass in this unit may be attributed to accelerated metabolism of carbon stored as intracellular oil, relative to the other three units. Thus, it appears that the pH range of 7.0-8.0 enables Yarrowia lipolytica both to accumulate biomass and metabolize stored carbon at rates faster than it is able at lower pH. Together, these results indicate that total biomass accumulation, percentage of biomass representing carotenoid accumulation, and the hydroxylation of beta-carotene to zeaxanthin may be manipulated by maintaining fermentation pH in the approximate range of 7.0-8.0. Moreover, these results suggest that within this same range, an optimum pH may be selected at which to maximize production of both non-oxygenated carotenoids and xanthophylls (e.g. hydroxylation of b-carotene to zeaxanthin and total carotenoid production. Example 19 Lycopene Epsilon Cyclase Sequences The DNA and proteins they encode of the certain lycopene epsilon cyclase sequences are provided below. Corresponding Genbank Accession and GI numbers are found in table 23. Ostreococcus lucimarinus sequence XP_001422490DNA(SEQ ID NO: 164)ATGAAGGATGATCGCGAATGGATTGCGTTTCAACAGCGCAAGGTGTTTAGTGAGCAAAAGCAAATCAAAGAGTACCTCAGTGCTTTGAACGACCGCGACAAGGTCGACGTTCTCGTTGTCGGTGCGGGCCCCGCAGGTCTGGCGATCGCAGCGGAGACGGCGAAGAAGGGTCTTTCTGTTGGTCTCGTCGCACCAGACACCCCGTTCGTGAACAACTACGGAGTATGGCTCGACGAGTTCAAAGATCTAGGGCTCGAACACTGCTTGCTTCATAAGTATGACGACGCATTGGTTTGGTTCGATGATTCTGATCCTGCGAGTGGAACTGAACTCGGTCGACCTTACGGTCAAGTGTGCCGCAGGCGTCTTCGCGACCATTTGTTGAAGGAGTGCGCGGCGGCTGGCGTCAAGTATTTACCAGGCCTGGTAGATTTTGTGCGTCACGGTGACGTCGAAAAGAACGAGTTAGCCGAAGCAAACAGAGGCCAGCAATTCACGTTGAATTCGCGTCTCGTCGTTGCCGGCACCGGTCACAACCGCGACATGCTCAGCTACGAAGAGGGTGCGCCGCCGGGCTGGCAGACTGCGTATGGCGTTGAGGTGCGCATTCCGAACCACGGTTTTCCCGTGAACAAGGCCGTGTTCATGGATTTTCGTCAAAGCGATCCGGAGGCGATGAAAGAGGAACAAGACGAGGGCGTTTGGCGCGTGCCGTCTTTCCTTTACGTGTTACCCGTGGACAAGGATGTGGTGTTCGTCGAGGAGACGTGCCTCGTCGCGCGCGTACAAGTGCCGTTCGATGAACTCAAACGGCGATTGTATCGTCGTATGAAGCGGATGGGTATGGAAATCGTCGAAGAAGACATCTTGGAAGTCGAGGCGAGTTGGATTCCACTGGGCGGTACCCCGCCGGTTGCCCCGCAACGCACCATCGCGTACGGTGCAGCAGCCGGCATGGTCCACCCTGCGTCTGGCTACTCCGTCGTAAACAGTATTAGCAAAGCTCCGCGTGTTGCGACGGCCATGGCCGAAGGCTTGAAGGAGGGTGGCGAGATTGAGGCGAGCCGAAGAGCGTGGGAAATCCTTTGGGGTGCGGAGCCACGAAGACAAATCGGTTTCTACCAGTTCGGTATGGAGCTTCTCATGTCGCTTCGCATCGAGCAGATGCGCAACTTCTTTAGTACCTTCTTTGCGCTTCCAACAAATCTGAGCAGAGGATTTTTGGGTAACAGATTGTCGAGCTCAGAGTTGATCATGTTTGCTCTCACTACGTTCGCAATTGGTAACAACGAACTTCGTGGGTTGTTGCTCGCTCACCTGGTTTCAProtein(SEQ ID NO: 165)MKDDREWIAFQQRKVFSEQKQIKEYLSALNDRDKVDVLVVGAGPAGLAIAAETAKKGLSVGLVAPDTPFVNNYGVWLDEFKDLGLEHCLLHKYDDALVWFDDSDPASGTELGRPYGQVCRRRLRDHLLKECAAAGVKYLPGLVDFVRHGDVEKNELAEANRGQQFTLNSRLVVAGTGHNRDMLSYEEGAPPGWQTAYGVEVRIPNHGFPVNKAVFMDFRQSDPEAMKEEQDEGVWRVPSFLYVLPVDKDVVFVEETCLVARVQVPFDELKRRLYRRMKRMGMEIVEEDILEVEASWIPLGGTPPVAPQRTIAYGAAAGMVHPASGYSVVNSISKAPRVATAMAEGLKEGGEIEASRRAWEILWGAEPRRQIGFYQFGMELLMSLRIEQMRNFFSTFFALPTNLSRGFLGNRLSSSELIMFALTTFAIGNNELRGLLLAHLVSlycopene epsilon cyclase ( Diospyros kaki ) sequence BAE94036DNA(SEQ ID NO: 166)ACTACGGCGTATGGGAGGATGAATTTAGAGATCTTGGACTTGAAAGGTGTATTGAACATGTTTGGAGAGACACAATTGTATATCTTGATGACAATGATCCCATTCTGATTGGTCGTGCTTATGGACGAGTTAGTCGTCACTTGCTCCACGAGGAGCTATTAAGAAGGTGTGTGGAGTCAGGTGTTTCATATTTGAGCTCAAAAGTGGAAAGAATTATTGAAACTACGAATGGGCAGAGTCTCATAGAGTGCGGAACTGATGTTGTTGTCCCATGCAGGCTTGCTACTGTTGCTTCGGGAGCAGCTTCTGGGAAACTTTTGAAGTTTGAGGTGGGAGGACCCAGAGTTTCTGTTCAAACAGCTTATGGTGTGGAGGTTGAGGTGGAAAACAATCCATATGACCCCAACTTGATGGTTTTCATGGATTACAGAGACTATGCCAAACAAAAAGTTCAGCCTTTGGAAGCACAATATCCAACATTTCTTTATGCCATGCCTATGTCCCCTACAAGAGTCTTCTTTGAGGAAACTTGTTTGGCTTCAAAGGATGCCATGCCTTTTGATCTATTAAAGAGGAAACTCATGGACAGATTAGAGACAATGGGAGTCCATGTTCTAAAAACGTATGAGGAGGAATGGTCTTProtein(SEQ ID NO: 167)YGVWEDEFRDLGLERCIEHVWRDTIVYLDDNDPILIGRAYGRVSRHLLHEELLRRCVESGVSYLSSKVERIIETTNGQSLIECGTDVVVPCRLATVASGAASGKLLKFEVGGPRVSVQTAYGVEVEVENNPYDPNLMVFMDYRDYAKQKVQPLEAQYPTFLYAMPMSPTRVFFEETCLASKDAMPFDLLKRKLMDRLETMGVHVLKTYEEEWS Example 20 Construction of a Lutein Producing Strain The following sequence, optimized for Y. lipolytica codon bias and encoding a putative lycopene epsilon cyclase from Ostreococcus lucimarinus CCE9901, is synthesized de novo: (SEQ ID NO: 168)TTCTAGAACAAAATGAAGGACGACCGAGAGTGGATCGCCTTCCAGCAGCGAAAGGTGTTCTCTGAGCAGAAGCAGATCAAGGAGTACCTGTCTGCCCTGAACGACCGAGACAAGGTGGACGTGCTGGTGGTGGGCGCCGGCCCCGCCGGCCTGGCCATCGCCGCCGAGACCGCCAAGAAGGGCCTGTCTGTGGGCCTGGTGGCCCCCGACACCCCCTTCGTGAACAACTACGGCGTGTGGCTGGACGAGTTCAAGGACCTGGGCCTGGAGCACTGTCTGCTGCACAAGTACGACGACGCCCTGGTGTGGTTCGACGACTCTGACCCCGCCTCTGGCACCGAGCTGGGCCGACCCTACGGCCAGGTGTGTCGACGACGACTGCGAGACCACCTGCTGAAGGAGTGTGCCGCCGCCGGCGTGAAGTACCTGCCCGGCCTGGTGGACTTCGTGCGACACGGCGACGTGGAGAAGAACGAGCTGGCCGAGGCCAACCGAGGCCAGCAGTTCACCCTGAACTCTCGACTGGTGGTGGCCGGCACCGGCCACAACCGAGACATGCTGTCTTACGAGGAGGGCGCCCCCCCCGGCTGGCAGACCGCCTACGGCGTGGAGGTGCGAATCCCCAACCACGGCTTCCCCGTGAACAAGGCCGTGTTCATGGACTTCCGACAGTCTGACCCCGAGGCCATGAAGGAGGAGCAGGACGAGGGCGTGTGGCGAGTGCCCTCTTTCCTGTACGTGCTGCCCGTGGACAAGGACGTGGTGTTCGTGGAGGAGACCTGTCTGGTGGCCCGAGTGCAGGTGCCCTTCGACGAGCTGAAGCGACGACTGTACCGACGAATGAAGCGAATGGGCATGGAGATCGTGGAGGAGGACATCCTGGAGGTGGAGGCCTCTTGGATCCCCCTGGGCGGCACCCCCCCCGTGGCCCCCCAGCGAACCATCGCCTACGGCGCCGCCGCCGGCATGGTGCACCCCGCCTCTGGCTACTCTGTGGTGAACTCTATCTCTAAGGCCCCCCGAGTGGCCACCGCCATGGCCGAGGGCCTGAAGGAGGGCGGCGAGATCGAGGCCTCTCGACGAGCCTGGGAGATCCTGTGGGGCGCCGAGCCCCGACGACAGATCGGCTTCTACCAGTTCGGCATGGAGCTGCTGATGTCTCTGCGAATCGAGCAGATGCGAAACTTCTTCTCTACCTTCTTCGCCCTGCCCACCAACCTGTCTCGAGGCTTCCTGGGCAACCGACTGTCTTCTTCTGAGCTGATCATGTTCGCCCTGACCACCTTCGCCATCGGCAACAACGAGCTGCGAGGCCTGCTGCTGGCCCACCTGGTGTCTTAAACGCGT This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpCyOs1. A second putative lycopene epsilon cyclase from Ostreococcus lucimarinus CCE9901 is similarly codon-optimized and synthesized de novo: (SEQ ID NO: 169)TTCTAGAACAAAATGCGAGCCCGACGAGCCCCCGCCGCCCGAGTGACCCGAGCCATCCGAGCCCGAGGCGACGCCGGCACCCGAGCCCGAGACGTGGCCCCCGGCGCCACCCGACGAGGCGCCTCTGCCACCCCCCGAGCCACCCGACGACCCTCTGCCCGAGAGACCCGACCCGAGCTGTACGGCCTGGACGCCTCTTGGGACCCCCTGACCTCTGGCGACCGACGAGAGTCTGAGGAGTCTCGAACCCCCCTGCCCGAGACCCTGCCCAACGTGCGATGGGGCACCTCTGCCTCTGAGGCCTACGACCTGGTGATCGTGGGCTGTGGCCCCGCCGGCCTGACCGCCGCCGACGAGGCCTCTAAGCGAGGCCTGCGAGTGGCCCTGATGGACCCCTCTCCCCTGGCCCCCTGGATGAACAACTACGGCGTGTGGTGTGACGAGTTCAAGTCTCTGGGCTTCGACGACTGTTACCGAGCCGTGTGGAACAAGGCCCGAGTGATCATCGACGACGGCGACGCCGACGGCAAGATGCTGGACCGAGCCTACGCCCAGGTGGACCGAAAGAAGCTGAAGCAGAAGCTGATCGCCCGATCTGTGACCCAGGGCGTGGAGTTCGGCATCGCCGCCGTGGACTCTTGTGACAACTCTGACCCCAACCACTCTGTGGTGACCCTGTCTGACGGCCGAAAGGTGTACGCCAAGATGGTGCTGGACGCCACCGGCCACTCTCGAAAGCTGGTGGACTTCGACCGAGACTTCACCCCCGGCTACCAGGCCGCCTTCGGCATCGTGTGTACCGTGGAGAAGCACGACTTCCCCCTGGACACCATGCTGTTCATGGACTGGCGAGACGAGCACCTGTCTCCCGAGTTCAAGCGAGCCAACGACCGACTGCCCACCTTCCTGTACGCCATGCCCTTCTCTGAGACCGAGGTGTTCCTGGAGGAGACCTCTCTGGTGGCCCGACCCGGCCTGGAGTTCGACGACCTGAAGCTGAAGCTGAAGGAGCGACTGGACTACCTGGGCGTGAAGGTGACCAAGGTGCACGAGGAGGAGTACTGTCTGATCCCCATGGGCGGCGTGCTGCCCACCTTCCCCCAGCGAACCCTGGGCATCGGCGGCACCGCCGGCATGGTGCACCCCTCTACCGGCTTCATGGTGGCCAAGACCATGCTGTGTGTGCGAACCCTGGTGGGCACCCTGGACGAGGCCCTGAAGGCCGGCAAGCGAGGCGACATCACCGGCGCCCTGGAGGCCGCCGAGGCCGCCCAGATGAACAACGGCAAGTTCGACGCCGACGCCACCGCCGCCCTGGTGTGGAACTCTATCTGGCCCGAGAACGACCTGCGAATGCGAACCTTCATGTGTTTCGGCATGGAGACCCTGATGCAGCTGGACATCGACGGCACCCGACAGTTCTTCGACACCTTCTTCGACCTGCCCAAGGACGTGTGGGCCGGCTTCCTGTCTTGGCGAATCCAGCCCGTGGGCCTGCTGTCTCTGGGCGTGAACCTGTTCGCCCTGTTCTCTAACTACATGCGAGTGAACTTCGTGAAGTCTGCCCTGCCCTTCATGGGCTCTTTCTTCGCCAACTAAACGCGT This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpCyOs2. The following sequence, optimized for Y. lipolytica codon bias and encoding a putative carotene epsilon hydroxylase from Ostreococcus tauri , is synthesized de novo: (SEQ ID NO: 170)TTCTAGAACAAAATGAAGGACGGCCAGGACGAGGACTCTGACGAGATCTGGGGCGGCCAGCGACACGCCTCTGAGATGAAGACCCCCACCCGACGAAAGGCCCGAACCAAGGCCGAGCGAGAGGCCTCTGCCGCCTCTTACGAGTGGTCTGCCTGGGCCTCTTCTTGTGGCGTGATCTCTGTGGCCATCACCGCCACCTACTTCCGAATCCTGCGAGAGGTGGACGTGAACGGCGGCGTGTTCCCCGTGGCCGAGCTGGTGGCCCAGCTGGCCCTGATCGCCGGCGCCGCCGTGGGCATGGAGTTCTACGCCCGATACGCCCACAAGCACCTGTGGCACGGCTCTTGGTGGACCATGTCTAACAAGTACCGACAGGAGTGGAACCGACCCATCTGGCTGCTGCACGAGTCTCACCACCTGCCCCGAGAGGGCGCCTTCGAGGCCAACGACGTGTTCGCCCTGATGAACGGCGTGCCCGCCTTCGCCCTGTGTGCCTTCGGCTTCTTCACCCCCGGCGTGTTCGGCGGCCTGTGTTTCGGCGCCGGCCTGGGCATCACCCTGTTCGGCATCGCCTACATGTACGTGCACGACGGCCTGGTGCACAAGCGATTCCCCACCGGCCCCCTGGGCAAGCTGCCCGTGATGCGACGAATCGCCGCCGGCCACACCATCCACCACACCGAGGCCTTCGAGGGCGTGCCCTGGGGCCTGTTCCTGGGCATCCAGGAGCTGGCCGCCGTGCCCGGCGGCCTGGAGGAGCTGGAGAAGGTGGTGATCGCCGCCGAGCGAAAGGAGAAGCGAGACGAGCTGGAGCTGGCCCGACGAGCCTCTGTGGGCCTGGTGACCGAGGGCGCCCACATCCCCTCTATGAAGGAGGCCCCCCAGTGTAAGCTGCCCGAGGACCCCTAAACGCGT This fragment, liberated with XbaI and MluI, is cloned into NheI- and MluI-cleaved pMB5082 to produce pEpHyOs1. The 1.9 kb KpnI-SacI TEF1p-crtZ fragment from pMB4837 (example 10) is cloned into KpnI- and SacI-cleaved pMB5082 to create pCrtZ-Ub. A strain expressing carRP, carB, GGS, and HMG1 trunc and auxotrophic for ura3 (MF946; example 2F) is transformed successively, in any order, with the URA3 plasmids pEpCyOs1 (or pEpCyOs2), pEpHyOs1, and pCrtZ-Ub, with the recycling of the ura3 marker between each step, as described in Example 15. Such a strain is expected to produce >1 mg/gDCW lutein. This strain may be further modified by transformation with pMB4789 (erg9[F317I]-3′UTR::URA3), as described in example 2H. The following tables are referenced throughout the description. Each reference and information designated by each of the Genbank Accession and GI numbers are hereby incorporated by reference in their entirety. The order of genes, polypeptides and sequences presented in the tables is not indicative of their relative importance and/or suitability to any of the embodiments disclosed herein. TABLE 1Examples of acetyl-CoA carboxylase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONXP_41026349097606hypothetical protein AN6126.2 [ Aspergillus nidulans FGSC A4]XP_32958032418204hypothetical protein [ Neurospora crassa ]XP_38675646124405hypothetical protein FG06580.1 [ Gibberella zeae PH-1]XP_36770239972623hypothetical protein MG07613.4 [ Magnaporthe grisea 70-15]XP_50172150548503hypothetical protein [ Yarrowia lipolytica ]EAK9970846440402hypothetical protein CaO19.7466 [ Candida albicans SC5314]XP_45721150413128unnamed protein product [ Debaryomyces hansenii ]NP_98261245184894AAR071Wp [ Eremothecium gossypii ]XP_44923650293649unnamed protein product [ Candida glabrata ]NP_59327119114183acetyl-coa carboxylase [ Schizosaccharomyces pombe ]NP_0144136324343Acc1p [ Saccharomyces cerevisiae ]XP_45535550310667unnamed protein product [ Kluyveromyces lactis ]T4253111272737acetyl-CoA carboxylase (EC 6.4.1.2) - fission yeast( Schizosaccharomyces pombe )AAA20073171504acetyl-CoA carboxylaseEAL2017650257469hypothetical protein CNBF2520 [ Cryptococcus neoformans var.neoformans B-3501A]XP_57131658268320acetyl-CoA carboxylase, putative [ Cryptococcus neoformans var.neoformans JEC21]XP_40224449076566hypothetical protein UM04629.1 [ Ustilago maydis 521]S602002133343acetyl-CoA carboxylase (EC 6.4.1.2) - smut fungus ( Ustilago maydis )BAA244102804173acetyl-coenzyme A carboxylase like carboxylase [ Saccharomycescerevisiae ]P328741708192HFA1 proteinS550897438088probable acetyl-CoA carboxylase (EC 6.4.1.2) HFA1 - yeast( Saccharomyces cerevisiae )NP_99083645382859acetyl-Coenzyme A carboxylase alpha [ Gallus gallus ]CAE0147132526576Acetyl-CoA carboxylase 2 [ Homo sapiens ]AAR3701840019048acetyl-CoA carboxylase 2 [ Homo sapiens ]NP_001 . . .57164283acetyl-CoA carboxylase [ Ovis aries ]NP_77664927806341acetyl-coenzyme A carboxylase alpha [acetyl-coA carboxylase] [ Bostaurus ]CAI2527156205878acetyl-Coenzyme A carboxylase [ Mus musculus ]XP_10988351828611PREDICTED: acetyl-Coenzyme A carboxylase [ Mus musculus ]NP_94213438679971acetyl-Coenzyme A carboxylase alpha isoform 3 [ Homo sapiens ]NP_94213138679960acetyl-Coenzyme A carboxylase alpha isoform 1 [ Homo sapiens ]NP_94213538679974acetyl-Coenzyme A carboxylase alpha isoform 4 [ Homo sapiens ]NP_94213638679977acetyl-Coenzyme A carboxylase alpha isoform 2 [ Homo sapiens ]AAP9412233112885acetyl-CoA carboxylase 1 [ Homo sapiens ]NP_07152911559962acetyl-coenzyme A carboxylase alpha [ Rattus norvegicus ]2006242A740964Ac-CoA carboxylaseAAS1368542405896acetyl-CoA carboxylase 1 [ Mus musculus ]NP_59866548976025acetyl-Coenzyme A carboxylase beta [ Mus musculus ]Q130852493311Acetyl-CoA carboxylase 1 (ACC-alpha) [Includes: Biotin carboxylase]XP_54825057091783PREDICTED: similar to acetyl-CoA carboxylase [ Canis familiaris ]XP_31407158385597ENSANGP00000015662 [ Anopheles gambiae str. PEST]CAG0853647226520unnamed protein product [ Tetraodon nigroviridis ]NP_72463624586460CG11198-PB, isoform B [ Drosophila melanogaster ]NP_61034224586458CG11198-PA, isoform A [ Drosophila melanogaster ]NP_0010844501855acetyl-Coenzyme A carboxylase beta [ Homo sapiens ]NP_44637416758804acetyl-Coenzyme A carboxylase beta [ Rattus norvegicus ]EAL6321960465120acetyl-CoA carboxylase [ Dictyostelium discoideum ]NP_92103437533464putative acetyl-CoA carboxylase [ Oryza sativa ( japonica cultivar-group)]T070847438099acetyl-CoA carboxylase (EC 6.4.1.2) A - soybeanAAP7889632264940acetyl-coenzyme A carboxylase ACC1A [ Zea mays ]AAO6290329123370acetyl-coenzyme A carboxylase [ Setaria italica ]BAA070121100253acetyl-CoA carboxylase [ Arabidopsis thaliana ]AAL0205615558947acetyl-coenzyme A carboxylase [ Setaria italica ]AAG4056311869927acetyl-CoA carboxylase 1 [ Arabidopsis thaliana ]D8648325293894protein F5J5.19 [imported] - Arabidopsis thalianaT079207438090probable acetyl-CoA carboxylase (EC 6.4.1.2) - rapeA577102130099acetyl-CoA carboxylase (EC 6.4.1.2) - wheatAAO6290229123376acetyl-coenzyme A carboxylase [ Setaria italica ]2208491A1588584Ac-CoA carboxylaseT095387438102acetyl-CoA carboxylase (EC 6.4.1.2) - alfalfaCAC1987512057067acetyl-CoA carboxylase [ Brassica napus ]AAP7889732264942acetyl-coenzyme A carboxylase ACC1B [ Zea mays ]T022357438095acetyl-CoA carboxylase (EC 6.4.1.2) - maizeAAG4056411869928acetyl-CoA carboxylase 2 [ Arabidopsis thaliana ]E8648325293893probable acetyl-CoA carboxylase, 9984-22276 [mported] - ArabidopsisthalianaCAC8416120975574acetyl-coenzyme A carboxylase [ Alopecurus myosuroides ]T070817438097acetyl-CoA carboxylase (EC 6.4.1.2) B - soybean (fragment)CAC1987612057069acetyl-CoA carboxylase [ Brassica napus ] TABLE 2Examples of pyruvate decarboxylase polypeptides.ACCESSIONGIPROTEIN DESCRIPTION1QPBB7245977Chain B, Pyruvate Decarboyxlase From Yeast (Form B) ComplexedWith PyruvamideCAA54522871533pyruvate decarboxylase [ Saccharomyces cerevisiae ]1PYDB515237Chain B, Pyruvate Decarboxylase (Pdc) (E.C.4.1.1.1)CAA283804109pyruvate decarboxylase [ Saccharomyces cerevisiae ]1PVDB1127233Chain B, Pyruvate Decarboxylase (Pdc) (E.C.4.1.1.1)CAA337094114unnamed protein product [ Saccharomyces cerevisiae ]AAN7724325992752pyruvate decarboxylase [ Candida glabrata ]NP_0132356323163Minor isoform of pyruvate decarboxylase, key enzyme in alcoholicfermentation [ Saccharomyces cerevisiae ]Q6FJA357012668Pyruvate decarboxylaseS36363486942pyruvate decarboxylase (EC 4.1.1.1) - yeast ( Kluyveromyces marxianus )Q1262952788279Pyruvate decarboxylaseAAP7589837359468pyruvate decarboxylase [ Saccharomyces kluyveri ]S706842131152pyruvate decarboxylase (EC 4.1.1.1) - yeast ( Kluyveromyces marxianusvar. lactis )NP_0116016321524Minor isoform of pyruvate decarboxylase, key enzyme in alcoholicfermentation [ Saccharomyces cerevisiae ]AAQ7361834500072pyruvate decarboxylase [ Saccharomyces kluyveri ]NP_98327045185554ACL134Cp [ Eremothecium gossypii ]AAF788958745337putative pyruvate decarboxylase [ Saccharomyces kluyveri ]CAB655546689662putative pyruvate decarboxylase [ Zygosaccharomyces bisporus ]AAP7589937359470pyruvate decarboxylase [ Saccharomyces kluyveri ]NP_98246945184751AAL073Wp [ Eremothecium gossypii ]CAA970911945321PDC6 [ Saccharomyces cerevisiae ]S507001086157pyruvate decarboxylase (EC 4.1.1.1) - yeast ( Hanseniaspora uvarum )XP_44649150288125unnamed protein product [ Candida glabrata ]XP_46233850427451unnamed protein product [ Debaryomyces hansenii ]AAC0316417066784pyruvate decarboxylase 1 [ Pichia stipitis ]EAK9656946437219hypothetical protein CaO19.10395 [ Candida albicans SC5314]XP_45713150412425unnamed protein product [ Debaryomyces hansenii ]AAC031652734883pyruvate decarboxylase 2 [ Pichia stipitis ]XP_45922450421349unnamed protein product [ Debaryomyces hansenii ]CAH5649452673248pyruvate decarboxylase [ Pichia anomala ]XP_50264750550349hypothetical protein [ Yarrowia lipolytica ]NP_0102036320123Probable decarboxylase, [ Saccharomyces cerevisiae ]BAA048861786148THI3 regulatory protein [ Saccharomyces cerevisiae ]XP_44907450293325unnamed protein product [ Candida glabrata ]EAL0409846444826hypothetical protein CaO19.12078 [ Candida albicans SC5314]CAD6072727803024unnamed protein product [ Podospora anserina ]T3875925777585probable pyruvate decarboxylase (EC 4.1.1.1) - fission yeast( Schizosaccharomyces pombe )XP_33117332421459hypothetical protein [ Neurospora crassa ]NP_59408319114995pyruvate decarboxylase [ Schizosaccharomyces pombe ]XP_40160949075036hypothetical protein UM03994.1 [ Ustilago maydis 521]XP_39001046136637hypothetical protein FG09834.1 [ Gibberella zeae PH-1]XP_40902549095128DCPY_EMENI Pyruvate decarboxylase [ Aspergillus nidulans FGSCA4]NP_98435045188127ADR254Wp [ Eremothecium gossypii ]AAD161784323053pyruvate decarboxylase [ Aspergillus oryzae ]P872082501326Pyruvate decarboxylaseEAL1833150255598hypothetical protein CNBJ2540 [ Cryptococcus neoformans var.neoformans B-3501A]XP_56747558260130pyruvate decarboxylase, putative [ Cryptococcus neoformans var.neoformans JEC21]AAM7354021666011pyruvate decarboxylase PdcB [ Rhizopus oryzae ]AAM7353921666009pyruvate decarboxylase PdcA [ Rhizopus oryzae ]XP_50250850550071hypothetical protein [ Yarrowia lipolytica ]CAA931581177659SPAC3H8.01 [ Schizosaccharomyces pombe ]XP_41253349123327hypothetical protein AN8396.2 [ Aspergillus nidulans FGSC A4]P518441706333Pyruvate decarboxylaseXP_45584250311631unnamed protein product [ Kluyveromyces lactis ]CAA611553688422pyruvate decarboxylase [ Kluyveromyces lactis ]XP_44490250284947unnamed protein product [ Candida glabrata ]CAA473194118pyruvate decarboxylase [ Saccharomyces cerevisiae ] TABLE 3Examples of isocitrate dehydrogenase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONO132853023996Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)(NADP+-specific ICDH) (IDP) (CtIDP1)EAK9167646432179hypothetical protein CaO19.5211 [ Candida albicans SC5314]O132853023996Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)(NADP+-specific ICDH) (IDP) (CtIDP1)EAK9430546434909hypothetical protein CaO19.3733 [ Candida albicans SC5314]XP_45168350303483unnamed protein product [ Kluyveromyces lactis ]XP_45977250422415unnamed protein product [ Debaryomyces hansenii ]O1329427805482Isocitrate dehydrogenase [NADP] peroxisomal (Oxalosuccinatedecarboxylase) (IDH) (PS-NADP-IDH) (CtIDP2)XP_46028950423413unnamed protein product [ Debaryomyces hansenii ]XP_39052346137663hypothetical protein FG10347.1 [ Gibberella zeae PH-1]XP_36734339971905hypothetical protein MG07268.4 [ Magnaporthe grisea 70-15]XP_32317632405126hypothetical protein [ Neurospora crassa ]XP_44544750286037unnamed protein product [ Candida glabrata ]AAK7673015027826mitochondrial NADP-dependent isocitrate dehydrogenase [ Aspergillusnidulans ]NP_0102176320137Idp1p [ Saccharomyces cerevisiae ]NP_98492145190667AER061Cp [ Eremothecium gossypii ]AAK7673115027827peroxisomal NADP-dependent isocitrate dehydrogenase [ Aspergillusnidulans ]P790893023999Isocitrate dehydrogenase [NADP], mitochondrial precursor (IDH)(NADP+-specific ICDH) (IDP)NP_0132756323203Cytosolic NADP-specific isocitrate dehydrogenase [ Saccharomycescerevisiae ]XP_40713649091350IDHP_ASPNG ISOCITRATE DEHYDROGENASE [NADP],MITOCHONDRIAL PRECURSOR (IDP) [ Aspergillus nidulans FGSCA4]NP_98252045184802AAL022Wp [ Eremothecium gossypii ]XP_44695350289047unnamed protein product [ Candida glabrata ]XP_44518450285511unnamed protein product [ Candida glabrata ]XP_45563850311227unnamed protein product [ Kluyveromyces lactis ]AAA64516736722isocitrate dehydrogenaseNP_97043442525054isocitrate dehydrogenase (NADP) [ Bdellovibrio bacteriovorus HD100]AAT9317351013759YNL009W [ Saccharomyces cerevisiae ]XP_56923358264154isocitrate dehydrogenase (NADP+), putative [ Cryptococcus neoformansvar. neoformans JEC21]XP_56923458264156isocitrate dehydrogenase (NADP+), putative [ Cryptococcus neoformansvar. neoformans JEC21]XP_40372649080406hypothetical protein UM06111.1 [ Ustilago maydis 521]XP_50357150552322XP_45815150428131unnamed protein product [ Debaryomyces hansenii ]O1330213124301Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial precursor(NAD+-specific ICDH)XP_40992749096934IDH1_AJECA Isocitrate dehydrogenase [NAD] subunit 1,mitochondrial precursor[ Aspergillus nidulans FGSC A4]XP_38590946122711IDH1_AJECA Isocitrate dehydrogenase [NAD] subunit 1,mitochondrial precursor [ Gibberella zeae PH-1]XP_36529339967489hypothetical protein MG01995.4 [ Magnaporthe grisea 70-15]NP_98387345187650ADL223Wp [ Eremothecium gossypii ]XP_45526650310493IDH1_KLULA [ Kluyveromyces lactis ]NP_59439719115309putative isocitrate dehydrogenase (EC 1.1.1.41) [ Schizosaccharomycespombe ]XP_32495532408949hypothetical protein [ Neurospora crassa ]CAE8194238636405probable isocitrate dehydrogenase [NAD] subunit 1, mitochondrialprecursor [ Neurospora crassa ]NP_0143616324291Idh1p [ Saccharomyces cerevisiae ]XP_44647950288101unnamed protein product [ Candida glabrata ]XP_56737858259936isocitrate dehydrogenase (NAD+), putative [ Cryptococcus neoformansvar. neoformans JEC21]XP_39894449069310hypothetical protein UM01329.1 [ Ustilago maydis 521]XP_50247950550013hypothetical protein [ Yarrowia lipolytica ]EAK9623846436883hypothetical protein CaO19.13213 [ Candida albicans SC5314]EAK9630546436951hypothetical protein CaO19.5791 [ Candida albicans SC5314]XP_46179750426401unnamed protein product [ Debaryomyces hansenii ]XP_32840332415850hypothetical protein [ Neurospora crassa ]CAF3199742820684isocitrate dehydrogenase, putative [ Aspergillus fumigatus ]XP_38975646136129hypothetical protein FG09580.1 [ Gibberella zeae PH-1]XP_36378639952139hypothetical protein MG01712.4 [ Magnaporthe grisea 70-15]AAL7303518463935isocitrate dehydrogenase [ Coccidioides immitis ]XP_40514049086142hypothetical protein AN1003.2 [ Aspergillus nidulans FGSC A4]NP_59520319111995probable isocitrate dehydrogenase [nad] subunit 2, mitochondrialprecursor [ Schizosaccharomyces pombe ]NP_0147796324709Idh2p [ Saccharomyces cerevisiae ]XP_44756450290265unnamed protein product [ Candida glabrata ]NP_98568445198655AFR137Cp [ Eremothecium gossypii ]XP_56683758258849isocitrate dehydrogenase, putative [ Cryptococcus neoformans var.neoformans JEC21]XP_45408650308171IDH2_KLULA [ Kluyveromyces lactis ]XP_39894349069308hypothetical protein UM01328.1 [ Ustilago maydis 521] TABLE 4Examples of ATP-citrate lyase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONXP_32707132413182hypothetical protein [ Neurospora crassa ]O9398830912679ATP-citrate synthase subunit 1 (ATP-citrate (pro-S-)-lyase 1) (Citratecleavage enzyme subunit 1)XP_37022239977669hypothetical protein MG06719.4 [ Magnaporthe grisea 70-15]XP_40657349090008ACL1_NEUCR Probable ATP-citrate synthase subunit 1 [ Aspergillusnidulans FGSC A4]XP_50478750554757hypothetical protein [ Yarrowia lipolytica ]Q9P7W330912748Probable ATP-citrate synthase subunit 1 (ATP-citrate (pro-S-)-lyase 1)(Citrate cleavage enzyme subunit 1)XP_39862049068662hypothetical protein UM01005.1 [ Ustilago maydis 521]NP_59620219112994probable ATP citrate lyase [ Schizosaccharomyces pombe ]XP_56746058260100conserved hypothetical protein [ Cryptococcus neoformans var.neoformans JEC21]NP_00100856118260acly-prov protein [ Xenopus tropicalis ]XP_41815450760837PREDICTED: similar to ATP citrate lyase [ Gallus gallus ]AAH8425354038148LOC495086 protein [ Xenopus laevis ]NP_94212738569423ATP citrate lyase isoform 2 [ Homo sapiens ]NP_00108738569421ATP citrate lyase isoform 1 [ Homo sapiens ]P5339620141248ATP-citrate synthase (ATP-citrate (pro-S-)-lyase) (Citrate cleavageenzyme)AAL3431617028103ATP-citrate lyase [ Rattus norvegicus ]NP_00100250540366zgc: 92008 [ Danio rerio ]AAH8477654311201LOC495316 protein [ Xenopus laevis ]S21173105392ATP citrate (pro-S)-lyase - humanAAT9442951092031RE70805p [ Drosophila melanogaster ]AAD3475428372804LD21334p [ Drosophila melanogaster ]AAH2150218204829Acly protein [ Mus musculus ]XP_31932358392375ENSANGP00000012364 [ Anopheles gambiae str. PEST]NP_72551424653990CG8322-PB, isoform B [ Drosophila melanogaster ]EAL2660154637198GA20986-PA [ Drosophila pseudoobscura ]CAE5672539579419Hypothetical protein CBG24512 [ Caenorhabditis briggsae ]CAE6466339593194Hypothetical protein CBG09435 [ Caenorhabditis briggsae ]XP_51149555645405PREDICTED: similar to ATP citrate lyase isoform 1 [ Pan troglodytes ]CAF9582947210997unnamed protein product [ Tetraodon nigroviridis ]AAO2256527754223putative ATP citrate lyase [ Arabidopsis thaliana ]AAL3378817065616putative ATP citrate lyase [ Arabidopsis thaliana ]CAB460775304837ATP citrate lyase [ Cyanophora paradoxa ]CAF9604447204726unnamed protein product [ Tetraodon nigroviridis ]AAK1331813160653ATP:citrate lyase [ Capsicum annuum ]AAQ7515934558815citrate lyase subunit 2 [ Alvinella pompejana epibiont 7G3]AAQ7512834558783citrate lyase subunit 2 [ Alvinella pompejana epibiont 6C6]XP_53764057091075PREDICTED: similar to ATP citrate lyase isoform 2 [ Canis familiaris ]XP_32706932413178hypothetical protein ((AJ243817) ATP citrate lyase, subunit 2 [ Sordariamacrospora ]) [ Neurospora crassa ]CAB761647160184ATP citrate lyase, subunit 2 [ Sordaria macrospora ]XP_37022339977671hypothetical protein MG06720.4 [ Magnaporthe grisea 70-15]XP_38621546123323hypothetical protein FG06039.1 [ Gibberella zeae PH-1]CAA106667159697ATP-citrat-lyase [ Gibberella pulicaris ]XP_40657249090004conserved hypothetical protein [ Aspergillus nidulans FGSC A4]XP_50323150551515hypothetical protein [ Yarrowia lipolytica ]NP_59324619114158putative ATP-citrate (pro-S-) lyase (EC 4.1.3.8) [ Schizosaccharomycespombe ]XP_39862049068662hypothetical protein UM01005.1 [ Ustilago maydis 521]XP_56746058260100conserved hypothetical protein [ Cryptococcus neoformans var.neoformans JEC21]AAT9442951092031RE70805p [ Drosophila melanogaster ]NP_72551424653990CG8322-PB, isoform B [ Drosophila melanogaster ]AAD3475428372804LD21334p [ Drosophila melanogaster ]EAL2660154637198GA20986-PA [ Drosophila pseudoobscura ]XP_31932358392375ENSANGP00000012364 [ Anopheles gambiae str. PEST]AAH8477654311201LOC495316 protein [ Xenopus laevis ]BAB006249229902ATP citrate-lyase [ Ciona intestinalis ]NP_00100856118260acly-prov protein [ Xenopus tropicalis ]AAH8425354038148LOC495086 protein [ Xenopus laevis ]AAH5637838614162ATP citrate lyase [ Mus musculus ]NP_00108738569421ATP citrate lyase isoform 1 [ Homo sapiens ]NP_94212738569423ATP citrate lyase isoform 2 [ Homo sapiens ]P5339620141248ATP-citrate synthase (ATP-citrate (pro-S-)-lyase) (Citrate cleavageenzyme)XP_51149555645405PREDICTED: similar to ATP citrate lyase isoform 1 [ Pan troglodytes ]NP_0586838392839ATP citrate lyase [ Rattus norvegicus ]NP_00100250540366zgc: 92008 [ Danio rerio ]S21173105392ATP citrate (pro-S)-lyase - humanNP_50828017551266atp citrate lyase (XC101) [ Caenorhabditis elegans ]CAE6466339593194Hypothetical protein CBG09435 [ Caenorhabditis briggsae ]CAE5672539579419Hypothetical protein CBG24512 [ Caenorhabditis briggsae ]NP_50626717557344ATP citrate lyase (120.6 kD) (5N599) [ Caenorhabditis elegans ]XP_53764057091075PREDICTED: similar to ATP citrate lyase isoform 2 [ Canis familiaris ]CAF9605947204551unnamed protein product [ Tetraodon nigroviridis ]F9663325404292hypothetical protein F8A5.32 [imported]- Arabidopsis thalianaAAM9114122136126similar to ATP-citrate-lyase [ Arabidopsis thaliana ]NP_84963430681854expressed protein [ Arabidopsis thaliana ]AAO2358227764922At1g09430/F19J9_9 [ Arabidopsis thaliana ]AAM6507821593129ATP citrate-lyase, putative [ Arabidopsis thaliana ]CAC8699615919089ATP citrate lyase b-subunit [ Lupinus albus ]AAQ7515834558814citrate lyase subunit 1 [ Alvinella pompejana epibiont 7G3]AAQ7512734558782citrate lyase subunit 1 [ Alvinella pompejana epibiont 6C6] TABLE 5Examples of malic enzyme polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONNP_0128966322823Mae1p [ Saccharomyces cerevisiae ]XP_44885850292851unnamed protein product [ Candida glabrata ]XP_45479350309563unnamed protein product [ Kluyveromyces lactis ]NP_98659845201028AGL068Wp [ Eremothecium gossypii ]XP_46088750424595unnamed protein product [ Debaryomyces hansenii ]EAK9773846438407hypothetical protein CaO19.3419 [ Candida albicans SC5314]XP_50411250553402hypothetical protein [ Yarrowia lipolytica ]XP_33009432419237hypothetical protein [ Neurospora crassa ]XP_38098146107844hypothetical protein FG00805.1 [ Gibberella zeae PH-1]XP_41107049102552hypothetical protein AN6933.2 [ Aspergillus nidulans FGSC A4]XP_36287539946676hypothetical protein MG08562.4 [ Magnaporthe grisea 70-15]NP_58776019075260malate oxidoreductase [nad] [ Schizosaccharomyces pombe ]NP_97818942780942malate oxidoreductase [ Bacillus cereus ATCC 10987]YP_03598249481098NAD-dependent malic enzyme [ Bacillus thuringiensis serovarkonkukian str. 97-27]YP_02793449184682malate oxidoreductase [ Bacillus anthracis str. Sterne]YP_01843847527089malate oxidoreductase [ Bacillus anthracis str. ‘Ames Ancestor’]ZP_00236547565532malate oxidoreductase VC1188 [ Bacillus cereus G9241]YP_08320952143619NAD-dependent malic enzyme [ Bacillus cereus ZK]XP_57167258269032malate dehydrogenase, putative [ Cryptococcus neoformans var.neoformans JEC21 ]NP_39158616080758hypothetical protein BSU37050 [ Bacillus subtilis subsp. subtilis str.168]YP_09269352786864MalS [ Bacillus licheniformis ATCC 14580]NP_83151630019885NAD-dependent malic enzyme [ Bacillus cereus ATCC 14579]YP_09346052787631YwkA [ Bacillus licheniformis ATCC 14580]YP_08103052082239Malic oxidoreductase [ Bacillus licheniformis ATCC 14580]NP_82268929828055putative malate dehydrogenase [ Streptomyces avermitilis MA-4680]O3438933517449Probable NAD-dependent malic enzyme 3 (NAD-ME 3)EAL1911150256386hypothetical protein CNBH2110 [ Cryptococcus neoformans var.neoformans B-3501A]NP_82504729830413putative malate dehydrogenase [ Streptomyces avermitilis MA-4680]ZP_00234047096498NADP-dependent malic enzyme [ Listeria monocytogenes str. ½aF6854]NP_92883737525493malate dehydrogenase (oxaloacetate-decarboxylating) [ Photorhabdusluminescens subsp. laumondii TTO1]NP_23083315641201malate oxidoreductase [ Vibrio cholerae O1 biovar eltor str. N16961]NP_93425737679648malic enzyme [ Vibrio vulnificus YJ016]NP_76161327366085Malic enzyme [ Vibrio vulnificus CMCP6]AC131425283688malolactic enzyme (malate dehydrogenase) homolog lmo1915 - Listeriamonocytogenes (strain EGD-e)YP_05560250842375NAD-dependent malic enzyme [ Propionibacterium acnes KPA171202]YP_09531052841511malate oxidoreductase [ Legionella pneumophila subsp. pneumophilastr. Philadelphia 1]ZP_00231547093832NADP-dependent malic enzyme [ Listeria monocytogenes str. 4bH7858]AC168625283689malolactic enzyme (malate dehydrogenase) homolog lin2029[imported] - Listeria innocua (strain Clip11262)YP_12659454294179malate oxidoreductase [ Legionella pneumophila str. Lens]YP_12356754297198malate oxidoreductase [ Legionella pneumophila str. Paris]EAJ7626044510091unknown [environmental sequence]YP_11427353803890malate oxidoreductase [ Methylococcus capsulatus str. Bath]NP_79763728898032malate oxidoreductase [ Vibrio parahaemolyticus RIMD 2210633]YP_04025049483026putative malolactic enzyme [ Staphylococcus aureus subsp. aureusMRSA252]ZP_00127653693400COG0281: Malic enzyme [ Pseudomonas syringae pv. syringae B728a]YP_04496150083451NAD-linked malate dehydrogenase, Rossman fold [ Acinetobacter sp.ADP1]YP_12822654295811hypothetical protein lpl2901 [ Legionella pneumophila str. Lens]NP_71938724375344malate oxidoreductase [ Shewanella oneidensis MR-1]XP_57285358271394nad-dependent malic enzyme, putative [ Cryptococcus neoformans var.neoformans JEC21]NP_25216115598667probable malic enzyme [ Pseudomonas aeruginosa PAO1]ZP_00136846164263COG0281: Malic enzyme [ Pseudomonas aeruginosa UCBPP-PA14]YP_12534554298976hypothetical protein lpp3043 [ Legionella pneumophila str. Paris]NP_79369528871076malate dehydrogenase [ Pseudomonas syringae pv. tomato str. DC3000]YP_09696452843165malate dehydrogenase (NAD-linked) [ Legionella pneumophila subsp.pneumophila str. Philadelphia 1]EAH9228044245125unknown [environmental sequence]YP_15498856459707Malic enzyme [ Idiomarina loihiensis L2TR]EAI6819544354928unknown [environmental sequence]YP_07005451595863NAD-dependent malic enzyme [ Yersinia pseudotuberculosis IP 32953]YP_13302554303032putative malate oxidoreductase [ Photobacterium profundum SS9]NP_96962342524243NAD-dependent malic enzyme [ Bdellovibrio bacteriovorus HD100]NP_85600931793516PROBABLE [NAD] DEPENDENT MALATE OXIDOREDUCTASEMEZ (MALIC ENZYME) (NAD-MALIC ENZYME) (MALATEDEHYDROGENASE TATEDECARBOXYATING))PYRUVIC-MALIC CARBOXYLASE) (NAD-ME) [ Mycobacteriumbovis AF2122/97]NP_93503537680426malic enzyme [ Vibrio vulnificus YJ016]YP_05092250121755NAD-dependent malic enzyme [ Erwinia carotovora subsp. atrosepticaSCRI1043]E707057431223probable malate oxidoreductase - Mycobacterium tuberculosis (strainH37RV)NP_21684857116971PROBABLE [NAD] DEPENDENT MALATE OXIDOREDUCTASEMEZ (MALIC ENZYME) (NAD-MALIC ENZYME) (MALATEDEHYDROGENASE TATEDECARBOXYATING))PYRUVIC-MALIC CARBOXYLASE) (NAD-ME) [ Mycobacteriumtuberculosis H37Rv]YP_14378655980489NAD-dependent malic enzyme (malate dehydrogenase) [ Thermusthermophilus HB8]YP_13020254309182putative malate oxidoreductase [ Photobacterium profundum SS9]NP_41599616129438NAD-linked malate dehydrogenase [ Escherichia coli K12]NP_81984329654151malate oxidoreductase [ Coxiella burnetii RSA 493]NP_75380926247769NAD-dependent malic enzyme [ Escherichia coli CFT073]NP_70761156479957NAD-linked malate dehydrogenase (malic enzyme) [ Shigella flexneri2a str. 301]F8572825283682NAD-linked malate dehydrogenase (malic enzyme) - Escherichia coli(strain O157:H7, substrain EDL933)YP_16369056552851malic enzyme [ Zymomonas mobilis subsp. mobilis ZM4]YP_15056256413487NAD-linked malic enzyme [ Salmonella enterica subsp. enterica serovarParatypi A str. ATCC 9150]NP_72061024378655malolactic enzyme [ Streptococcus mutans UA159]NP_46052516764910NAD-linked malate dehydrogenase [ Salmonella typhimurium LT2]ZP_00319348865537COG0281: Malic enzyme [ Oenococcus oeni PSU-1]NP_78479728377905malolactic enzyme [ Lactobacillus plantarum WCFS1]T134967431227malolactic enzyme (EC 1.1.1.- ) - Leuconostoc oenosAAV6576655793550malolactic enzyme [ Oenococcus oeni ]A9709625283683malic enzyme [imported] - Clostridium acetobutylicumYP_19395158337366malolactic enzyme [ Lactobacillus acidophilus NCFM]H9709625283684malic enzyme [imported] - Clostridium acetobutylicumZP_00323748870993COG0281: Malic enzyme [ Pediococcus pentosaceus ATCC 25745]ZP_00146041689468COG0281: Malic enzyme [ Psychrobacter sp. 273-4]D8673725283676malolactic enzyme [imported] - Lactococcus lactis subsp. lactis (strainIL1403)ZP_00287048825851COG0281: Malic enzyme [ Enterococcus faecium ]ZP_00143934762975Malolactic enzyme [ Fusobacterium nucleatum subsp. vincentii ATCC49256]1922245A737262malolactic enzymeYP_16991456708018NAD-dependent malic enzyme [ Francisella tularensis subsp. tularensisSchu 4]YP_05502750841800putative malate oxidoreductase [ Propionibacterium acnes KPA171202]ZP_00062523023297COG0281: Malic enzyme [ Leuconostoc mesenteroides subsp.mesenteroides ATCC 8293]NP_29630215807565malate oxidoreductase [ Deinococcus radiodurans R1]NP_28559915807938malate oxidoreductase [ Deinococcus radiodurans R1]YP_13206954302076hypothetical malate oxidoreductase [ Photobacterium profundum SS9]CAA50716467569malolactic enzyme [ Lactococcus lactis ]ZP_00290648833596COG0281: Malic enzyme [ Magnetococcus sp. MC-1]ZP_00315548861632COG0281: Malic enzyme [ Microbulbifer degradans 2-40]NP_77310927381580malic enzyme [ Bradyrhizobium japonicum USDA 110]AAQ9565837622953malic enzyme [ Dictyostelium discoideum ]CAC1950556204311malic enzyme 1, NADP(+)-dependent, cytosolic [ Homo sapiens ]AAH8066051873855Mod1 protein [ Mus musculus ]P40927729986NADP-dependent malic enzyme (NADP-ME)AAT0253346850200NADP-dependent malic enzyme 1 [ Hydrilla verticillata ]BAC3708626346875unnamed protein product [ Mus musculus ]T027637431235probable malate dehydrogenase (oxaloacetate-decarboxylating)(NADP) (EC 1.1.1.40) - maizeXP_38736746125627hypothetical protein FG07191.1 [ Gibberella zeae PH-1]AAC506131465733cytosolic NADP(+)-dependent malic enzymeCAA39421669118sbcA8 recE fusion [ Escherichia coli ]CAA39420669117sbcA8 recE fusion [ Escherichia coli ]NP_0326416678912malic enzyme, supernatant [ Mus musculus ]CAA39419581228sbcA8 recE fusion [ Escherichia coli ]AAB013801335389NADP-dependent malic enzymeJC41601085347malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) - humanE9682825283677probable malate oxidoreductase, 93001-96525 [imported] - ArabidopsisthalianaBAD8791057899974cytosolic NADP malic enzyme [ Oryza sativa ( japonica cultivar-group)]EAJ7708344511304unknown [environmental sequence]P13697266504NADP-dependent malic enzyme (NADP-ME) (Malic enzyme 1)NP_0367327106353malic enzyme 1 [ Rattus norvegicus ]YP_06593951246055related to NAD-dependent malic enzyme [ Desulfotalea psychrophilaLSv54]CAC1816416944467related to malate dehydrogenase (oxaloacetate-decarboxylating)(NADP+) [ Neurospora crassa]XP_32295332404680hypothetical protein [ Neurospora crassa ]AAK9150218460985NADP-dependent malic enzyme [ Zea mays ]AAQ8839637147841non-photosynthetic NADP-malic enzyme [ Zea mays ]NP_00100357525624zgc: 100941 [ Danio rerio ]1GQ2P21465488Chain P, Malic Enzyme From Pigeon LiverAAO2605328195290malic enzyme [ Mucor circinelloides ]AAH8425054038006Me2 protein [ Xenopus laevis ]XP_36259039946106hypothetical protein MG08173.4 [ Magnaporthe grisea 70-15]AAH0328713096987Mod1 protein [ Mus musculus ]Q295582497785NADP-dependent malic enzyme (NADP-ME) (Malic enzyme 1)XP_53221757094622PREDICTED: similar to malate dehydrogenase decarboxylase(NADP+) [ Canis familiaris ]P28227126734NADP-dependent malic enzyme (NADP-ME)NP_49696817537199malic enzyme nadp-dependent (2O518) [ Caenorhabditis elegans ]NP_91453334906372unnamed protein product [ Oryza sativa ( japonica cultivar-group)]AAD105044096786NADP-malic enzyme [ Zea mays ]AAO6752350897495mitochondrial malic enzyme 2 [ Xenopus laevis ]P432791170871NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)AAK8307415077109putative cytosolic NADP-malic enzyme [ Flaveria pringlei ]AAP3301130575690NADP-malic enzyme [ Zea mays ]AAN8669027357017malic enzyme [ Mastigamoeba balamuthi ]P7871541017288Malic enzyme, hydrogenosomal precursor (ME)AAP3220430526303NADP-dependent malic enzyme [ Sorghum bicolor ]AAV3124954287505NADP malic enzyme [ Oryza sativa ( japonica cultivar-group)]T064027431232malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) 2, cytosolic - tomatoQ99KE155583978NAD-dependent malic enzyme, mitochondrial precursor (NAD-ME)(Malic enzyme 2)XP_39992249071266hypothetical protein UM02307.1 [ Ustilago maydis 521]P36444547886NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)AAO3003428059162malate oxidoreductase (malic enzyme) [ Arabidopsis thaliana ]AAK8307315077107putative cytosolic NADP-malic enzyme [ Flaveria pringlei ]NP_0023874505145malic enzyme 2, NAD(+)-dependent, mitochondrial [ Homo sapiens ]AAA33487168528NADP-dependent malic enzyme (EC 1.1.1.40)BAA747354239891NADP-malic enzyme [ Aloe arborescens ]NP_98963445383538malic enzyme 1, NADP(+)-dependent, cytosolic [ Gallus gallus ]1GZ3D31615316Chain D, The Regulation Of Human Mitochondrial Nad(P)+-Dependent Malic Enzyme By Atp And FumarateAAW5645057791240chloroplast NADP-dependent malic enzyme precursor [ Flaveriabidentis ]AAT0253446850202NADP-dependent malic enzyme 2 [ Hydrilla verticillata ]S29742422339malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) - pig roundworm1O0SB34811253Chain B, Crystal Structure Of Ascaris Suum Malic Enzyme ComplexedWith NadhP27443126732NAD-dependent malic enzyme, mitochondrial precursor (NAD-ME)T064017431231malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) precursor - tomatoAAL1617516226466AT5g11670/T22P22_60 [ Arabidopsis thaliana ]AAF730068118507NADP-dependent malic protein [ Ricinus communis ]AAK9753015420975malic enzyme [ Meleagris gallopavo ]EAI9034844385841unknown [environmental sequence]P516151708924NADP-DEPENDENT MALIC ENZYME (NADP-ME)AAA19575169327NADP-dependent malic enzymeS437181084300malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) - common ice plantP341051346485NADP-DEPENDENT MALIC ENZYME (NADP-ME)AAS3859742733630similar to Mastigamoeba balamuthi Malic enzyme (EC 1.1.1.38)[Dictyostelium discoideum]BAC5410127530932cytosolic NADP-malic enzyme [ Lithospermum erythrorhizon ]AAT0253546850204NADP-dependent malic enzyme 3 [ Hydrilla verticillata]CAB660036706333NADP-dependent malate dehydrogenase (decarboxylating) [ Apiumgraveolens ]AAH8486054311418LOC495390 protein [ Xenopus laevis ]CAA39422669119sbcA8 recE fusion [ Escherichia coli ]NP_91671334910732P0022F10.12 [ Oryza sativa ( japonica cultivar-group)]CAA56354510876NADP dependent malic enzyme [ Phaseolus vulgaris ]DEFBC7427668malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) - kidney beanJC59677431234malate dehydrogenase (oxaloacetate-decarboxylating) (NADP) (EC1.1.1.40) - aloeNP_19796015239517malate oxidoreductase, putative [ Arabidopsis thaliana ]NP_65195921356279CG5889-PA [ Drosophila melanogaster ]CAB642636634090malate dehydrogenase (NADP-dependent oxaloacetatedecarboxylating), malic enzyme [ Drosophila melanogaster ]BAB2088754606800NADP dependent malic enzyme [ Oryza sativa ( japonica cultivar-group)]EAL2742454638022GA19206-PA [ Drosophila pseudoobscura ]NP_0066715729920malic enzyme 3, NADP(+)-dependent, mitochondrial [ Homo sapiens ]AAB088741561774malate dehydrogenase [ Vitis vinifera ]1PJLH33358128Chain H, Crystal Structure Of Human M-Nad-Me In Ternary ComplexWith Nad And Lu3+1GZ4D22218682Chain D, The Regulation Of Human Mitochondrial Nad(P)+-Dependent Malic Enzyme By Atp And Fumarate1QR6B5822327Chain B, Human Mitochondrial Nad(P)-Dependent Malic Enzyme1PJ3D39654475Chain D, Crystal Structure Of Human Mitochondrial Nad(P)+-Dependent Malic EnzymeP22178126736NADP-dependent malic enzyme, chloroplast precursor (NADP-ME)XP_41030549097690hypothetical protein AN6168.2 [ Aspergillus nidulans FGSC A4]AAH2247218490280Malic enzyme 3, NADP(+)-dependent, mitochondrial [ Homo sapiens ] TABLE 6Examples of AMP deaminase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAA34420171053AMP deaminase (EC 3.5.4.6)XP_44668450288509unnamed protein product [ Candida glabrata ]NP_98315345185436ABR204Cp [ Eremothecium gossypii ]XP_45333750306727unnamed protein product [ Kluyveromyces lactis ]EAL0232246443037adenosine/AMP deaminase [ Candida albicans SC5314 ]XP_46021150423261unnamed protein product [ Debaryomyces hansenii ]XP_50382250552824hypothetical protein [ Yarrowia lipolytica ]XP_41300949131023hypothetical protein AN8872.2 [ Aspergillus nidulans FGSC A4]XP_36025639941438hypothetical protein MG05630.4 [ Magnaporthe grisea 70-15]XP_38154746108978hypothetical protein FG01371.1 [ Gibberella zeae PH-1]XP_33016732419447probable AMP deaminase [MIPS] [ Neurospora crassa ]CAB9731616945394probable AMP deaminase [ Neurospora crassa ]T5099611359582probable AMP deaminase [imported] - Neurospora crassaNP_59515319111945amp deaminase [ Schizosaccharomyces pombe ]EAL2222650259553hypothetical protein CNBC3640 [ Cryptococcus neoformans var.neoformans B-3501A]XP_40223749076548hypothetical protein UM04622.1 [ Ustilago maydis 521]CAA62797995562AMP deaminase [ Schizosaccharomyces pombe ]AAF654077638159AMP deaminase [ Dictyostelium discoideum ]XP_53703957088163PREDICTED: similar to AMP deaminase 2 (AMP deaminase isoformL) [ Canis familiaris ]AAH4911929145073Adenosine monophosphate deaminase 2 (isoform L) [ Mus musculus ]XP_56969158265070AMP deaminase, putative [ Cryptococcus neoformans var. neoformansJEC21]AAD563035922018AMP deaminase isoform L [ Homo sapiens ]NP_00402821264318adenosine monophosphate deaminase 2 (isoform L) isoform 1 [ Homosapiens ]A44313345738AMP deaminase (EC 3.5.4.6) isoform L - humanCAI1930756206061adenosine monophosphate deaminase 2 (isoform L) [ Homo sapiens ]AAA62126644509AMP deaminase isoform L splicing variantCAI1930556206059adenosine monophosphate deaminase 2 (isoform L) [ Homo sapiens ]XP_31049758424203ENSANGP00000017310 [ Anopheles gambiae str. PEST]CAI1930656206060adenosine monophosphate deaminase 2 (isoform L) [ Homo sapiens ]AAC50308608499AMP deaminaseCAG0682547229629unnamed protein product [ Tetraodon nigroviridis ]NP_72774145551453CG32626-PD, isoform D [ Drosophila melanogaster ]NP_72773945551452CG32626-PA, isoform A [ Drosophila melanogaster ]NP_72774024641890CG32626-PB, isoform B [ Drosophila melanogaster ]AAN0933722832227CG32626-PC, isoform C [ Drosophila melanogaster ]T012597484807AMP deaminase homolog F16M14.21 - Arabidopsis thalianaXP_50659151963676PREDICTED P0034A04.129 gene product [ Oryza sativa ( japonicacultivar-group)]NP_85029430687456AMP deaminase, putative/myoadenylate deaminase, putative[ Arabidopsis thaliana ]CAG0750947228777unnamed protein product [ Tetraodon nigroviridis ]NP_49497432564190Adenosine/AMP deaminase (85.4 kD) (2F499) [ Caenorhabditis elegans ]T157717497030hypothetical protein C34F11.3 - Caenorhabditis elegansCAE5906439596837Hypothetical protein CBG02349 [ Caenorhabditis briggsae ]NP_49497332564194Adenosine/AMP deaminase family member (2F499) [ Caenorhabditiselegans ]BAA065051321635erythrocyte-type AMP deaminase [ Homo sapiens ]NP_0004714502079adenosine monophosphate deaminase (isoform E) [ Homo sapiens ]S681472134756AMP deaminase (EC 3.5.4.6), erythrocte, splice form 1c - humanAAH5638038614134Ampd3 protein [ Mus musculus ]O087392494043AMP DEAMINASE 3 (AMP DEAMINASE ISOFORM E) (AMPDEAMINASE H-TYPE) (HEART-TYPE AMPD)NP_11373213928736adenosine monophosphate deaminase 3 [ Rattus norvegicus ]O091782494044AMP deaminase 3 (AMP deaminase isoform E)XP_42097350747746PREDICTED: similar to AMP deaminase 3 (Erythrocyte AMPdeaminase) [ Gallus gallus ]NP_95614241054127AMP deaminase 3 [ Danio rerio ]CAG0170947222742unnamed protein product [ Tetraodon nigroviridis ]NP_95718741053780hypothetical protein MGC77905 [ Danio rerio ]XP_39295748104570similar to ENSANGP00000017310 [ Apis mellifera ]AAH0718313938134Ampd3 protein [ Mus musculus ]CAG0560547220579unnamed protein product [ Tetraodon nigroviridis ]NP_62023120302047adenosine monophosphate deaminase 1 (isoform M) [ Rattus norvegicus ]XP_54024757098851PREDICTED: similar to AMP deaminase 1 (AMP deaminase isoformM) [ Canis familiaris ]CAF9963847230445unnamed protein product [ Tetraodon nigroviridis ]XP_51367155587796PREDICTED: adenosine monophosphate deaminase 1 (isoform M) [ Pantroglodytes ]CAI1882856203368adenosine monophosphate deaminase 1 (isoform M) [ Homo sapiens ]CAI1882956203369OTTHUMP00000059283 [ Homo sapiens ]CAI1883056203370adenosine monophosphate deaminase 1 (isoform M) [ Homo sapiens ]EAA1993123484684AMP deaminase homolog [ Plasmodium yoelii yoelii ]CAH9970656500932AMP deaminase, putative [ Plasmodium berghei ]XP_13110338076931similar to AMP deaminase 1 (Myoadenylate deaminase) (AMPdeaminase isoform M) [ Mus musculus ]CAH7738756523366AMP deaminase, putative [ Plasmodium chabaudi ] TABLE 7Examples of acetoacetyl-CoA thiolase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONP10551135758Acetyl-CoA acetyltransferase (Acetoacetyl-CoA thiolase)Q04677418002Acetyl-CoA acetyltransferase IB (Peroxisomal acetoacetyl-CoAthiolase) (Thiolase IB)Q1259834925109Acetyl-CoA acetyltransferase IA (Peroxisomal acetoacetyl-CoAthiolase) (Thiolase IA)T102477433657acetyl-CoA C-acetyltransferase (EC 2.3.1.9), cytosolic - radishT4274111257345probable acetyl-CoA C-acetyltransferase (EC 2.3.1.9) - fission yeast( Schizosaccharomyces pombe )AAL1892416417944acetyl Co-A acetyltransferase [ Hevea brasiliensis ]AAM6705821618008acetoacyl-CoA-thiolase [ Arabidopsis thaliana ]AAO5160528829030similar to acetyl-coa acetyltransferase (EC 2.3.1.9)[ Schizosaccharomyces pombe ]AAU9561853854350cytosolic acetoacetyl-coenzyme A thiolase [ Nicotiana tabacum ]AAU9561953854352peroxisomal acetoacetyl-coenzyme A thiolase [ Nicotiana tabacum ]BAA970038777413acetyl-CoA C-acetyltransferase [ Arabidopsis thaliana ]CAE7642938567134probable acetoacetyl-CoA thiolase [ Neurospora crassa ]EAK9085246431255hypothetical protein CaO19.1591 [ Candida albicans SC5314]EAL3226454643520GA10651-PA [ Drosophila pseudoobscura ]NP_0152976325229Acetyl-CoA C-acetyltransferase (acetoacetyl-CoA thiolase)[ Saccharomyces cerevisiae ]NP_56869430695411acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,putative [ Arabidopsis thaliana ]NP_57241424640423CG10932-PA [ Drosophila melanogaster ]NP_59668619113478acetyl-coa acetyltransferase (EC 2.3.1.9) [ Schizosaccharomyces pombe ]NP_85115430695409acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,putative [ Arabidopsis thaliana ]NP_90841134894172putative acetoacetyl-coenzyme A thiolase [ Oryza sativa ( japonicacultivar-group)]NP_97490042573608acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,putative [ Arabidopsis thaliana ]NP_97490142573610acetyl-CoA C-acyltransferase, putative/3-ketoacyl-CoA thiolase,putative [ Arabidopsis thaliana ]NP_98426245188039ADR165Cp [ Eremothecium gossypii ]XP_38949746134945hypothetical protein FG09321.1 [ Gibberella zeae PH-1]XP_40118649074048hypothetical protein UM03571.1 [ Ustilago maydis 521]XP_40554649087148hypothetical protein AN1409.2 [ Aspergillus nidulans FGSC A4]XP_44930650293789unnamed protein product [ Candida glabrata ]XP_44930650293789unnamed protein product [ Candida glabrata ]XP_45029850899020putative acetyl-CoA C-acyltransferase [ Oryza sativa ( japonica cultivar-group)]XP_45359950307241unnamed protein product [ Kluyveromyces lactis ]XP_46074150424309unnamed protein product [ Debaryomyces hansenii ]XP_50064650546253hypothetical protein [ Yarrowia lipolytica ] TABLE 8Examples of HMG-CoA synthase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONB557291083370hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5), mitochondrial -mouseP548691708235Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor (HMG-CoA synthase)S1388786312hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5) - chickenS27197284048hydroxymethylglutaryl-CoA synthase (EC 4.1.3.5), cytosolic, fibroblastisoform - humanAAA370763870723-hydroxy-3-methylglutaryl coenzyme A synthase (HMG CoA)AAF8958096219053-hydroxy-3-methylglutaryl coenzyme A synthase [ Dendroctonusjeffreyi ]AAH0029733991031HMGCS1 protein [ Homo sapiens ]AAH31363216186333-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [ Mus musculus ]AAH4292927552834Hmgcs1-prov protein [ Xenopus laevis ]AAH7969450925193MGC80816 protein [ Xenopus laevis ]AAH83543540354693-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [ Rattusnorvegicus ]AAO5256928830079similar to Homo sapiens (Human). Hypothetical protein FLJ40785[ Dictyostelium discoideum ]AAP35966305834433-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) [ Homosapiens ]BAB2365712836439unnamed protein product [ Mus musculus ]BAC0455921754758unnamed protein product [ Homo sapiens ]BAC0523321758044unnamed protein product [ Mus musculus ]CAA520321772495hydroxymethylglutaryl-CoA synthase [ Blattella germanica ]CAC1855311602786putative 3-hydroxy-3-methylglutaryl coenzyme A synthase[ Phycomyces blakesleeanus ]CAG3313148145817HMGCS2 [ Homo sapiens ]CAH9211155730782hypothetical protein [ Pongo pygmaeus ]CAI22408562050973-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 (mitochondrial)[ Homo sapiens ]EAK9745146438115hypothetical protein CaO19.7312 [ Candida albicans SC5314]EAL2503454635631GA18098-PA [ Drosophila pseudoobscura ]NP_002121540207203-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) [ Homosapiens ]NP_01358063235093-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase[ Saccharomyces cerevisiae ]NP_032282315606893-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [ Mus musculus ]NP_05896483935383-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [ Rattusnorvegicus ]NP_59385919114771hydroxymethylglutaryl-coa synthase (EC 4.1.3.5) [ Schizosaccharomycespombe ]NP_666054319818423-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [ Mus musculus ]NP_72557024654139CG4311-PE, isoform E [ Drosophila melanogaster ]NP_775117274655213-hydroxy-3-methylglutaryl-Coenzyme A synthase 2 [ Rattusnorvegicus ]NP_95737941055180similar to 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 [ Daniorerio]NP_98373945187516ADL356Cp [ Eremothecium gossypii ]NP_990742453822793-hydroxy-3-methylglutaryl-CoA synthase [ Gallus gallus ]NP_99954547523816hydroxymethylglutaryl-CoA synthase [ Sus scrofa ]XP_31587258387870ENSANGP00000017491 [ Anopheles gambiae str. PEST]XP_32324132405256probable hydroxymethylglutaryl-CoA synthase [MIPS] [ Neurosporacrassa ]XP_36821839973655hypothetical protein MG01026.4 [ Magnaporthe grisea 70-15]XP_38944246134253conserved hypothetical protein [ Gibberella zeae PH-1]XP_39720248141273similar to CG4311-PA [ Apis mellifera ]XP_40297749078452hypothetical protein UM05362.1 [ Ustilago maydis 521]XP_40906049095198hypothetical protein AN4923.2 [ Aspergillus nidulans FGSC A4]XP_44697250289085unnamed protein product [ Candida glabrata ]XP_45352950307101unnamed protein product [ Kluyveromyces lactis ]XP_45647050405663unnamed protein product [ Debaryomyces hansenii ]XP_50605250557288hypothetical protein [ Yarrowia lipolytica ]XP_51369355587844PREDICTED: 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 2(mitochondrial) [ Pan troglodytes ]XP_53648357085299PREDICTED: similar to HMGCS1 protein [ Canis familiaris ]XP_56980558265298hydroxymethylglutaryl-CoA synthase, putative [ CryptococcusXP_57193058269548conserved hypothetical protein [ Cryptococcus neoformans var.neoformans JEC21] TABLE 9Examples of HMG-CoA reductase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONA2358690238hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) - golden hamsterO74164111328503-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)P5163917082523-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)P5496017082513-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)Q12649182762683-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)Q2951224952623-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)Q9Y7D2111332113-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoAreductase)S30338422383hydroxymethylglutaryl-CoA reductase (NADPH2) (EC 1.1.1.34) -German cockroachS721947450066hydroxymethylglutaryl-CoA reductase (EC 1.1.1.88) - fission yeast( Schizosaccharomyces pombe )AAA369893870523-hydroxy-3-methylglutaryl coenzyme A [ Mesocricetus auratus ]AAA370773053553-hydroxy-3-methylglutaral coenzyme A reductase (EC 1.1.1.34)AAA497402142373-hydroxy-3-methylglutaryl-coenzyme A reductaseAAD2097598174583-hydroxy-3-methylglutaryl coenzyme A reductase [ Ips paraconfusus ]AAH7419749257596Unknown (protein for MGC: 82101) [ Xenopus laevis ]AAL09351158244533-hydroxy-3-methylglutaryl coenzyme A reductase [ Ips pini ]AAO8543429468180HMG-CoA reductase [ Aspergillus nidulans ]AAP72015321656223-hydroxy-3-methylglutaryl-Coenzyme A reductase [ Homo sapiens ]AAR0286245272118HMG-CoA reductase [ Dicentrarchus labrax ]AAT9281951013051YLR450W [ Saccharomyces cerevisiae ]BAC2056723574646HMG-CoA reductase [ Penicillium citrinum ]CAA639704376229HMG-CoA-reductase; hydroxymethylglutaryl-CoA reductase (NADPH)[ Gibberella fujikuroi ]CAE47850415812013-hydroxy-3-methylglutaryl-coenzyme a reductase, putative [ Aspergillusfumigatus ]CAF9213547213283unnamed protein product [ Tetraodon nigroviridis ]CAH9257755731745hypothetical protein [ Pongo pygmaeus ]EAK9457746435190hypothetical protein CaO19.8633 [ Candida albicans SC5314]EAL2019550257490hypothetical protein CNBF0070 [ Cryptococcus neoformans var.neoformans B-3501A]AAF803748886086HMG-CoA reductase [ Dendroctonus jeffreyi ]NP_0135556323483Hmg2p [ Saccharomyces cerevisiae ]NP_0136366323565Hmg1p [ Saccharomyces cerevisiae ]NP_032281561190963-hydroxy-3-methylglutaryl-Coenzyme A reductase [ Mus musculus ]NP_037266405388523-hydroxy-3-methylglutaryl-Coenzyme A reductase [ Rattus norvegicus ]NP_588235190757353-hydroxy-3-methylglutaryl-coenzyme a reductase[ Schizosaccharomyces pombe ]NP_98501045190756AER152Wp [ Eremothecium gossypii ]NP_989816453831933-hydroxy-3-methylglutaryl-CoA reductase [ Gallus gallus ]NP_99972447551099HMGCoA reductase [ Strongylocentrotus purpuratus ]XP_32489232408825hypothetical protein [ Neurospora crassa ]XP_36413039955070hypothetical protein MG08975.4 [ Magnaporthe grisea 70-15]XP_38937346134115hypothetical protein FG09197.1 [ Gibberella zeae PH-1]XP_40062949072680hypothetical protein UM03014.1 [ Ustilago maydis 521]XP_40573049087632hypothetical protein AN1593.2 [ Aspergillus nidulans FGSC A4]XP_40795449092986hypothetical protein AN3817.2 [ Aspergillus nidulans FGSC A4]XP_44926850293713unnamed protein product [ Candida glabrata ]XP_45174050303597unnamed protein product [ Kluyveromyces lactis ]XP_45887250420671unnamed protein product [ Debaryomyces hansenii ]XP_50355850552167hypothetical protein [ Yarrowia lipolytic a]XP_53632357084803PREDICTED: similar to 3-hydroxy-3-methylglutaryl-coenzyme Areductase (HMG-CoA reductase) [ Canis s]XP_57145058268588hydroxymethylglutaryl-CoA reductase (NADPH), putative[ Cryptococcus neoformans var. neoformans JEC21] TABLE 10Examples of mevalonate kinase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONXP_38608846123069hypothetical protein FG05912.1 [ Gibberella zeae PH-1]XP_40800649093090hypothetical protein AN3869.2 [ Aspergillus nidulans FGSC A4]XP_37044939978123hypothetical protein MG06946.4 [ Magnaporthe grisea 70-15]EAL0479746445529hypothetical protein CaO19.4809 [ Candida albicans SC5314]XP_32293532404644hypothetical protein ((AL513444) related to MEVALONATEKINASE [ Neurospora crassa ])NP_00100755925207zgc: 103473 [ Danio rerio ]XP_46085150424525unnamed protein product [ Debaryomyces hansenii ]XP_56785158260882cystathionine beta-lyase, putative [ Cryptococcus neoformans var.neoformans JEC21]XP_56785058260880cystathionine beta-lyase, putative [ Cryptococcus neoformans var.neoformans JEC21]AAQ0241633303805mevalonate kinase [synthetic construct]CAA53059450346unnamed protein product [Hepatitis B virus]AAH1614016359371MVK protein [ Homo sapiens ]AAH0560613542811Mevalonate kinase [ Mus musculus ]XP_40311149078786hypothetical protein UM05496.1 [ Ustilago maydis 521]XP_45253250305147unnamed protein product [ Kluyveromyces lactis ]CAG0852747226511unnamed protein product [ Tetraodon nigroviridis ]XP_44613850287417unnamed protein product [ Candida glabrata ]AAO5152228828936similar to Rattus norvegicus (Rat). Mevalonate kinase (EC 2.7.1.36)(MK) [ Dictyostelium discoideum ]NP_98519145190937AER335Wp [ Eremothecium gossypii ]XP_50095650546973hypothetical protein [ Yarrowia lipolytica ]NP_0139356323864Erg12p [ Saccharomyces cerevisiae ]AAD454215578718mevalonate kinase [ Arabidopsis thaliana ]NP_92072337532842putative mevalonate kinase [ Oryza sativa ( japonica cultivar-group)]NP_85108430690651mevalonate kinase (MK) [ Arabidopsis thaliana ]AAL1892516417946mevalonate kinase [ Hevea brasiliensis ]NP_78833828573850CG33009-PA, isoform A [ Drosophila melanogaster ]AAU2083451988124Hypothetical protein Y42G9A.4b [ Caenorhabditis elegans ]AAU8781352839819Hypothetical protein Y42G9A.4d [ Caenorhabditis elegans ]AAU2083551988125Hypothetical protein Y42G9A.4c [ Caenorhabditis elegans ]YP_18388757641409mevalonate kinase [ Thermococcus kodakaraensis KOD1]NP_14347814591399mevalonate kinase [ Pyrococcus horikoshii OT3]BAA244092804172mevalonate kinase [ Saccharomyces cerevisiae ]NP_12623214520757mevalonate kinase [ Pyrococcus abyssi GE5]XP_52257455639331PREDICTED: similar to Mevalonate kinase (MK) [ Pan troglodytes ]NP_07111411499870mevalonate kinase (mvk) [ Archaeoglobus fulgidus DSM 4304]XP_42394950797461PREDICTED: similar to mevalonate kinase [ Gallus gallus ]NP_63378621227864Mevalonate kinase [ Methanosarcina mazei Go1]ZP_00297148840229COG1577: Mevalonate kinase [ Methanosarcina barkeri str. fusaro ]EAH5078744170778unknown [environmental sequence]NP_61556620089491mevalonate kinase [ Methanosarcina acetivorans C2A]1VISA40890012Chain A, Crystal Structure Of Mevalonate KinaseEAK0355944549994unknown [environmental sequence]NP_24808015669275mevalonate kinase [ Methanocaldococcus jannaschii DSM 2661]1KKHA20150886Chain A, Crystal Structure Of The Methanococcus JannaschiiMevalonate KinaseQ505592497518Mevalonate kinase (MK)CAF8812347200914unnamed protein product [ Tetraodon nigroviridis ]NP_27518915678075mevalonate kinase [ Methanothermobacter thermautotrophicus str. DeltaH]EAI8874544383877unknown [environmental sequence]ZP_00204046141948COG1577: Mevalonate kinase [ Methanococcoides burtonii DSM 6242]XP_54343557105916PREDICTED: similar to Mevalonate kinase (MK) [ Canis familiaris ]EAI3892044313360unknown [environmental sequence]NP_14861114602065mevalonate kinase [ Aeropyrum pernix K1]EAD0895343286228unknown [environmental sequence]EAD4569743361720unknown [environmental sequence]YP_13486255377012mevalonate kinase [ Haloarcula marismortui ATCC 43049]NP_72065024378695putative mevalonate kinase [ Streptococcus mutans UA159]NP_61427620094429Mevalonate kinase [ Methanopyrus kandleri AV19]E8427025409931mevalonate kinase [imported] - Halobacterium sp. NRC-1NP_69114623097680mevalonate kinase [ Oceanobacillus iheyensis HTE831]ZP_00323348870579COG1577: Mevalonate kinase [ Pediococcus pentosaceus ATCC 25745]AAG024409937386mevalonate kinase [ Enterococcus faecalis ]EAD1227843292898unknown [environmental sequence]NP_49832817555862mevalonate kinase (64.1 kD) (3H214) [ Caenorhabditis elegans ]EAB3148342928976unknown [environmental sequence]ZP_00331950590618COG1577: Mevalonate kinase [ Streptococcus suis 89/1591]NP_81464229375488mevalonate kinase [ Enterococcus faecalis V583]AC143425514495mevalonate kinase homolog lin0010 [imported] - Listeria innocua(strain Clip11262)ZP_00357753796847COG1577: Mevalonate kinase [ Chloroflexus aurantiacus ]EAD8204843454743unknown [environmental sequence]CAE7361839586491Hypothetical protein CBG21109 [ Caenorhabditis briggsae ]YP_01262446906235mevalonate kinase [ Listeria monocytogenes str. 4b F2365]NP_98845545358898Mevalonate kinase [ Methanococcus maripaludis S2]ZP_00234847097293mevalonate kinase [ Listeria monocytogenes str. ½a F6854]ZP_00286248824993COG1577: Mevalonate kinase [ Enterococcus faecium ]ZP_00230747093020mevalonate kinase [ Listeria monocytogenes str. 4b H7858]NP_59710219173299MEVALONATE KINASE [ Encephalitozoon cuniculi ]CAD2442220429111phosphomevalonate kinase [ Paracoccus zeaxanthinifaciens ]NP_78530828378416mevalonate kinase [ Lactobacillus plantarum WCFS1]EAA3909829247539GLP_305_18405_19430 [ Giardia lamblia ATCC 50803]NP_81963829653946phosphomevalonate kinase, putative [ Coxiella burnetii RSA 493]EAH4974644168765unknown [environmental sequence]EAH4974544168764unknown [environmental sequence]NP_37818215922513hypothetical protein ST2185 [ Sulfolobus tokodaii str. 7]ZP_00045923002259COG1577: Mevalonate kinase [ Lactobacillus gasseri ]H9018125393827mevalonate kinase [imported] - Sulfolobus solfataricusYP_05412050405028Mevalonate kinase, putative [ Paramecium tetraurelia ]BAB077909695270mevalonate kinase [ Streptomyces sp. CL190]AAG024359937379mevalonate kinase [ Staphylococcus epidermidis ]NP_56049518313828mevalonate kinase [ Pyrobaculum aerophilum str. IM2]YP_18783457866187mevalonate kinase [ Staphylococcus epidermidis RP62A]EAK4078244602942unknown [environmental sequence]CAC5137015212070mevalonate kinase [ Lactobacillus helveticus ]AAG024249937364mevalonate kinase [ Staphylococcus aureus ]YP_18552157651465mevalonate kinase [ Staphylococcus aureus subsp. aureus COL]YP_04004449482820mevalonate kinase [ Staphylococcus aureus subsp. aureus MRSA252]YP_19403758337452mevalonate kinase [ Lactobacillus acidophilus NCFM]D8667525400965mevalonate kinase [imported] - Lactococcus lactis subsp. lactis (strainIL1403)NP_76391627467279mevalonate kinase [ Staphylococcus epidermidis ATCC 12228]CAF8943447197810unnamed protein product [ Tetraodon nigroviridis ]EAF3833343767792unknown [environmental sequence]EAK4684144611394unknown [environmental sequence]H8982725507776mevalonate kinase [imported] - Staphylococcus aureus (strain N315)ZP_00314948861061COG0153: Galactokinase [ Microbulbifer degradans 2-40]EAK1782444570143unknown [environmental sequence]EAH8627644235719unknown [environmental sequence]YP_11841854024176putative mevalonate kinase [ Nocardia farcinica IFM 10152]ZP_00319648865749COG1577: Mevalonate kinase [ Oenococcus oeni PSU-1]AAG024309937372mevalonate kinase [ Staphylococcus haemolyticus ]NP_26907515674901mevalonate kinase [ Streptococcus pyogenes M1 GAS]NP_80252028896170putative mevalonate kinase [ Streptococcus pyogenes SSI-1]AAL9757919748102mevalonate kinase [ Streptococcus pyogenes MGAS8232]ZP_00366656808907COG1577: Mevalonate kinase [ Streptococcus pyogenes M49 591]NP_96506042519130mevalonate kinase [ Lactobacillus johnsonii NCC 533]NP_81963929653947mevalonate kinase, putative [ Coxiella burnetii RSA 493]EAD9702443484567unknown [environmental sequence]BAD8680057753870mevalonate kinase [ Streptomyces sp. KO-3988] TABLE 11Examples of phosphomevalonate kinase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAA34596171479phosphomevalonate kinaseXP_45251450305111unnamed protein product [ Kluyveromyces lactis ]NP_98521045190956AER354Wp [ Eremothecium gossypii ]XP_44614450287429unnamed protein product [ Candida glabrata ]XP_46234050427455unnamed protein product [ Debaryomyces hansenii ]EAL0409646444824hypothetical protein CaO19.12076 [ Candida albicans SC5314]EAL0394146444668hypothetical protein CaO19.4606 [ Candida albicans SC5314]XP_50361950552418hypothetical protein [ Yarrowia lipolytica ]XP_38994046136497hypothetical protein FG09764.1 [ Gibberella zeae PH-1]XP_32979532418634hypothetical protein [ Neurospora crassa ]XP_36965239976529hypothetical protein MG05812.4 [ Magnaporthe grisea 70-15]XP_40644849089559hypothetical protein AN2311.2 [ Aspergillus nidulans FGSC A4]NP_59342119114333putative phosphomevalonate kinase [ Schizosaccharomyces pombe ]XP_56838558261950expressed protein [ Cryptococcus neoformans var. neoformans JEC21]EAL1762850254887hypothetical protein CNBM0120 [ Cryptococcus neoformans var.neoformans B-3501A]AAL1892616417948phosphomevalonate kinase [ Hevea brasiliensis ]BAD4327451969164hypothetical protein [ Arabidopsis thaliana ]BAD4465251971975hypothetical protein [ Arabidopsis thaliana ]XP_39837549068172hypothetical protein UM00760.1 [ Ustilago maydis 521]BAD4448651971643hypothetical protein [ Arabidopsis thaliana ]F9047925393214(Phospho) mevalonate kinase, probable [imported] - SulfolobussolfataricusYP_19403958337454phosphomevalonate kinase [ Lactobacillus acidophilus NCFM] TABLE 12Examples of mevalonate pyrophosphate decarboxylase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAT9317151013755YNR043W [ Saccharomyces cerevisiae ]1FI4A13786942Chain A, The X-Ray Crystal Structure Of Mevalonate 5-DiphosphateDecarboxylase At 2.3 Angstrom Resolution.XP_45554850311049unnamed protein product [ Kluyveromyces lactis ]XP_44533550285813unnamed protein product [ Candida glabrata ]XP_45691250409853unnamed protein product [ Debaryomyces hansenii ]NP_98643545200865AGL232Cp [ Eremothecium gossypii ]AAF193996625790diphosphomevalonate decarboxylase MVD1 [ Candida albicans ]XP_32884532416734hypothetical protein [ Neurospora crassa ]XP_50504150555265hypothetical protein [ Yarrowia lipolytica ]NP_59402719114939diphosphomevalonate decarboxylase [ Schizosaccharomyces pombe ]XP_36490539963452hypothetical protein MG09750.4 [ Magnaporthe grisea 70-15]XP_39060046137817hypothetical protein FG10424.1 [ Gibberella zeae PH-1]XP_40855149094180hypothetical protein AN4414.2 [ Aspergillus nidulans FGSC A4]AAA345067544604ORF [ Saccharomyces cerevisiae ]EAL1892750256200hypothetical protein CNBI1880 [ Cryptococcus neoformans var.neoformans B-3501A]XP_56824758261674diphosphomevalonate decarboxylase, putative [ Cryptococcusneoformans var. neoformans JEC21]XP_40279449077992hypothetical protein UM05179.1 [ Ustilago maydis 521]AAH8178451980639Mevalonate (diphospho) decarboxylase [ Rattus norvegicus ]EAL0016646440864hypothetical protein CaO19.6105 [ Candida albicans SC5314]NP_61959720149736mevalonate (diphospho) decarboxylase [ Mus musculus ]NP_11232413592005mevalonate (diphospho) decarboxylase [ Rattus norvegicus ]BAC4085226354448unnamed protein product [ Mus musculus ]XP_54678357087071Mevalonate pyrophosphate decarboxylase [ Canis familiaris ]Q99JF523814095Diphosphomevalonate decarboxylase (Mevalonate pyrophosphatedecarboxylase)AAH6390739645379LOC394871 protein [ Xenopus tropicalis ]CAF9953447230341unnamed protein product [ Tetraodon nigroviridis ]AAP3557630582699mevalonate (diphospho) decarboxylase [ Homo sapiens ]AAP3630130584105Homo sapiens mevalonate (diphospho) decarboxylase [syntheticconstruct]AAL1892716417950mevalonate disphosphate decarboxylase [ Hevea brasiliensis ]AAV3243354292590mevalonate disphosphate decarboxylase [ Ginkgo biloba ]AAP6820831711704At2g38700 [ Arabidopsis thaliana ]AAM6498821593039mevalonate diphosphate decarboxylase [ Arabidopsis thaliana ]NP_56699518410026mevalonate diphosphate decarboxylase, putative [ Arabidopsis thaliana ]XP_42313050771155PREDICTED: similar to mevalonate pyrophosphate decarboxylase[ Gallus gallus ]AAM6519221593243diphosphomevalonate decarboxylase-like protein [ Arabidopsis thaliana ]NP_00100755925435zgc: 100824 [ Danio rerio ]NP_57306828571205CG8239-PA [ Drosophila melanogaster ]BAD2794250252009putative mevalonate disphosphate decarboxylase [ Oryza sativa ( japonicacultivar-group) ]T4758411281655diphosphomevalonate decarboxylase (EC 4.1.1.33) F24B22.210[similarity] - Arabidopsis thalianaXP_30737331196851ENSANGP00000013738 [ Anopheles gambiae str. PEST]CAE7324539591192Hypothetical protein CBG20661 [ Caenorhabditis briggsae ]NP_49696617537201mevalonate decarboxylase (41.5 kD) (2O512) [ Caenorhabditis elegans ]XP_39323048121058similar to mevalonate pyrophosphate decarboxylase [ Apis mellifera ]G9047925393662diphosphomevalonate decarboxylase, probable [imported] - SulfolobussolfataricusNP_49696717537203mevalonate decarboxylase (2O512) [ Caenorhabditis elegans ]NP_69114723097681mevalonate diphosphate decarboxylase [ Oceanobacillus iheyensisHTE831]EAL2928254640164GA20922-PA [ Drosophila pseudoobscura ]AD143425515042mevalonate diphosphate decarboxylase homolog lin0011 [imported] -Listeria innocua (strain Clip11262)ZP_00230847093021diphosphomevalonate decarboxylase [ Listeria monocytogenes str. 4bH7858]YP_01262546906236diphosphomevalonate decarboxylase [ Listeria monocytogenes str. 4bF2365]ZP_00234847097294diphosphomevalonate decarboxylase [ Listeria monocytogenes str. ½aF6854]NP_81963729653945diphosphomevalonate decarboxylase [ Coxiella burnetii RSA 493]NP_37688815921219hypothetical diphosphomevalonate decarboxylase [ Sulfolobus tokodaiistr. 7]ZP_00331950590617COG3407: Mevalonate pyrophosphate decarboxylase [ Streptococcussuis 89/1591]NP_58580519074299MEVALONATE PYROPHOSPHATE DECARBOXYLASE[ Encephalitozoon cuniculi ]YP_18783557866188mevalonate diphosphate decarboxylase [ Staphylococcus epidermidisRP62A]CAD2442320429112mevalonate diphosphate decarboxylase [ Paracoccus zeaxanthinifaciens ]AAG024319937373mevalonate diphosphate decarboxylase [ Staphylococcus haemolyticus ]NP_76391727467280mevalonate diphosphate decarboxylase [ Staphylococcus epidermidisATCC 12228]AAG024469937394mevalonate diphosphate decarboxylase [ Enterococcus faecium ]ZP_00286348824994COG3407: Mevalonate pyrophosphate decarboxylase [ Enterococcusfaecium ]AAG024419937387mevalonate diphosphate decarboxylase [ Enterococcus faecalis ]YP_18552257651466mevalonate diphosphate decarboxylase [ Staphylococcus aureus subsp.aureus COL]A8982825505863mevalonate diphosphate decarboxylase [imported] - Staphylococcusaureus (strain N315)NP_81464129375487mevalonate diphosphate decarboxylase [ Enterococcus faecalis V583]YP_04004549482821mevalonate diphosphate decarboxylase [ Staphylococcus aureus subsp.aureus MRSA252]NP_78530728378415diphosphomevalonate decarboxylase [ Lactobacillus plantarum WCFS1]ZP_00319648865750COG3407: Mevalonate pyrophosphate decarboxylase [ Oenococcus oeniPSU-1]ZP_00323348870580COG3407: Mevalonate pyrophosphate decarboxylase [ Pediococcuspentosaceus ATCC 25745]E8667525400967diphosphomevalonate decarboxylase [imported] - Lactococcus lactissubsp. lactis (strain IL1403)EAE3111043552684unknown [environmental sequence]BAB077919695271diphosphomevalonate decarboxylase [ Streptomyces sp. CL190]CAC5137115212071mevalonate diphosphate decarboxylase [ Lactobacillus helveticus ]ZP_00045923002258COG3407: Mevalonate pyrophosphate decarboxylase [ Lactobacillusgasseri ]NP_96506142519131mevalonate pyrophosphate decarboxylase [ Lactobacillus johnsonii NCC533]BAD8680157753871mevalonate diphosphate decarboxylase [ Streptomyces sp. KO-3988]YP_19403858337453mevalonate diphosphate decarboxylase [ Lactobacillus acidophilusNCFM]YP_11841954024177putative diphosphomevalonate decarboxylase [ Nocardia farcinica IFM10152]EAK1882044571499unknown [environmental sequence]EAI8593544379784unknown [environmental sequence]NP_72133624379381putative mevalonate diphosphate decarboxylase [ Streptococcus mutansUA159]D9504425388338diphosphomevalonate decarboxylase [imported] - Streptococcuspneumoniae (strain TIGR4)AAG024569937408mevalonate diphosphate decarboxylase [ Streptococcus pneumoniae ]C9791425511486diphosphomevalonate decarboxylase (EC 4.1.1.33) [imported] -Streptococcus pneumoniae (strain R6)EAK4768344612560unknown [environmental sequence]EAB8642543039778unknown [environmental sequence]YP_14097155822530mevalonate pyrophosphate decarboxylase [ Streptococcus thermophilusCNRZ1066]YP_13908155820639mevalonate pyrophosphate decarboxylase [ Streptococcus thermophilusLMG 18311]BAD0737640882372mevalonate diphosphate decarboxylase [ Actinoplanes sp. A40644]NP_96851242523132Diphosphomevalonate decarboxylase [ Bdellovibrio bacteriovorusHD100]EAI0670544265427unknown [environmental sequence]YP_06001850914046Diphosphomevalonate decarboxylase [ Streptococcus pyogenesMGAS10394]AAG024519937401mevalonate diphosphate decarboxylase [ Streptococcus pyogenes ]NP_26907615674902mevalonate pyrophosphate decarboxylase [ Streptococcus pyogenes M1GAS]ZP_00366656808906COG3407: Mevalonate pyrophosphate decarboxylase [ Streptococcuspyogenes M49 591]NP_68832322537472diphosphomevalonate decarboxylase [ Streptococcus agalactiae2603V/R]NP_73583225011437hypothetical protein gbs1395 [ Streptococcus agalactiae NEM316]EAC4026743149093unknown [environmental sequence]AAL9758019748103mevalonate pyrophosphate decarboxylase [ Streptococcus pyogenesMGAS8232]EAI7691544367119unknown [environmental sequence]EAD3504243339207unknown [environmental sequence]YP_07312951598941mevalonate pyrophosphate decarboxylase [ Borrelia garinii PBi]EAI9009244385501unknown [environmental sequence]BAB078189711347mevalonate diphosphate decaroboxylase [ Kitasatospora griseola ]EAD7285043433025unknown [environmental sequence]NP_21282015595031mevalonate pyrophosphate decarboxylase [ Borrelia burgdorferi B31]YP_12433754297968hypothetical protein lpp2023 [ Legionella pneumophila str. Paris]YP_09605652842257mevalonate diphosphate decarboxylase [ Legionella pneumophila subsp.pneumophila str. Philadelphia 1]EAA3990329248368GLP_479_14176_13169 [ Giardia lamblia ATCC 50803]EAH0625244088237unknown [environmental sequence]YP_12735454294939hypothetical protein lpl2018 [ Legionella pneumophila str. Lens]EAD4575343361830unknown [environmental sequence]NP_80251928896169putative mevalonate pyrophosphate decarboxylase [ Streptococcuspyogenes SSI-1] TABLE 13Examples of IPP isomerase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONNP_0152086325140Idi1p [ Saccharomyces cerevisiae ]XP_44800850291151unnamed protein product [ Candida glabrata ]NP_98382845187605ADL268Cp [ Eremothecium gossypii ]XP_45512150310203unnamed protein product [ Kluyveromyces lactis ]XP_46235850427491unnamed protein product [ Debaryomyces hansenii ]EAL0168546442395potential isopentenyl diphosphate isomerase [ Candida albicans SC5314]XP_50497450555131hypothetical protein [ Yarrowia lipolytica ]XP_32842532415894hypothetical protein [ Neurospora crassa ]XP_36720039971619hypothetical protein MG07125.4 [ Magnaporthe grisea 70-15]XP_38989846136413conserved hypothetical protein [ Gibberella zeae PH-1]XP_40471649085144hypothetical protein AN0579.2 [ Aspergillus nidulans FGSC A4]CAD3715021627818isopentenyl-diphosphate delta-isomerase [ Aspergillus fumigatus ]NP_59516419111956isopentenyl-diphosphate delta-isomerase [ Schizosaccharomyces pombe ]XP_56664158258457isopentenyl-diphosphate delta-isomerase, putative [ Cryptococcusneoformans var. neoformans JEC21]XP_40245349077100hypothetical protein UM04838.1 [ Ustilago maydis 521]O355866225528Isopentenyl-diphosphate delta-isomerase 1 (IPP isomerase 1)AAP3660930584713Homo sapiens isopentenyl-diphosphate delta isomerase [syntheticconstruct]AAF378737188790isopentenyl pyrophosphate isomerase [ Dictyostelium discoideum ]NP_44599116758306isopentenyl-diphosphate delta isomerase [ Rattus norvegicus ]O426416225529Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)BAA339793790386IPP isomerase [ Xanthophyllomyces dendrorhous ]Q139076225527Isopentenyl-diphosphate delta-isomerase 1 (IPP isomerase 1)AAH2241848257241IDI1 protein [ Homo sapiens ]AAH1922748257312IDI1 protein [ Homo sapiens ]AAH5782735505325IDI1 protein [ Homo sapiens ]NP_00449940018633isopentenyl-diphosphate delta isomerase [ Homo sapiens ]AAH8978658477715Unknown (protein for MGC: 108635) [ Rattus norvegicus ]CAH9184455730243hypothetical protein [ Pongo pygmaeus ]XP_41856150732281PREDICTED: similar to isopentenyl-diphosphate delta isomerase; IPPisomerase [ Gallus gallus ]AAH0699948257093IDI1 protein [ Homo sapiens ]CAF9878247225155unnamed protein product [ Tetraodon nigroviridis ]NP_80887529366820isopentenyl-diphosphate delta isomerase [ Mus musculus ]XP_50762255633353PREDICTED: similar to isopentenyl-diphosphate delta isomerase; IPPisomerase [ Pan troglodytes ]AAH8264852139082LOC494671 protein [ Xenopus laevis ]NP_00101158332496hypothetical LOC496783 [ Xenopus tropicalis ]AAF299766856556isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Lactuca sativa ]AAG104239971806isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Tagetes erecta ]O489646225525Isopentenyl-diphosphate delta-isomerase I (IPP isomerase I)(Isopentenyl pyrophosphate isomerase I)AAF299736856550isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Adonis palaestina ]AAF299776856558isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Tagetes erecta ]AAQ8416735186998isopentenyl pyrophosphate isomerase [ Pueraria montana var. lobata ]AAF299746856552isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Adonis palaestina ]Q394726225526Isopentenyl-diphosphate delta-isomerase I (IPP isomerase I)(Isopentenyl pyrophosphate isomerase I)S495881085973isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 - Clarkiabreweri (fragment)AAL9198019568939isopentenyl pyrophosphate isomerase IDI1 [ Melaleuca alternifolia ]BAB4097313603406isopentenyl diphosphate isomerase 1 [ Nicotiana tabacum ]AAF299756856554isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Lactuca sativa ]T5202725493162isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 [validated] -Haematococcus pluvialisAAL9197919568937isopentenyl pyrophosphate isomerase IDI2 [ Melaleuca alternifolia ]T4681211362218isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) [imported] -Haematococcus pluvialisT5124811362217isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 2 [validated] -Haematococcus pluvialisBAB4097413603408isopentenyl diphosphate isomerase 2 [ Nicotiana tabacum ]O489656225532Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)(Isopentenyl pyrophosphate isomerase II)XP_22550934877710similar to isopentenyl diphosphate delta-isomerase type 2 [ Rattusnorvegicus ]XP_50640151963472PREDICTED OJ1612_A04.101 gene product [ Oryza sativa ( japonicacultivar-group)]AAF299786856560isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Oryza sativa ]AAH7654150369278Unknown (protein for IMAGE: 7037641) [ Danio rerio ]AAT9403351038230putative isopentenyl-diphosphate delta-isomerase [ Oryza sativa( japonica cultivar-group)]XP_22550234876517similar to isopentenyl diphosphate delta-isomerase type 2 [ Rattusnorvegicus ]Q394716225533Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)(Isopentenyl pyrophosphate isomerase II)AAB677431213450isopentenyl pyrophosphate isomerase [ Clarkia breweri ]NP_19714822326844isopentenyl-diphosphate delta-isomerase I [ Arabidopsis thaliana ]BAB096119759126isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Arabidopsis thaliana]AAD417665305669isopentenyl pyrophosphate isomerase [ Hevea brasiliensis ]AAB677411213442isopentenyl pyrophosphate isomerase [ Arabidopsis thaliana ]XP_39512548101420similar to CG8646-PA [ Apis mellifera ]AAN2878423505849At3g02780/F13E7_28 [ Arabidopsis thaliana ]AAF369967110585isopentenyl pyrophosphate:dimethylallyl pyrophosphate isomerase[ Brassica oleracea var. botrytis ]BAB1669015289752putative IPP isomerase [ Eucommia ulmoides ]AAQ1486933340598isopentenyl pyrophosphate isomerase [ Zea mays ]BAC6542128971819isopentenyl-diphosphate delta-isomerase [ Periploca sepium ]S713692129625isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) 1 - ArabidopsisthalianaAAF299796856562isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Arabidopsis thaliana ]AAF299806856564isopentenyl pyrophosphate:dimethyllallyl pyrophosphate isomerase[ Arabidopsis thaliana ]AAP2167430267831isopentenyl diphosphate delta-isomerase type 2 [ Mus musculus ]Q396646225534Isopentenyl-diphosphate delta-isomerase II (IPP isomerase II)(Isopentenyl pyrophosphate isomerase II)NP_65096224648688CG5919-PA [ Drosophila melanogaster ]AAM5028421429130RE22306p [ Drosophila melanogaster ]XP_32138858395620ENSANGP00000011643 [ Anopheles gambiae str. PEST]Q9BXS120978506Isopentenyl-diphosphate delta-isomerase 2 (IPP isomerase 2))T079797484383isopentenyl-diphosphate Delta-isomerase (EC 5.3.3.2) ipi1 -Chlamydomonas reinhardtiiXP_22550834876527similar to diphosphate dimethylallyl diphosphate isomerase 2 [ Rattusnorvegicus ]AAT9210251011386isopentenyl-diphosphate delta-isomerase [ Ixodes pacificus ]XP_22550734876555similar to isopentenyl diphosphate delta-isomerase type 2 [ Rattusnorvegicus ]XP_34462334876537similar to isopentenyl diphosphate delta-isomerase type 2 [ Rattusnorvegicus ]S44843630677K06H7.3 protein - Caenorhabditis elegansXP_22549827687955similar to diphosphate dimethylallyl diphosphate isomerase 2 [ Rattusnorvegicus ]AAT0846847013849isopentenyl-diphosphate isomerase [ Caenorhabditis elegans ]EAI7963644370808unknown [environmental sequence]CAE7505539587401Hypothetical protein CBG22969 [ Caenorhabditis briggsae ]EAL0404746444775potential isopentenyl diphosphate isomerase fragment [ Candida albicansSC5314]XP_22552834876543similar to isopentenyl diphosphate delta-isomerase type 2 [ Rattusnorvegicus ]XP_54428257040602PREDICTED: similar to isopentenyl-diphosphate delta isomerase [ Canisfamiliaris ]XP_22551127688013similar to diphosphate dimethylallyl diphosphate isomerase 2 [ Rattusnorvegicus ]P26173114853Isopentenyl-diphosphate delta-isomerase (IPP isomerase)(Bacteriochlorophyll synthase 20 kDa chain)EAJ0406944405322unknown [environmental sequence]EAH2749644127513unknown [environmental sequence]AAF914999653280isopentenyl pyrophosphate isomerase [ Daucus carota ]AAM4866121328655isopentyl-diphosphate delta-isomerase [uncultured proteobacterium]EAK1782644570145unknown [environmental sequence]EAD5951543391069unknown [environmental sequence]YP_12870254307682hypothetical isopentenyldiphosphate isomerase [ Photobacteriumprofundum SS9]EAK6665644639203unknown [environmental sequence]YP_11818954023947putative isopentenyldiphosphate isomerase [ Nocardia farcinica IFM10152]T5074011282665isopentenyl diphosphate isomerase homolog [imported] - RhodobactersphaeroidesZP_00207746193541COG1443: Isopentenyldiphosphate isomerase [ Rhodobacter sphaeroides2.4.1]EAK1647044568229unknown [environmental sequence]YP_16540356695056isopentyl-diphosphate delta-isomerase [ Silicibacter pomeroyi DSS-3]EAD0877543285885unknown [environmental sequence]YP_19562358616494putative isopentenyl-diphosphate delta-isomerase [ Azoarcus sp. EbN1]EAI3891844313358unknown [environmental sequence]NP_93058337527239hypothetical protein plu3365 [ Photorhabdus luminescens subsp.laumondii TTO1]YP_16025456478665isopentenyl-diphosphate delta-isomerase [ Azoarcus sp. EbN1]EAH6984244206571unknown [environmental sequence]EAK2625444582307unknown [environmental sequence]AAR2438138569721isopentyl-diphosphate delta isomerase [ Sus scrofa ]AAM4860721328600isopentenyl-diphosphate delta-isomerase, putative [unculturedproteobacterium]EAD8204943454744unknown [environmental sequence]ZP_00192445914126COG1443: Isopentenyldiphosphate isomerase [ Mesorhizobium sp.BNC1]YP_05678050843553isopentenyl-diphosphate delta-isomerase [ Propionibacterium acnesKPA171202]YP_05088050121713putative isopentenyl-diphosphate delta-isomerase [ Erwinia carotovorasubsp. atroseptica SCRI1043]EAF2923543749645unknown [environmental sequence]NP_63082321225044putative IPP isomerase [ Streptomyces coelicolor A3(2)]Q82MJ734582349Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)ZP_00337452010110COG1443: Isopentenyldiphosphate isomerase [ Silicibacter sp. TM1040]AAS7581945737905isopentenyl/dimethylallyl diphosphate isomerase [ Nicotianabenthamiana ]Q8KP3730913023Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)XP_50762155633351PREDICTED: similar to isopentenyl-diphosphate delta isomerase 2 [ Pantroglodytes ]XP_34462134876521similar to diphosphate dimethylallyl diphosphate isomerase 2 [ Rattusnorvegicus ]XP_34632234880719similar to diphosphate dimethylallyl diphosphate isomerase 2 [ Rattusnorvegicus ]YP_15206056414985probable isomerase [ Salmonella enterica subsp. enterica serovar ParatypiA str. ATCC 9150]AAT4244248429280putative isopentenyl diphosphate isomerase [ Edwardsiella ictaluri ]Q9KK7513878536Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)NP_80664929143307probable isomerase [ Salmonella enterica subsp. enterica serovar TyphiTy2]YP_06312450955836isopentenyldiphosphate isomerase [ Leifsonia xyli subsp. xyli str.CTCB07]Q8FND746395593Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)CAF2064741326485ISOPENTENYLDIPHOSPHATE ISOMERASE [ Corynebacteriumglutamicum ATCC 13032]Q8NN9923821718Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)Q7X5H246395586Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)NP_33624615841209isopentenyl-diphosphate delta-isomerase [ Mycobacterium tuberculosisCDC1551]Q83MJ946395588Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)P6092346395576Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)Q8FE7531563050Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (Isopentenylpyrophosphate isomerase)1R67A38493022Chain A, Y104a Mutant Of E. Coli Ipp IsomeraseQ9KWD113878537Isopentenyl-diphosphate delta-isomerase (IPP isomerase)Q7VEU046395585Isopentenyl-diphosphate delta-isomerase (IPP isomerase)B8433325410326isopentenyl pyrophosphate isomerase [imported] - Halobacterium sp.NRC-1NP_41736516130791isopentenyl diphosphate isomerase [ Escherichia coli K12]E8594425355426probable enzyme Z4227 [imported] - Escherichia coli (strain O157:H7,substrain EDL933)1HZTA15826050Chain A, Crystal Structure Of Metal-Free IsopentenylDiphosphate:dimethylallyl Diphosphate Isomerase1PVFB50513321Chain B, E. Coli Ipp Isomerase In Complex With DiphosphateEAD6357943403471unknown [environmental sequence]1I9AB13786886Chain B, Mevalonate 5-Diphosphate Decarboxylase And IsopentenylDiphosphate IsomeraseYP_01299246906603MutT/nudix family protein [ Listeria monocytogenes str. 4b F2365]ZP_00229347091503MutT/nudix family protein [ Listeria monocytogenes str. 4b H7858]EAI3719444310821unknown [environmental sequence]YP_13786455380014probable isopentenyl-diphosphate delta-isomerase [ Haloarculamarismortui ATCC 43049]CAD9205642516867putative isopentenyl diphosphate isomerase type 1 [ Haloferaxmediterranei ]1OW2B42543244Chain B, Isopentenylpyrophosphate-DimethylallylpyrophosphateIsomerase: Complex Of C67a Mutant With Eipp TABLE 14Examples of FPP synthase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONQ922502497455Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyldiphosphate synthetase)XP_36306539948036hypothetical protein MG08649.4 [ Magnaporthe grisea 70-15]XP_38696046124813FPPS_GIBFU Farnesyl pyrophosphate synthetase (FPP synthetase)(FPS) [ Gibberella zeae PH-1]Q922353122099Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyldiphosphate synthetase)XP_41214949116518hypothetical protein AN8012.2 [ Aspergillus nidulans FGSC A4]XP_50359950552378hypothetical protein [ Yarrowia lipolytica ]NP_59329919114211farnesyl pyrophosphate synthetase [ Schizosaccharomyces pombe ]CAD4286921955860farnesyl pyrophosphate synthase [ Mucor circinelloides f. lusitanicus ]XP_44878750292709unnamed protein product [ Candida glabrata ]NP_0123686322294Erg20p [ Saccharomyces cerevisiae ]T420817433997farnesyl-pyrophosphate synthetase - fission yeast( Schizosaccharomyces pombe ) (fragment)EAK9375146434339likely farnesyl diphosphate synthetase [ Candida albicans SC5314]XP_45130050302727FPPS_KLULA [ Kluyveromyces lactis ]XP_57113758267962isoprenoid biosynthesis-related protein, putative [ Cryptococcusneoformans var. neoformans JEC21]XP_46072050424267unnamed protein product [ Debaryomyces hansenii ]NP_98473945190485AEL122Wp [ Eremothecium gossypii ]BAD1536146367743farnesyl diphosphate synthase [ Lactarius chrysorrheus ]S714337433991farnesyl-pyrophosphate synthetase - ergot fungus (fragment)CAA656431523990farnesyl pyrophosphate synthetase [ Claviceps purpurea ]XP_39906149069544hypothetical protein UM01446.1 [ Ustilago maydis 521]S714327433990farnesyl-pyrophosphate synthetase - Sphaceloma manihoticola(fragment)AAH6891246249832MGC83119 protein [ Xenopus laevis ]1FPS1065289Chain, Avian Farnesyl Diphosphate Synthase (Fps) (E.C.2.5.1.10)P088363915686Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyldiphosphate synthetase)AAH8351553733369Unknown (protein for IMAGE: 7049076) [ Danio rerio ]1UBX1942050Chain, Structure Of Farnesyl Pyrophosphate Synthetase1UBY1942051Chain, Structure Of Farnesyl Pyrophosphate SynthetaseAAF378727188788farnesyl diphosphate synthase [ Dictyostelium discoideum ]NP_80346329135293farnesyl diphosphate synthase [ Bos taurus ]AAK6384714488053farnesyl diphosphate synthase [ Mentha X piperita ]AAV5889655710092farnesyl diphosphate synthase [ Centella asiatica ]T062727433988farnesyl-pyrophosphate synthetase FPS1 - tomatoJC48462117737farnesyl-pyrophosphate synthetase - Artemisia annuaP05369120478Farnesyl pyrophosphate synthetase (FPP synthetase) (FPS) (Farnesyldiphosphate synthetase)O2424125452945Farnesyl pyrophosphate synthetase 1 (FPP synthetase 1)O2424225452946Farnesyl pyrophosphate synthetase 2 (FPP synthetase 2)AAH5912537590777Testis-specific farnesyl pyrophosphate synthetase [ Rattus norvegicus ]AAH4849728913418Farnesyl diphosphate synthetase [ Mus musculus ]AAP7472032329199farnesyl diphosphate synthase [ Artemisia tridentata subsp. spiciformis ]CAG1185047225367unnamed protein product [ Tetraodon nigroviridis ]AAM5142921436457putative farnesyl-pyrophosphate synthetase FPS2 [ Arabidopsis thaliana ]AAP7471932329197farnesyl diphosphate synthase [ Artemisia tridentata subsp. spiciformis ]AAM0892720135548farnesyl pyrophosphate synthase [ Malus X domestica ]XP_53725257089113PREDICTED: similar to farnesyl diphosphate synthase [ Canisfamiliaris ]AAQ5601134013692farnesyl diphosphate synthase [ Hevea brasiliensis ]AAQ1487233340604truncated geranylgeranyl-diphosphate synthase [ Zea mays ]AAQ1487133340602geranylgeranyl-diphosphate synthase [ Zea mays ]AAD172044324960farnesyl diphosphate synthase [ Artemisia annua ]AAH8788656789674Farnesyl diphosphate synthetase [ Mus musculus ]AAK6815214573639farnesyldiphosphate synthase [X Citrofortunella microcarpa ]AAA52423182399farnesyl pyrophosphate synthetase (EC 2.5.1.1)S664702129849farnesyl-pyrophosphate synthetase fps1 - white lupineCAA290644725unnamed protein product [ Saccharomyces cerevisiae ]CAI1271555957735farnesyl diphosphate synthase [ Homo sapiens ]BAA0352340788949KIAA1293 [ Homo sapiens ]P143241346031Farnesyl pyrophosphate synthetase (FPP synthetase)S664712129850farnesyl-pyrophosphate synthetase fps2 - white lupineAAA35820182405farnesyl pyrophosphate synthetaseCAA591701491641dimethylallyltransferase [ Capsicum annuum ]BAB1668715289750putative FPP synthase 1 [ Eucommia ulmoides ]CAA727931922251farnesyl pyrophosphate synthase [ Gossypium arboreum ]CAH9107055728661hypothetical protein [ Pongo pygmaeus ]AAK5859414279425farnesyl pyrophosphate synthase [ Humulus lupulus ]AAB072641146159farnesyl diphosphate synthase short form [ Arabidopsis thaliana ]Q0915221431776Farnesyl pyrophosphate synthetase 1, mitochondrial precursor (FPPsynthetase 1)O649056016044Farnesyl pyrophosphate synthetase (FPP synthetase)BAB6082214422406putative FPP synthase 2 [ Eucommia ulmoides ]S520091076319farnesyl-pyrophosphate synthetase FPS1 - Arabidopsis thalianaNP_91711834911542putative farnesyl-pyrophosphate synthetase [ Oryza sativa ( japonicacultivar-group)]AAD326484894899farnesyl diphosphate synthase [ Artemisia annua ]AAA40960203582cholesterol-regulated protein CR39AAR2705338684029farnesyl diphosphate synthetase [ Ginkgo biloba ]AAU4399852353430putative farnesyl pyrophosphate synthase [ Oryza sativa ( japonicacultivar-group)]AAL8259518958450farnesyl pyrophosphare synthase [ Musa acuminata ]NP_91706934911444putative farnesyl-pyrophosphate synthetase [ Oryza sativa ( japonicacultivar-group)]XP_22880234879769similar to testis-specific farnesyl pyrophosphate synthetase [ Rattusnorvegicus ]BAD8181056785155putative farnesyl-pyrophosphate synthetase fps2 [ Oryza sativa ( japonicacultivar-group)]AAN6252224796660farnesyl pyrophosphate synthetase [ Eucommia ulmoides ]NP_59533419112126farnesyl pyrophosphate synthetase [ Schizosaccharomyces pombe ]T5206625458583probable farnesyl pyrophosphate synthase [imported] - riceAAL4906717946048RE52884p [ Drosophila melanogaster ]CAA089193395483dimethylallyltransferase; farnesyl pyrophosphate synthase [ Drosophilamelanogaster ]XP_54766257089869PREDICTED: similar to farnesyl diphosphate synthase [ Canisfamiliaris ]EAL2613554636732GA11601-PA [ Drosophila pseudoobscura ]BAB6082114422404putative FPP synthase 1 [ Eucommia ulmoides ]AAP7472132329201chrysanthemyl diphosphate synthase [ Artemisia tridentata subsp.spiciformis ]XP_49690251466663PREDICTED: similar to Farnesyl pyrophosphate synthetase (FPPsynthetase) [ Homo sapiens ]XP_47418250929309OSJNBa0071I13.18 [ Oryza sativa ( japonica cultivar-group)]CAA873271160178partial sequence [ Homo sapiens ]BAD2072947776234farnesyl pyrophosphate synthase [ Candida glabrata ]BAC5387330984142farnesyl pyrophosphate synthase [ Phaseolus lunatus ]BAB6949015991313farnesyl pyrophosphate syntase [ Bombyx mori ]NP_97456542572937farnesyl pyrophosphate synthetase 2 (FPS2)/FPP synthetase 2[ Arabidopsis thaliana ]CAA089185678609dimethylallyltransferase; farnesyl pyrophosphate synthase [ Agrotisipsilon ]AAP8626732527731Ac2-125 [ Rattus norvegicus ]AAO1773530522953farnesyl pyrophosphate synthase [ Trypanosoma brucei ]AAK7186114647139farnesyl pyrophosphate synthase [ Trypanosoma cruzi ]AAL7335718478919farnesyl diphosphate synthase precursor [ Trypanosoma cruzi ]AAO6355229124957putative farnesyl pyrophosphate synthase [ Plasmodium falciparum ]CAI0047156498227farnesyl pyrophosphate synthase, putative [ Plasmodium berghei ]NP_70115523508486farnesyl pyrophosphate synthase, putative [ Plasmodium falciparum3D7]XP_47418050929305OSJNBa0071I13.16 [ Oryza sativa ( japonica cultivar-group)]AAL7335818478922farnesyl diphosphate synthase precursor [ Trypanosoma cruzi ]EAH4899544167328unknown [environmental sequence]NP_49302717508563farnesyl pyrophosphate synthetase (1M510) [ Caenorhabditis elegans ]CAE7171139580204Hypothetical protein CBG18688 [ Caenorhabditis briggsae ]XP_48722051766977similar to farnesyl pyrophosphate synthase [ Mus musculus ] TABLE 15Examples of GGPP synthase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAT9287151013155YPL069C [ Saccharomyces cerevisiae ]XP_44702550289191unnamed protein product [ Candida glabrata ]NP_98462345190369AEL238Cp [ Eremothecium gossypii ]XP_39027346137163GGPP_GIBFU Geranylgeranyl pyrophosphate synthetase (GGPPsynthetase) [ Gibberella zeae PH-1]XP_40479149085320hypothetical protein AN0654.2 [ Aspergillus nidulans FGSC A4]XP_36848639974191hypothetical protein MG00758.4 [ Magnaporthe grisea 70-15]Q922366831550Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)AAO8543229468176geranylgeranyl diphosphate synthase [ Aspergillus nidulans ]XP_57277458271236farnesyltranstransferase, putative [ Cryptococcus neoformans var.neoformans JEC21]XP_50292350550901hypothetical protein [ Yarrowia lipolytica ]AAK1152513021716geranylgeranyl pyrophosphate synthase [ Penicillium paxilli ]XP_32692032412880GERANYLGERANYL PYROPHOSPHATE SYNTHETASE (GGPPSYNTHETASE) [ Neurospora crassa ]CAF3203242820719geranylgeranyl pyrophosphate synthetase, putative [ Aspergillusfumigatus ]BAD2996550355599Phoma betae geranylgeranyl diphosphate synthaseXP_38476746117498hypothetical protein FG04591.1 [ Gibberella zeae PH-1]BAD2997050355631geranylgeranyldiphosphate synthase [ Phoma betae ]CAB891157649674geranylgeranyl pyrophosphate synthase [ Mucor circinelloides f. lusitanicus ]CAG0954547229030unnamed protein product [ Tetraodon nigroviridis ]CAI1375355960163geranylgeranyl diphosphate synthase 1 [ Homo sapiens ]AAH6991347124116Geranylgeranyl diphosphate synthase 1 [ Mus musculus ]AAH6776845709211GGPS1 protein [ Homo sapiens ]XP_45500350309979unnamed protein product [ Kluyveromyces lactis ]P569669296978Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)NP_00100756090562geranylgeranyl diphosphate synthase 1 [ Rattus norvegicus ]AAT6571749409613geranylgeranyl diphosphate synthase [ Aspergillus flavus ]NP_95632941053321geranylgeranyl diphosphate synthase 1 [ Danio rerio ]BAA905256899844geranylgeranyl diphosphate synthase [ Nigrospora sphaerica ]XP_40572949087630hypothetical protein AN1592.2 [ Aspergillus nidulans FGSC A4]AAK1153113021724geranylgeranyl pyrophosphate synthase [ Penicillium paxilli ]XP_41228049119197hypothetical protein AN8143.2 [ Aspergillus nidulans FGSC A4]AAC052732944400geranylgeranyl pyrophosphate synthase [ Drosophila melanogaster ]NP_52395824660002CG8593-PA [ Drosophila melanogaster ]XP_40207449076128hypothetical protein UM04459.1 [ Ustilago maydis 521]EAL3019154641441GA21189-PA [ Drosophila pseudoobscura ]XP_53634057084951PREDICTED: hypothetical protein XP_536340 [ Canis familiaris ]XP_42468550811194PREDICTED: similar to geranylgeranyl diphosphate synthase 1, partial[ Gallus gallus ]AAH0679813905030Ggps1 protein [ Mus musculus ]AAP0601829841005similar to NM_010282 geranylgeranyl diphosphate synthase 1; GGPPsynthase [ Schistosoma japonicum ]XP_46033850423511unnamed protein product [ Debaryomyces hansenii ]AAC055952957271geranylgeranyl pyrophosphate synthase [ Drosophila melanogaster ]EAK9219746432727hypothetical protein CaO19.6674 [ Candida albicans SC5314]XP_53557357108760PREDICTED: similar to geranylgeranyl diphosphate synthase 1 [ Canisfamiliaris ]AAH8321253734594Zgc: 56514 protein [ Danio rerio ]XP_48646651827552similar to geranylgeranyl diphosphate synthase 1; GGPP synthase [ Musmusculus ]CAH1800651469024geranylgeranyl diphosphate synthase [ Fusarium proliferatum ]CAA755683549881geranylgeranyl diphosphate synthase [ Gibberella fujikuroi ]XP_39745548143654similar to CG8593-PA [ Apis mellifera ]XP_41094749101294hypothetical protein AN6810.2 [ Aspergillus nidulans FGSC A4]XP_38191446109712hypothetical protein FG01738.1 [ Gibberella zeae PH-1]XP_36447839959279hypothetical protein MG09448.4 [ Magnaporthe grisea 70-15]XP_36088939942704hypothetical protein MG03432.4 [ Magnaporthe grisea 70-15]XP_36921839975655hypothetical protein MG00026.4 [ Magnaporthe grisea 7 0-15]XP_40654449089926hypothetical protein AN2407.2 [ Aspergillus nidulans FGSC A4]XP_36759539972409hypothetical protein MG07506.4 [ Magnaporthe grisea 70-15]XP_36377539952117hypothetical protein MG01701.4 [ Magnaporthe grisea 70-15]XP_36848639974191hypothetical protein MG00758.4 [ Magnaporthe grisea 70-15]XP_39027346137163GGPP_GIBFU Geranylgeranyl pyrophosphate synthetase (GGPPsynthetase) [ Gibberella zeae PH-1]Q922366831550Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)AAK1152513021716geranylgeranyl pyrophosphate synthase [ Penicillium paxilli ]CAF3203242820719geranylgeranyl pyrophosphate synthetase, putative [ Aspergillusfumigatus ]XP_40479149085320hypothetical protein AN0654.2 [ Aspergillus nidulans FGSC A4]AAO8543229468176geranylgeranyl diphosphate synthase [ Aspergillus nidulans ]BAD2996550355599Phoma betae geranylgeranyl diphosphate synthaseBAD2997050355631geranylgeranyldiphosphate synthase [ Phoma betae ]BAA905256899844geranylgeranyl diphosphate synthase [ Nigrospora sphaerica ]AAT6571749409613geranylgeranyl diphosphate synthase [ Aspergillus flavus ]XP_38476746117498hypothetical protein FG04591.1 [ Gibberella zeae PH-1]CAB891157649674geranylgeranyl pyrophosphate synthase [ Mucor circinelloides f. lusitanicus ]XP_57277458271236farnesyltranstransferase, putative [ Cryptococcus neoformans var.neoformans JEC21]AAK1153113021724geranylgeranyl pyrophosphate synthase [ Penicillium paxilli ]XP_50292350550901hypothetical protein [ Yarrowia lipolytica ]CAI1375355960163geranylgeranyl diphosphate synthase 1 [ Homo sapiens ]CAG0954547229030unnamed protein product [ Tetraodon nigroviridis ]XP_41228049119197hypothetical protein AN8143.2 [ Aspergillus nidulans FGSC A4]P569669296978Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)NP_00100756090562geranylgeranyl diphosphate synthase 1 [ Rattus norvegicus ]AAH6991347124116Geranylgeranyl diphosphate synthase 1 [ Mus musculus ]AAH6776845709211GGPS1 protein [ Homo sapiens ]NP_95632941053321geranylgeranyl diphosphate synthase 1 [ Danio rerio ]EAL3019154641441GA21189-PA [ Drosophila pseudoobscura ]XP_42468550811194PREDICTED: similar to geranylgeranyl diphosphate synthase 1, partial[ Gallus gallus ]XP_53634057084951PREDICTED: hypothetical protein XP_536340 [ Canis familiaris ]NP_52395824660002CG8593-PA [ Drosophila melanogaster ]AAC052732944400geranylgeranyl pyrophosphate synthase [ Drosophila melanogaster ]XP_40572949087630hypothetical protein AN1592.2 [ Aspergillus nidulans FGSC A4]AAC055952957271geranylgeranyl pyrophosphate synthase [ Drosophila melanogaster ]XP_40207449076128hypothetical protein UM04459.1 [ Ustilago maydis 521]AAP0601829841005similar to NM_010282 geranylgeranyl diphosphate synthase 1; GGPPsynthase [ Schistosoma japonicum ]AAH0679813905030Ggps1 protein [ Mus musculus ]XP_53557357108760PREDICTED: similar to geranylgeranyl diphosphate synthase 1 [ Canisfamiliaris ]AAH8321253734594Zgc: 56514 protein [ Danio rerio ]AAP2108530097620albino-3 [ Neurospora crassa ]NP_98462345190369AEL238Cp [ Eremothecium gossypii ]XP_44702550289191unnamed protein product [ Candida glabrata ]AAT9287151013155YPL069C [ Saccharomyces cerevisiae ]XP_48646651827552similar to geranylgeranyl diphosphate synthase 1; GGPP synthase [ Musmusculus ]XP_41094749101294hypothetical protein AN6810.2 [ Aspergillus nidulans FGSC A4]XP_39745548143654similar to CG8593-PA [ Apis mellifera ]XP_45500350309979unnamed protein product [ Kluyveromyces lactis ]EAK9219746432727hypothetical protein CaO19.6674 [ Candida albicans SC5314]XP_38191446109712hypothetical protein FG01738.1 [ Gibberella zeae PH-1]XP_46033850423511unnamed protein product [ Debaryomyces hansenii ]CAH1800651469024geranylgeranyl diphosphate synthase [ Fusarium proliferatum ]XP_36088939942704hypothetical protein MG03432.4 [ Magnaporthe grisea 70-15]XP_40654449089926hypothetical protein AN2407.2 [ Aspergillus nidulans FGSC A4]XP_36447839959279hypothetical protein MG09448.4 [ Magnaporthe grisea 70-15]XP_36377539952117hypothetical protein MG01701.4 [ Magnaporthe grisea 70-15]XP_36759539972409hypothetical protein MG07506.4 [ Magnaporthe grisea 70-15]XP_36921839975655hypothetical protein MG00026.4 [ Magnaporthe grisea 70-15]C39273483124phytoene synthase - Erwinia herbicolaBAB7960018143445crtE [ Pantoea agglomerans pv. milletiae ]BAA14124216682crtE [ Pantoea ananatis ]AAN8559627228290Geranylgeranyl Pyrophosphate Synthase [ Pantoea stewartii ]AAA32797413730geranylgeranyl pyrophosphate synthaseQ08291585326Geranyltranstransferase (Farnesyl-diphosphate synthase) (FPP synthase)S525841073293crtE protein - Erwinia herbicolaS537221076576farnesyltranstransferase (EC 2.5.1.29) precursor - pepperAAC448481842242geranylgeranyl synthaseBAA195831944371geranylgeranyl pyrophosphate synthase [ Arabidopsis thaliana ]S712302129674geranylgeranyl pyrophosphate synthase (EC 2.5.1.—) 2 precursor -Arabidopsis thalianaBAA231572578822geranyl geranyl pyrophosphate synthase [ Arabidopsis thaliana ]AAC778743885426geranylgeranyl pyrophosphate synthase [ Helianthus annuus ]CAB387444490594geranylgeranyl pyrophosphate synthase [ Rhodobacter sphaeroides ]BAA780474958920GGPP synthase [ Daucus carota ]BAA826135631295geranylgeranyl diphosphate synthase (SelGGPS) [ Synechococcuselongatus ]CAB560645912297geranylgeranyl pyrophosphate synthase [ Paracoccus marcusii ]BAA862846277254geranylgeranyl pyrophosphate synthase [ Croton sublyratus ]T110217447356farnesyltranstransferase (EC 2.5.1.29) - white lupineAAF781998650415geranylgeranyl synthase [ Bradyrhizobium sp. ORS278]AAG104249971808GGDP synthase [ Tagetes erecta]CAC1056110637876gpp synthase large subunit [ Mentha × piperita ]T5087911279298phytoene synthase [imported] - Rubrivivax gelatinosusBAB0134311994221geranyl geranyl pyrophosphate synthase-like protein [ Arabidopsisthaliana ]Q4269813431546Geranylgeranyl pyrophosphate synthetase, chloroplast precursor (GGPPsynthetase)Q4313313431547Geranylgeranyl pyrophosphate synthetase, chloroplast precursor (GGPPsynthetase)P5497613878921Geranylgeranyl pyrophosphate synthetase (GGPP synthetase)(Farnesyltranstransferase)BAB5060014023995geranyltranstransferase; farnesyl-diphosphate synthase [ Mesorhizobiumloti MAFF303099]BAB6067814325238geranylgeranyl diphosphate synthase [ Hevea brasiliensis ]BAB6082014422402putative GGPP synthase [ Eucommia ulmoides ]NP_18958915228704geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase[ Arabidopsis thaliana ]NP_18865115231055geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase[ Arabidopsis thaliana ]NP_18806915231869geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase[ Arabidopsis thaliana ]NP_18807315231881geranylgeranyl pyrophosphate synthase, putative/GGPP synthetase[ Arabidopsis thaliana ]AAL0199715553715farnesyl diphosphate synthase [ Xanthobacter sp. Py2]AAL0199815553717geranylgeranyl diphosphate synthase [ Xanthobacter sp. Py2]NP_25273215599238geranyltranstransferase [ Pseudomonas aeruginosa PAO1]NP_24547015602398IspA [ Pasteurella multocida subsp. multocida str. Pm70]NP_39030816079484hypothetical protein BSU24280 [ Bacillus subtilis subsp. subtilis str. 168]NP_44001016329282geranylgeranyl pyrophosphate synthase [ Synechocystis sp. PCC 6803]NP_44001016329282geranylgeranyl pyrophosphate synthase [ Synechocystis sp. PCC 6803]AAL1761417352451geranylgeranyl diphosphate synthase [ Abies grandis ]NP_52034317546941PROBABLE GERANYLTRANSTRANSFERASE (FARNESYL-DIPHOSPHATE SYNTHASE) PROTEIN [ Ralstonia solanacearum GMAAL7634918645048geranyltranstransferase [uncultured proteobacterium]AAM2163820386366geranylgeranyl pyrophosphate synthase [ Cistus incanus subsp. creticus ]AAM2163920386368geranylgeranyl pyrophosphate synthase [ Cistus incanus subsp. creticus ]NP_62291620807745Geranylgeranyl pyrophosphate synthase [ Thermoanaerobactertengcongensis MB4]AAM4865021328644geranylgeranyl pyrophosphate synthetase [uncultured proteobacterium]NP_65979421492720probable polyprenyl synthetase. [ Rhizobium etli ]AAM6449621592547putative geranylgeranyl pyrophosphate synthase GGPS3 [ Arabidopsisthaliana ]AAM6510721593158geranylgeranyl pyrophosphate synthase [ Arabidopsis thaliana ]NP_68081122297564geranylgeranyl pyrophosphate synthase [ Thermosynechococcuselongatus BP-1]ZP_00047423003800COG0142: Geranylgeranyl pyrophosphate synthase [ Lactobacillusgasseri ]ZP_00125223469933COG0142: Geranylgeranyl pyrophosphate synthase [ Pseudomonassyringae pv. syringae B728a]NP_69876023502633geranyltranstransferase [ Brucella suis 1330]E8456625313373probable geranylgeranyl pyrophosphate synthase [imported] -Arabidopsis thalianaF8543425313385geranylgeranyl pyrophosphate synthase [imported] - ArabidopsisthalianaAC124525313389geranyltranstransferase homolog lmo1363 [imported] - Listeriamonocytogenes (strain EGD-e)E8399725313393geranyltranstransferase BH2781 [imported] - Bacillus halodurans (strainC-125)G8456625313395probable geranylgeranyl pyrophosphate synthase [imported] -Arabidopsis thalianaAH291025315863geranyltranstransferase [imported] - Agrobacterium tumefaciens (strainC58, Dupont)D8750525398795geranyltranstransferase [imported] - Caulobacter crescentusA8993225505949hypothetical protein ispA [imported] - Staphylococcus aureus (strainN315)F9768525520741geranyltransferase (AF203881) [imported] - Agrobacterium tumefaciens(strain C58, Cereon)AI328525527013geranyltranstransferase (EC 2.5.1.10) [imported] - Brucella melitensis(strain 16M)BAC4257126450928putative geranylgeranyl pyrophosphate synthase GGPS3 [ Arabidopsisthaliana ]NP_78519528378303geranyltranstransferase [ Lactobacillus plantarum WCFS1]NP_79054628867927geranyltranstransferase [ Pseudomonas syringae pv. tomato str. DC3000]AAO6339228950937At2g23800 [ Arabidopsis thaliana]AAO9311329893480geranylgeranyl pyrophosphate synthetase; CrtE [ Rubrivivaxgelatinosus ]NP_83389130022260Dimethylallyltransferase [ Bacillus cereus ATCC 14579]AAP5903731621279CrtE [ Thiocapsa roseopersicina ]ZP_00137432039216COG0142: Geranylgeranyl pyrophosphate synthase [ Pseudomonasaeruginosa UCBPP-PA14]NP_86476632471772geranylgeranyl pyrophosphate synthetase [precursor] [ Rhodopirellulabaltica SH 1]NP_87552133240579Geranylgeranyl pyrophosphate synthase [ Prochlorococcus marinussubsp. marinus str. CCMP1375]NP_88139933593755probable geranyltranstransferase [ Bordetella pertussis Tohama I]NP_88469433597051probable geranyltranstransferase [ Bordetella parapertussis 12822]NP_88845633600896probable geranyltranstransferase [ Bordetella bronchiseptica RB50]NP_89318733861626Polyprenyl synthetase [ Prochlorococcus marinus subsp. pastoris str.CCMP1986]NP_89494033863380Polyprenyl synthetase [ Prochlorococcus marinus str. MIT 9313]NP_89683533865276geranylgeranyl pyrophosphate synthase [ Synechococcus sp. WH 8102]NP_89683533865276geranylgeranyl pyrophosphate synthase [ Synechococcus sp. WH 8102]AAQ6508634365549At3g14530 [ Arabidopsis thaliana ]NP_94587739933601putative geranyltranstransferase (farnesyl-diphosphate synthase)[ Rhodopseudomonas palustris CGA009]NP_94686739934591geranylgeranyl pyrophosphate synthase [ Rhodopseudomonas palustrisCGA009]NP_95281539996864geranyltranstransferase [ Geobacter sulfurreducens PCA]AAR3780540062934polyprenyl synthetase [uncultured bacterium 442]AAR3785840062988geranylgeranyl pyrophosphate synthetase [uncultured bacterium 443]AAR9849541018904geranyl geranyl synthase [ Bradyrhizobium sp. ORS278]AAR9908241059107geranylgeranyl pyrophosphate synthase [ Plectranthus barbatus ]NP_96534942519419geranyltranstransferase [ Lactobacillus johnsonii NCC 533]NP_98054442783297geranyltranstransferase [ Bacillus cereus ATCC 10987]EAA9634842858148unknown [environmental sequence]EAB3650642939031unknown [environmental sequence]EAB3664242939300unknown [environmental sequence]EAC3920843146996unknown [environmental sequence]EAD2600743320598unknown [environmental sequence]EAE4308443576643unknown [environmental sequence]EAE7006143630884unknown [environmental sequence]EAF7030843832107unknown [environmental sequence]EAG8849444055952unknown [environmental sequence]EAH5206044173220unknown [environmental sequence]EAH7835444221788unknown [environmental sequence]EAH8411744231960unknown [environmental sequence]EAI1176244272832unknown [environmental sequence]EAI4939144328289unknown [environmental sequence]EAI5484644336042unknown [environmental sequence]EAI6835644355138unknown [environmental sequence]EAI6871344355672unknown [environmental sequence]EAI6940144356609unknown [environmental sequence]EAI7387344362658unknown [environmental sequence]EAJ7363444506168unknown [environmental sequence]EAJ7735144511694unknown [environmental sequence]EAK7063944644254unknown [environmental sequence]ZP_00175145523854COG0142: Geranylgeranyl pyrophosphate synthase [ Crocosphaerawatsonii WH 8501]AAS7625345752710At1g49530 [ Arabidopsis thaliana ]ZP_00195745916757COG0142: Geranylgeranyl pyrophosphate synthase [ Mesorhizobium sp.BNC1]1RTRB46015556Chain B, Crystal Structure Of S. Aureus Farnesyl PyrophosphateSynthaseZP_00186346105954COG0142: Geranylgeranyl pyrophosphate synthase [ Rubrobacterxylanophilus DSM 9941]ZP_00200246107045COG0142: Geranylgeranyl pyrophosphate synthase [ Rubrobacterxylanophilus DSM 9941]ZP_00171146132567COG0142: Geranylgeranyl pyrophosphate synthase [ Ralstonia eutrophaJMP134]ZP_00207346192680COG0142: Geranylgeranyl pyrophosphate synthase [ Rhodobactersphaeroides 2.4.1]ZP_00207446192861COG0142: Geranylgeranyl pyrophosphate synthase [ Rhodobactersphaeroides 2.4.1]AAS8286046241274geranyl diphosphate synthase large subunit [ Antirrhinum majus ]ZP_00210846308696COG0142: Geranylgeranyl pyrophosphate synthase [ Ehrlichia canis str.Jake]YP_01056846579760geranylgeranyl diphosphate synthase [ Desulfovibrio vulgaris subsp.vulgaris str. Hildenborough]BAD1831347076770geranyltranstransferase [ Geobacillus stearothermophilus ]ZP_00231547093750geranyltranstransferase [ Listeria monocytogenes str. 4b H7858]ZP_00233547095946geranyltranstransferase [ Listeria monocytogenes str. ½a F6854]AAT3522247531118fusion of carotene synthesis proteins [synthetic construct]ZP_00240147569437geranyltranstransferase [ Bacillus cereus G9241]ZP_00243547573473COG0142: Geranylgeranyl pyrophosphate synthase [ Rubrivivaxgelatinosus PM1]ZP_00262648728941COG0142: Geranylgeranyl pyrophosphate synthase [ Pseudomonasfluorescens PfO-1]ZP_00270248765678COG0142: Geranylgeranyl pyrophosphate synthase [ Rhodospirillumrubrum ]ZP_00270548766028COG0142: Geranylgeranyl pyrophosphate synthase [ Rhodospirillumrubrum ]ZP_00273248768894COG0142: Geranylgeranyl pyrophosphate synthase [ Ralstoniametallidurans CH34]ZP_00291448834438COG0142: Geranylgeranyl pyrophosphate synthase [ Magnetococcus sp.MC-1]ZP_00302448848203COG0142: Geranylgeranyl pyrophosphate synthase [ Novosphingobiumaromaticivorans DSM 12444]ZP_00312948858958COG0142: Geranylgeranyl pyrophosphate synthase [ Clostridiumthermocellum ATCC 27405]ZP_00317748863841COG0142: Geranylgeranyl pyrophosphate synthase [ Microbulbiferdegradans 2-40]ZP_00322548869790COG0142: Geranylgeranyl pyrophosphate synthase [ Pediococcuspentosaceus ATCC 25745]AAT5132349086036PA4043 [synthetic construct]ZP_00330149236117COG0142: Geranylgeranyl pyrophosphate synthase [ Moorellathermoacetica ATCC 39073]YP_03422249476181Geranyltranstransferase (farnesyl-diphosphate synthase) [ Bartonellahenselae str. Houston-1]YP_04099549483771putative geranyltranstransferase [ Staphylococcus aureus subsp. aureusMRSA252]YP_04357949486358putative geranyltranstransferase [ Staphylococcus aureus subsp. aureusMSSA476]AAT7198250253560At3g32040 [ Arabidopsis thaliana ]AAT9031550952782putative geranylgeranyl pyrophosphate synthetase [unculturedproteobacterium eBACred25D05]YP_06643551246551probable geranylgeranyl pyrophosphate synthase [ Desulfotaleapsychrophila LSv54]YP_07567351892982geranylgeranyl pyrophosphate synthase [ Symbiobacteriumthermophilum IAM 14863]YP_08551152141318geranyltranstransferase [ Bacillus cereus ZK]YP_09216652786337YqiD [ Bacillus licheniformis ATCC 14580]ZP_00129853691368COG0142: Geranylgeranyl pyrophosphate synthase [ Desulfovibriodesulfuricans G20]YP_10513653716444geranyltranstransferase [ Burkholderia mallei ATCC 23344]YP_11176953722784geranyltranstransferase [ Burkholderia pseudomallei K96243]ZP_00363054030933COG0142: Geranylgeranyl pyrophosphate synthase [ Polaromonas sp.JS666]YP_12902154308001putative geranyltranstransferase [ Photobacterium profundum SS9]AAV7439556122554geranylgeranyl diphosphate synthase [ Adonis palaestina ]AAV7439656122556geranylgeranyl diphosphate synthase [ Adonis palaestina ]YP_14824656420928geranyltranstransferase (farnesyl-diphosphate synthase) [ Geobacilluskaustophilus HTA426]YP_15651856461237Geranylgeranyl pyrophosphate synthase [ Idiomarina loihiensis L2TR]YP_16259056551751geranyltranstransferase [ Zymomonas mobilis subsp. mobilis ZM4]YP_17147056750769geranylgeranyl pyrophosphate synthase [ Synechococcus elongatus PCC6301]YP_17595956964228geranyltranstransferase [ Bacillus clausii KSM-K16]YP_18640757650478geranyltranstransferase [ Staphylococcus aureus subsp. aureus COL]YP_19069058038726Dimethylallyltransferase [ Gluconobacter oxydans 621H]AAW6665858201026geranyl diphosphate synthase [ Picrorhiza kurrooa ]YP_19418758337602geranylgeranyl diphosphate (GGPP) synthase [ Lactobacillus acidophilusNCFM]YP_19746958579257Possible geranyltranstransferase [ Ehrlichia ruminantium str.Welgevonden]YP_20193858582922geranyltranstransferase; farnesyl-diphosphate synthase [ Xanthomonasoryzae pv. oryzae KACC10331]YP_19651058617311Possible geranyltranstransferase [ Ehrlichia ruminantium str. Gardel] TABLE 16Examples of squalene synthetase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAA34597171481squalene synthetaseCAA425833686farnesyl-diphosphate farnesyltransferase [ Saccharomyces cerevisiae ]Q9HGZ651704336Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)BAB122079955387squalene synthase [ Candida glabrata ]XP_45345750306959unnamed protein product [ Kluyveromyces lactis ]Q752X951701405Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)O7416551701378Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)XP_45857950420093unnamed protein product [ Debaryomyces hansenii ]EAK9545146436082hypothetical protein CaO19.11099 [ Candida albicans SC5314]P785892499979Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)Q9Y75351701459Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)XP_40751349092104hypothetical protein AN3376.2 [ Aspergillus nidulans FGSC A4]XP_36439439958237hypothetical protein MG09239.4 [ Magnaporthe grisea 70-15]Q7S4Z651701416Probable farnesyl-diphosphate farnesyltransferase (Squalene synthetase)CAD6058127764301unnamed protein product [ Podospora anserina ]XP_38955746135731hypothetical protein FG09381.1 [ Gibberella zeae PH-1]NP_59536319112155farnesyl-diphosphate farnesyltransferase [ Schizosaccharomyces pombe ]B48057477750farnesyl-diphosphate farnesyltransferase (EC 2.5.1.21) - fission yeast( Schizosaccharomyces pombe )NP_03432134328173farnesyl diphosphate farnesyl transferase 1 [ Mus musculus ]CAH9251755731622hypothetical protein [ Pongo pygmaeus ]AAF000386002565squalene synthase [ Mus musculus ]P537981706773Farnesyl-diphosphate farnesyltransferase (Squalene synthetase) (SQS)(SS) (FPP:FPP farnesyltransferase)NP_00445331542632farnesyl-diphosphate farnesyltransferase 1 [ Homo sapiens ]AAP3667130584837Homo sapiens farnesyl-diphosphate farnesyltransferase 1 [syntheticconstruct]1EZFC11514497Chain C, Crystal Structure Of Human Squalene SynthaseAAH0925114328083Farnesyl-diphosphate farnesyltransferase 1 [ Homo sapiens ]AAH8401654035372LOC494973 protein [ Xenopus laevis ]I520902136196squalene synthase - humanXP_42004350745256PREDICTED: similar to Farnesyl-diphosphate farnesyltransferase 1[ Gallus gallus ]AAH8181051858605Farnesyl diphosphate farnesyl transferase 1 [ Rattus norvegicus ]CAE4836350841455TPA: FDFT1 protein [ Bos taurus ]XP_56978358265254farnesyl-diphosphate farnesyltransferase, putative [ Cryptococcusneoformans var. neoformans JEC21]XP_56978258265252farnesyl-diphosphate farnesyltransferase, putative [ Cryptococcusneoformans var. neoformans JEC21]XP_53455757105080PREDICTED: similar to FDFT1 protein [ Canis familiaris ]XP_40198949075920FDFT_USTMA Farnesyl-diphosphate farnesyltransferase (Squalenesynthetase) [ Ustilago maydis 521] TABLE 17aExamples of phytoene dehydrogenase polypeptides.ACCESSIONPROTEIN DESCRIPTION1613414BcrtI gene1613414FcrtD gene1904206Amethoxyneurosporene dehydrogenase2121278Azeta carotene desaturaseA86203hypothetical protein [imported] - Arabidopsis thalianaA96612hypothetical protein F12K22.18 [imported] - Arabidopsis thalianaA99470phytoene dehydrogenase (desaturase) (crtI) [imported] - Sulfolobus solfataricusAAA24820phytoene dehydrogenase [ Pantoea agglomerans ]AAA34001phytoene desaturaseAAA50313photoprotective pigmentAAA64981phytoene dehydrogenase [ Pantoea agglomerans ]AAA91161zeta-carotene desaturase precursorAAA99519phytoene desaturaseAAC44798hydroxyneurosporene and rhodopin dehydrogenase [ Rubrivivax gelatinosus ]AAC44850phytoene desaturaseAAC48983phytoene dehydrogenase precursorAAF78201phytoene desaturase [ Bradyrhizobium sp. ORS278]AAG10426phytoene desaturase [ Tagetes erecta ]AAG14399zeta-carotene desaturase precursor [ Oryza sativa ]AAG28700CrtI [ Streptomyces griseus ]AAG50743hypothetical protein [ Arabidopsis thaliana ]AAH85048Unknown (protein for MGC: 97898) [ Xenopus laevis ]AAK51545phytoene desaturase [ Citrus × paradisi ]AAK51557zeta-carotene desaturase precursor [ Citrus × paradisi ]AAK64299phytoene desaturase [ Corynebacterium glutamicum ]AAL02000phytoene dehydrogenase [ Xanthobacter sp. Py2]AAL15300AT4g14210/dl3145c [ Arabidopsis thaliana ]AAL38046phytoene desaturase [ Hordeum vulgare ]AAL73986hypothetical protein MMT-7 [ Mus musculus ]AAL80005phytoene desaturase [ Sandersonia aurantiaca ]AAL91366carotenoid isomerase [ Lycopersicon esculentum ]AAM45380phytoene desaturase [ Tagetes erecta ]AAM48646phytoene dehydrogenase [uncultured proteobacterium]AAM63349putative zeta-carotene desaturase precursor [ Arabidopsis thaliana ]AAM94364phytoene desaturase [ Agromyces mediolanus ]AAN75037CrtD [ Rhodospirillum rubrum ]AAN85599Phytoene Desaturase [ Pantoea stewartii ]AAO24235phytoene desaturase [ Crocus sativus ]AAO46892phytoene dehydrogenase [ Blakeslea trispora ]AAO46894phytoene dehydrogenase [ Blakeslea trispora ]AAO53257phytoene desaturase [ Xanthophyllomyces dendrorhous ]AAO53258phytoene desaturase splice variant [ Xanthophyllomyces dendrorhous ]AAO64750At5g49550/K6M13_10 [ Arabidopsis thaliana ]AAO93135phytoene dehydrogenase; CrtI [ Rubrivivax gelatinosus ]AAP59036CrtD [ Thiocapsa roseopersicina ]AAP79175phytoene dehydrogenase [ Bigelowiella natans ]AAQ04224zeta-carotene desaturase ZDS1 [ Malus × domestica]AAQ04225zeta-carotene desaturase ZDS2 [ Malus × domestica]AAQ65246phytoene desaturase [ Methylobacterium extorquens ]AAQ65246phytoene desaturase [ Methylobacterium extorquens ]AAQ88931WLPL439 [ Homo sapiens ]AAR37797methoxyneurosporene dehydrogenase [uncultured bacterium 442]AAR37802phytoene dehydrogenase [uncultured bacterium 442]AAR37850methoxyneurosporene dehydrogenase [uncultured bacterium 443]AAR37855phytoene dehydrogenase [uncultured bacterium 443]AAR86105phytoene desaturase [ Momordica charantia var. abbreviata ]AAR98491phytoene desaturase [ Bradyrhizobium sp. ORS278]AAR98494phytoene dehydrogenase [ Bradyrhizobium sp. ORS278]AAR98733phytoene desaturase [ Lilium longiflorum ]AAS17750phytoene desaturase [ Solanum tuberosum ]AAT01639phytoene desaturase [ Petunia × hybrida ]AAT35222fusion of carotene synthesis proteins [synthetic construct]AAT74579PDS [ Citrus sinensis ]AAT74580ZDS [ Citrus sinensis ]AAT76050zeta-carotene desaturase [ Citrus clementina ]AAT76434phytoene desaturase [ Hydrilla verticillata ]AAT90316putative methoxyneurosporene dehydrogenase [uncultured proteobacteriumeBACred25D05]AAU34019retina and RPE/choroid [ Macaca fascicularis ]AAW23161phytoene dehydrogenase [ Rhodococcus erythropolis ]AB2035phytoene desaturase [imported] - Nostoc sp. (strain PCC 7120)AB2064hypothetical protein alr2064 [imported] - Nostoc sp. (strain PCC 7120)AC2446hypothetical protein all5123 [imported] - Nostoc sp. (strain PCC 7120)AF1557phytoene dehydrogenase homolog lin0999 [imported] - Listeria innocua (strainClip11262)AF2029hypothetical protein alr1788 [imported] - Nostoc sp. (strain PCC 7120)AG2103zeta-carotene desaturase [imported] - Nostoc sp. (strain PCC 7120)AG2509zeta-carotene desaturase [imported] - Nostoc sp. (strain PCC 7120) plasmidpCC7120alphaAH1199phytoene dehydrogenase homolog lmo1000 [imported] - Listeria monocytogenes(strain EGD-e)AI2185hypothetical protein all3040 [imported] - Nostoc sp. (strain PCC 7120)AI2273hypothetical protein all3744 [imported] - Nostoc sp. (strain PCC 7120)B55548crtN protein - Staphylococcus aureusB84327phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1B90061squalene synthase [imported] - Staphylococcus aureus (strain N315)BAA14127crtI [ Pantoea ananatis ]BAA20276phytoene desaturase [ Erythrobacter longus ]BAA76534Phytoene disaturase [ Acidiphilium rubrum ]BAB10768phytoene dehydrogenase-like [ Arabidopsis thaliana ]BAB50520phytoene dehydrogenase [ Mesorhizobium loti MAFF303099]BAB51896mlr5446 [ Mesorhizobium loti MAFF303099]BAB68552zeta-carotene desaturase [ Citrus unshiu ]BAB79603crtI [ Pantoea agglomerans pv. milletiae]BAB82461phytoene desaturase [ Gentiana lutea ]BAB82462phytoene desaturase [ Gentiana lutea ]BAB98016Phytoene dehydrogenase and related proteins [ Corynebacterium glutamicum ATCC13032]BAC75676putative phytoene desaturase [ Gordonia sp. TM414]BAC77668phytoene desaturase [marine bacterium P99-3]BAC77671gamma-carotene desaturase [marine bacterium P99-3]BAD07279phytoene desaturase [ Citrus sinensis ]BAD07280zeta-carotene desaturase [ Citrus sinensis ]BAD07287phytoene desaturase [ Citrus limon ]BAD07288zeta-carotene desaturase [ Citrus limon ]CAA52098squalene synthase [ Staphylococcus aureus ]CAA60479Phytoene desaturase [ Haematococcus pluvialis ]CAA66626unnamed protein product [ Staphylococcus aureus ]CAB38739phytoene dehydrogenase [ Rhodobacter sphaeroides ]CAB38743methoxyneurosporene dehydrogenase [ Rhodobacter sphaeroides ]CAB40843phytoene dehydrogenase [ Mucor circinelloides f. lusitanicus ]CAB56041zeta-carotene desaturase [ Nostoc sp. PCC 7120]CAB56062phytoene desaturase [ Paracoccus marcusii ]CAB59726phytoene desaturase [ Lycopersicon esculentum ]CAB65434zeta carotene desaturase [ Synechococcus leopoliensis ]CAB94794phytoene dehydrogenase [ Mycobacterium aurum ]CAC85667zeta-carotene desaturase [ Citrus sinensis ]CAD19989phytoene dehydrogenase [ Gibberella fujikuroi ]CAD27442putative zeta-carotene desaturase [ Helianthus annuus ]CAD55814putative zeta-carotene desaturase [ Helianthus annuus ]CAE00192phytoene desaturase [ Nicotiana benthamiana ]CAE83576phytoene desaturase [ Nicotiana tabacum ]CAF19330PHYTOENE DEHYDROGENASE (DESATURASE) [ Corynebacteriumglutamicum ATCC 13032]CAF21094PHYTOENE DEHYDROGENASE (DESATURASE) (N-terminal fragment)[ Corynebacterium glutamicum ATCC 13032]CAF21337phytoene desaturase [ Pisum sativum ]CAH91165hypothetical protein [ Pongo pygmaeus ]E90061hypothetical protein SA2351 [imported] - Staphylococcus aureus (strain N315)EAA90383unknown [environmental sequence]EAA98598unknown [environmental sequence]EAB09790unknown [environmental sequence]EAB14136unknown [environmental sequence]EAB18725unknown [environmental sequence]EAB29729unknown [environmental sequence]EAB30992unknown [environmental sequence]EAB41377unknown [environmental sequence]EAB54727unknown [environmental sequence]EAB76679unknown [environmental sequence]EAB87028unknown [environmental sequence]EAB92587unknown [environmental sequence]EAB94459unknown [environmental sequence]EAB96864unknown [environmental sequence]EAC01884unknown [environmental sequence]EAC38895unknown [environmental sequence]EAC60360unknown [environmental sequence]EAD05874unknown [environmental sequence]EAD05999unknown [environmental sequence]EAD20520unknown [environmental sequence]EAE06978unknown [environmental sequence]EAE70773unknown [environmental sequence]EAF04985unknown [environmental sequence]EAF51354unknown [environmental sequence]EAF62819unknown [environmental sequence]EAF75453unknown [environmental sequence]EAG09111unknown [environmental sequence]EAG19412unknown [environmental sequence]EAG23070unknown [environmental sequence]EAG25053unknown [environmental sequence]EAG25054unknown [environmental sequence]EAG29279unknown [environmental sequence]EAG39845unknown [environmental sequence]EAG56100unknown [environmental sequence]EAG63013unknown [environmental sequence]EAG68633unknown [environmental sequence]EAG71574unknown [environmental sequence]EAG89835unknown [environmental sequence]EAH04928unknown [environmental sequence]EAH04936unknown [environmental sequence]EAH08586unknown [environmental sequence]EAH22597unknown [environmental sequence]EAH22853unknown [environmental sequence]EAH31648unknown [environmental sequence]EAH55579unknown [environmental sequence]EAH68071unknown [environmental sequence]EAH73302unknown [environmental sequence]EAH79041unknown [environmental sequence]EAH86965unknown [environmental sequence]EAH97108unknown [environmental sequence]EAH99977unknown [environmental sequence]EAI01660unknown [environmental sequence]EAI03576unknown [environmental sequence]EAI06784unknown [environmental sequence]EAI11087unknown [environmental sequence]EAI15261unknown [environmental sequence]EAI15547unknown [environmental sequence]EAI17521unknown [environmental sequence]EAI21398unknown [environmental sequence]EAI29728unknown [environmental sequence]EAI38468unknown [environmental sequence]EAI43591unknown [environmental sequence]EAI51589unknown [environmental sequence]EAI58453unknown [environmental sequence]EAI72974unknown [environmental sequence]EAI77885unknown [environmental sequence]EAI78272unknown [environmental sequence]EAI80262unknown [environmental sequence]EAI83937unknown [environmental sequence]EAI86664unknown [environmental sequence]EAJ00517unknown [environmental sequence]EAJ05570unknown [environmental sequence]EAJ08238unknown [environmental sequence]EAJ15524unknown [environmental sequence]EAJ18144unknown [environmental sequence]EAJ20649unknown [environmental sequence]EAJ21683unknown [environmental sequence]EAJ24413unknown [environmental sequence]EAJ28774unknown [environmental sequence]EAJ30522unknown [environmental sequence]EAJ35157unknown [environmental sequence]EAJ37407unknown [environmental sequence]EAJ39929unknown [environmental sequence]EAJ54356unknown [environmental sequence]EAJ54959unknown [environmental sequence]EAJ56207unknown [environmental sequence]EAJ58447unknown [environmental sequence]EAJ59958unknown [environmental sequence]EAJ63347unknown [environmental sequence]EAJ66054unknown [environmental sequence]EAJ67637unknown [environmental sequence]EAJ69812unknown [environmental sequence]EAJ74441unknown [environmental sequence]EAJ76472unknown [environmental sequence]EAJ76473unknown [environmental sequence]EAJ80355unknown [environmental sequence]EAJ80839unknown [environmental sequence]EAJ81408unknown [environmental sequence]EAJ86174unknown [environmental sequence]EAJ87600unknown [environmental sequence]EAJ88203unknown [environmental sequence]EAJ88682unknown [environmental sequence]EAJ92341unknown [environmental sequence]EAJ94774unknown [environmental sequence]EAJ97555unknown [environmental sequence]EAJ97958unknown [environmental sequence]EAK07654unknown [environmental sequence]EAK08513unknown [environmental sequence]EAK08529unknown [environmental sequence]EAK10609unknown [environmental sequence]EAK10614unknown [environmental sequence]EAK12902unknown [environmental sequence]EAK13034unknown [environmental sequence]EAK15092unknown [environmental sequence]EAK22483unknown [environmental sequence]EAK23222unknown [environmental sequence]EAK24187unknown [environmental sequence]EAK24674unknown [environmental sequence]EAK28785unknown [environmental sequence]EAK34731unknown [environmental sequence]EAK34742unknown [environmental sequence]EAK36883unknown [environmental sequence]EAK37522unknown [environmental sequence]EAK42705unknown [environmental sequence]EAK43213unknown [environmental sequence]EAK52580unknown [environmental sequence]EAK53452unknown [environmental sequence]EAK58759unknown [environmental sequence]EAK62665unknown [environmental sequence]EAK63558unknown [environmental sequence]F84187phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1F90272phytoene dehydrogenase related protein [imported] - Sulfolobus solfataricusG87635phytoene dehydrogenase-related protein [imported] - Caulobacter crescentusG90413phytoene dehydrogenase related protein [imported] - Sulfolobus solfataricusH83880hypothetical protein BH1848 [imported] - Bacillus halodurans (strain C-125)H84320phytoene dehydrogenase [imported] - Halobacterium sp. NRC-1JC7723phytoene desaturase (EC 1.14.99.—) 1 - citrusNP_060220all-trans-13,14-dihydroretinol saturase [ Homo sapiens ]NP_080435all-trans-13,14-dihydroretinol saturase [ Mus musculus ]NP_193157phytoene dehydrogenase, chloroplast/phytoene desaturase (PDS) [ Arabidopsisthaliana ]NP_214383protoporphyrinogen oxidase [ Aquifex aeolicus VF5]NP_276913phytoene dehydrogenase [ Methanothermobacter thermautotrophicus str. Delta H]NP_293819phytoene dehydrogenase, putative [ Deinococcus radiodurans R1]NP_294534dehydrogenase, putative [ Deinococcus radiodurans R1]NP_294585phytoene dehydrogenase [ Deinococcus radiodurans R1]NP_295972methoxyneurosporene dehydrogenase [ Deinococcus radiodurans R1]NP_338490oxidoreductase, putative [ Mycobacterium tuberculosis CDC1551]NP_376437hypothetical protein ST0549 [ Sulfolobus tokodaii str. 7]NP_377056hypothetical protein ST1130 [ Sulfolobus tokodaii str. 7]NP_388895protoporphyrinogen IX and coproporphyrinogen III oxidase [ Bacillus subtilis subsp.subtilis str. 168]NP_441167phytoene desaturase [ Synechocystis sp. PCC 6803]NP_441254hypothetical protein sll0254 [ Synechocystis sp. PCC 6803]NP_442491b-carotene ketolase [ Synechocystis sp. PCC 6803]NP_442727hypothetical protein sll0033 [ Synechocystis sp. PCC 6803]NP_562475probable diapophytoene dehydrogenase [ Clostridium perfringens str. 13]NP_568712amine oxidase-related [ Arabidopsis thaliana ]NP_601630hypothetical protein NCgl2346 [ Corynebacterium glutamicum ATCC 13032]NP_601630hypothetical protein NCgl2346 [ Corynebacterium glutamicum ATCC 13032]NP_616426phytoene dehydrogenase family protein [ Methanosarcina acetivorans C2A]NP_624522putative phytoene dehydrogenase (phytoene desaturase) (putative secreted protein)[ Streptomyces coelicolor A3(2)]NP_626360putative carotenoid dehydrogenase (putative secreted protein) [ Streptomycescoelicolor A3(2)]NP_630834putative phytoene dehydrogenase [ Streptomyces coelicolor A3(2)]NP_643053phytoene dehydrogenase [ Xanthomonas axonopodis pv. citri str. 306]NP_647302hypothetical protein MW2485 [ Staphylococcus aureus subsp. aureus MW2]NP_659552all-trans-13,14-dihydroretinol saturase [ Rattus norvegicus ]NP_661086lycopene cyclase, putative [ Chlorobium tepidum TLS]NP_661546carotenoid isomerase, putative [ Chlorobium tepidum TLS]NP_661701phytoene desaturase [ Chlorobium tepidum TLS]NP_662300zeta-carotene desaturase [ Chlorobium tepidum TLS]NP_681023putative phytoene dehydrogenase [ Thermosynechococcus elongatus BP-1]NP_681127zeta-carotene desaturase [ Thermosynechococcus elongatus BP-1]NP_682351phytoene dehydrogenase/phytoene desaturase [ Thermosynechococcus elongatusBP-1]NP_693380phytoene dehydrogenase [ Oceanobacillus iheyensis HTE831]NP_693382phytoene dehydrogenase [ Oceanobacillus iheyensis HTE831]NP_737250phytoene desaturase [ Corynebacterium efficiens YS-314]NP_763380hypothetical protein VV21505 [ Vibrio vulnificus CMCP6]NP_786524squalene synthase [ Lactobacillus plantarum WCFS1]NP_822198phytoene desaturase [ Streptomyces avermitilis MA-4680]NP_822828squalene/phytoene dehydrogenase [ Streptomyces avermitilis MA-4680]NP_827278putative phytoene dehydrogenase [ Streptomyces avermitilis MA-4680]NP_851528putative phytoene dehydrogenase [ Streptomyces rochei ]NP_857496PUTATIVE DEHYDROGENASE [ Mycobacterium bovis AF2122/97]NP_868798probable phytoene dehydrogenase [ Rhodopirellula baltica SH 1]NP_869339phytoene dehydrogenase [ Rhodopirellula baltica SH 1]NP_870237phytoene dehydrogenase [ Rhodopirellula baltica SH 1]NP_874530Zeta-carotene desaturase [ Prochlorococcus marinus subsp. marinus str. CCMP1375]NP_874561Phytoene dehydrogenase, phytoene desaturase [ Prochlorococcus marinus subsp.marinus str. CCMP1375]NP_874977Phytoene dehydrogenase/carotenoid isomerase [ Prochlorococcus marinus subsp.marinus str. CCMP1375]NP_892236zeta-carotene desaturase [ Prochlorococcus marinus subsp. pastoris str. CCMP1986]NP_892265phytoene desaturase [ Prochlorococcus marinus subsp. pastoris str. CCMP1986]NP_892458Bacterial-type phytoene dehydrogenase [ Prochlorococcus marinus subsp. pastorisstr. CCMP1986]NP_893232putative carotenoid isomerase [ Prochlorococcus marinus subsp. pastoris str.CCMP1986]NP_894882putative carotenoid isomerase [ Prochlorococcus marinus str. MIT 9313]NP_895385NAD binding site [ Prochlorococcus marinus str. MIT 9313]NP_895793zeta-carotene desaturase [ Prochlorococcus marinus str. MIT 9313]NP_895829phytoene desaturase [ Prochlorococcus marinus str. MIT 9313]NP_896854hypothetical protein SYNW0761 [ Synechococcus sp. WH 8102]NP_896994Carotenoid isomerase [ Synechococcus sp. WH 8102]NP_898304zeta-carotene desaturase [ Synechococcus sp. WH 8102]NP_898346phytoene desaturase [ Synechococcus sp. WH 8102]NP_902647hypothetical protein CV2977 [ Chromobacterium violaceum ATCC 12472]NP_923340beta-carotene ketolase [ Gloeobacter violaceus PCC 7421]NP_923639hypothetical protein gll0693 [ Gloeobacter violaceus PCC 7421]NP_923813phytoene dehydrogenase [ Gloeobacter violaceus PCC 7421]NP_925079hypothetical protein gvip293 [ Gloeobacter violaceus PCC 7421]NP_931515phytoene dehydrogenase (phytoene desaturase) [ Photorhabdus luminescens subsp.laumondii TTO1]NP_936379hypothetical protein VVA0323 [ Vibrio vulnificus YJ016]NP_940208phytoene dehydrogenase related enzyme [ Corynebacterium diphtheriae NCTC13129]NP_945754NAD binding site:Amine oxidase [ Rhodopseudomonas palustris CGA009]NP_946860phytoene dehydrogenase CrtI [ Rhodopseudomonas palustris CGA009]NP_946866methoxyneurosporene dehydrogenase [ Rhodopseudomonas palustris CGA009]NP_948851phytoene dehydrogenase-related protein [ Rhodopseudomonas palustris CGA009]NP_962004hypothetical protein MAP3070 [ Mycobacterium avium subsp. paratuberculosis str.k10]NP_968600Phytoene dehydrogenase [ Bdellovibrio bacteriovorus HD100]NP_974222zeta-carotene desaturase (ZDS1)/carotene 7,8-desaturase [ Arabidopsis thaliana ]NP_974545phytoene dehydrogenase, chloroplast/phytoene desaturase (PDS) [ Arabidopsisthaliana ]O49901Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)P17059Methoxyneurosporene dehydrogenaseP54971Phytoene dehydrogenase (Phytoene desaturase)P54978Phytoene dehydrogenase (Phytoene desaturase)P54979Phytoene dehydrogenase (Phytoene desaturase)P54981Phytoene dehydrogenase (Phytoene desaturase)P54982Phytoene dehydrogenase (Phytoene desaturase)P74306Zeta-carotene desaturase (Carotene 7,8-desaturase)Q01671Methoxyneurosporene dehydrogenaseQ02861Phytoene dehydrogenase (Phytoene desaturase)Q38893Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)Q40406Phytoene dehydrogenase, chloroplast precursor (Phytoene desaturase)Q9FV46Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)Q9SE20Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)Q9SMJ3Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)Q9ZTN9Phytoene dehydrogenase, chloroplast precursor (Phytoene desaturase)Q9ZTP4Zeta-carotene desaturase, chloroplast precursor (Carotene 7,8-desaturase)S29314phytoene dehydrogenase (EC 1.3.—.—) - pepperS32171hydroxyneurosporene dehydrogenase (EC 1.3.—.—) - Myxococcus xanthusS49624methoxyneurosporene dehydrogenase (EC 1.3.—.—) CrtD - Rhodobacter sphaeroidesS52586phytoene dehydrogenase (EC 1.3.—.—) - Erwinia herbicolaS65060phytoene desaturase precursor - maizeT10701probable phytoene dehydrogenase (EC 1.3.—.—) - green alga ( Dunaliella bardawil )T31463probable diapophytoene dehydrogenase crtN - Heliobacillus mobilisT46822phytoene desaturase (EC 1.3.—.—) [validated] - Xanthophyllomyces dendrorhousT48646phytoene dehydrogenase (EC 1.—.—.—) [validated] - Cercospora nicotianaeT50745phytoene dehydrogenase (EC 1.3.—.—) [imported] - Rhodobacter sphaeroidesT50749methoxyneurosporene dehydrogenase (EC 1.3.—.—) crtD [imported] - RhodobactersphaeroidesT50893methoxyneurosporene dehydrogenase [imported] - Rubrivivax gelatinosusT50910phytoene dehydrogenase [imported] - Rubrivivax gelatinosusT51119phytoene desaturase crtI [imported] - Brevibacterium linensT51123betacarotene desaturase [imported] - Brevibacterium linensXP_324732PHYTOENE DEHYDROGENASE (PHYTOENE DESATURASE) (ALBINO-1PROTEIN) [ Neurospora crassa ]XP_383241hypothetical protein FG03065.1 [ Gibberella zeae PH-1]XP_401825hypothetical protein UM04210.1 [ Ustilago maydis 521]XP_470568Putative phytoene dehydrogenase precursor [ Oryza sativa ]XP_473486OSJNBa0084K11.8 [ Oryza sativa ( japonica cultivar-group)]XP_477063putative zeta-carotene desaturase precursor [ Oryza sativa ( japonica cultivar-group)]XP_525801PREDICTED: hypothetical protein XP_525801 [ Pan troglodytes ]XP_540198PREDICTED: hypothetical protein XP_540198 [ Canis familiaris ]YP_006049phytoene dehydrogenase [ Thermus thermophilus HB27]YP_013621phytoene dehydrogenase, putative [ Listeria monocytogenes str. 4b F2365]YP_024310phytoene dehydrogenase [ Picrophilus torridus DSM 9790]YP_041986squalene synthase [ Staphylococcus aureus subsp. aureus MRSA252]YP_041988putative phytoene dehydrogenase related protein [ Staphylococcus aureus subsp.aureus MRSA252]YP_044561squalene synthase [ Staphylococcus aureus subsp. aureus MSSA476]YP_044564putative phytoene dehydrogenase related protein [ Staphylococcus aureus subsp.aureus MSSA476]YP_062471phytoene dehydrogenase [ Leifsonia xyli subsp. xyli str. CTCB07]YP_117947putative phytoene desaturase [ Nocardia farcinica IFM 10152]YP_120612putative phytoene desaturase [ Nocardia farcinica IFM 10152]YP_135077phytoene dehydrogenase [ Haloarcula marismortui ATCC 43049]YP_136483phytoene dehydrogenase [ Haloarcula marismortui ATCC 43049]YP_145331probable phytoene dehydrogenase [ Thermus thermophilus HB8]YP_145348phytoene dehydrogenase [ Thermus thermophilus HB8]YP_171014carotene isomerase [ Synechococcus elongatus PCC 6301]YP_172823phytoene dehydrogenase [ Synechococcus elongatus PCC 6301]YP_173078carotene isomerase [ Synechococcus elongatus PCC 6301]YP_173207zeta-carotene desaturase [ Synechococcus elongatus PCC 6301]YP_184572predicted oxidoreductase [ Thermococcus kodakaraensis ]YP_187368dehydrosqualene desaturase [ Staphylococcus aureus subsp. aureus COL]YP_187371phytoene dehydrogenase [ Staphylococcus aureus subsp. aureus COL]YP_187371phytoene dehydrogenase [ Staphylococcus aureus subsp. aureus COL]YP_187371phytoene dehydrogenase [ Staphylococcus aureus subsp. aureus COL]ZP_000490COG1233: Phytoene dehydrogenase and related proteins [ Magnetospirillummagnetotacticum MS-1]ZP_000509COG1233: Phytoene dehydrogenase and related proteins [ Magnetospirillummagnetotacticum MS-1]ZP_000518COG1233: Phytoene dehydrogenase and related proteins [ Magnetospirillummagnetotacticum MS-1]ZP_000566COG0562: UDP-galactopyranose mutase [ Magnetospirillum magnetotacticum MS-1]ZP_000627COG1233: Phytoene dehydrogenase and related proteins [ Leuconostocmesenteroides subsp. mesenteroides ATCC 8293]ZP_000627COG1233: Phytoene dehydrogenase and related proteins [ Leuconostocmesenteroides subsp. mesenteroides ATCC 8293]ZP_001073COG1233: Phytoene dehydrogenase and related proteins [ Nostoc punctiforme PCC73102]ZP_001081COG1233: Phytoene dehydrogenase and related proteins [ Nostoc punctiforme PCC73102]ZP_001091COG3349: Uncharacterized conserved protein [ Nostoc punctiforme PCC 73102]ZP_001116COG1233: Phytoene dehydrogenase and related proteins [ Nostoc punctiforme PCC73102]ZP_001117COG3349: Uncharacterized conserved protein [ Nostoc punctiforme PCC 73102]ZP_001119COG3349: Uncharacterized conserved protein [ Nostoc punctiforme PCC 73102]ZP_001124COG1233: Phytoene dehydrogenase and related proteins [ Nostoc punctiforme PCC73102]ZP_001510COG1233: Phytoene dehydrogenase and related proteins [ Dechloromonas aromaticaRCB]ZP_001591COG3349: Uncharacterized conserved protein [ Anabaena variabilis ATCC 29413]ZP_001593COG1233: Phytoene dehydrogenase and related proteins [ Anabaena variabilisATCC 29413]ZP_001602COG3349: Uncharacterized conserved protein [ Anabaena variabilis ATCC 29413]ZP_001614COG3349: Uncharacterized conserved protein [ Anabaena variabilis ATCC 29413]ZP_001645COG3349: Uncharacterized conserved protein [ Synechococcus elongatus PCC 7942]ZP_001650COG3349: Uncharacterized conserved protein [ Synechococcus elongatus PCC 7942]ZP_001722COG1233: Phytoene dehydrogenase and related proteins [ Methylobacillusflagellatus KT]ZP_001746COG3349: Uncharacterized conserved protein [ Crocosphaera watsonii WH 8501]ZP_001752COG3349: Uncharacterized conserved protein [ Crocosphaera watsonii WH 8501]ZP_001770COG1232: Protoporphyrinogen oxidase [ Crocosphaera watsonii WH 8501]ZP_001777COG1233: Phytoene dehydrogenase and related proteins [ Crocosphaera watsoniiWH 8501]ZP_001787COG3349: Uncharacterized conserved protein [ Crocosphaera watsonii WH 8501]ZP_001837COG1233: Phytoene dehydrogenase and related proteins [ Exiguobacterium sp. 255-15]ZP_001867COG1233: Phytoene dehydrogenase and related proteins [ Rubrobacter xylanophilusDSM 9941]ZP_002073COG1233: Phytoene dehydrogenase and related proteins [ Rhodobacter sphaeroides2.4.1]ZP_002077COG1233: Phytoene dehydrogenase and related proteins [ Rhodobacter sphaeroides2.4.1]ZP_002339phytoene dehydrogenase, putative [ Listeria monocytogenes str. ½a F6854]ZP_002680COG1233: Phytoene dehydrogenase and related proteins [ Rhodospirillum rubrum ]ZP_002705COG1233: Phytoene dehydrogenase and related proteins [ Rhodospirillum rubrum ]ZP_002771COG1232: Protoporphyrinogen oxidase [ Burkholderia fungorum LB400]ZP_002892hypothetical protein Mmc102002317 [ Magnetococcus sp. MC-1]ZP_002916COG3349: Uncharacterized conserved protein [ Thermobifida fusca ]ZP_002963COG1233: Phytoene dehydrogenase and related proteins [ Methanosarcina barkeristr. fusaro]ZP_003022COG1233: Phytoene dehydrogenase and related proteins [ Novosphingobiumaromaticivorans DSM 12444]ZP_003036COG1233: Phytoene dehydrogenase and related proteins [ Novosphingobiumaromaticivorans DSM 12444]ZP_003107COG1233: Phytoene dehydrogenase and related proteins [ Cytophaga hutchinsonii ]ZP_003202COG1233: Phytoene dehydrogenase and related proteins [ Oenococcus oeni PSU-1]ZP_003258COG1233: Phytoene dehydrogenase and related proteins [ Trichodesmiumerythraeum IMS101]ZP_003268COG3349: Uncharacterized conserved protein [ Trichodesmium erythraeum IMS101]ZP_003269COG3349: Uncharacterized conserved protein [ Trichodesmium erythraeum IMS101]ZP_003276COG1233: Phytoene dehydrogenase and related proteins [ Trichodesmiumerythraeum IMS101]ZP_003283COG1233: Phytoene dehydrogenase and related proteins [ Trichodesmiumerythraeum IMS101]ZP_003557COG1233: Phytoene dehydrogenase and related proteins [ Exiguobacterium sp. 255-15]ZP_003559COG3349: Uncharacterized conserved protein [ Chloroflexus aurantiacus ]ZP_003565COG1233: Phytoene dehydrogenase and related proteins [ Chloroflexus aurantiacus ]ZP_003577COG1233: Phytoene dehydrogenase and related proteins [ Chloroflexus aurantiacus ]ZP_003593COG1233: Phytoene dehydrogenase and related proteins [ Chloroflexus aurantiacus ]ZP_003595COG1233: Phytoene dehydrogenase and related proteins [ Chloroflexus aurantiacus ]ZP_003685carotenoid isomerase, putative [ Campylobacter lari RM2100] TABLE 17bExamples of phytoene dehydrogenase polypeptides.RowAccessionGIProtein Description11613414B227039crtI gene2CAA3653345998unnamed protein product [ Rhodobacter capsulatus ]3ABP69925145555312Phytoene dehydrogenase-related protein [ Rhodobacter sphaeroidesATCC 17025]4ABG29855109453650phytoene dehydrogenase [ Roseobacter denitrificans OCh 114]5YP_001 . . .126462676Phytoene dehydrogenase-related protein [ Rhodobacter sphaeroidesATCC 17029]6CAB387394490589phytoene dehydrogenase [ Rhodobacter sphaeroides ]7AAF242896690721CrtI [ Rhodobacter sphaeroides ]8ZP_019 . . .149914257Phytoene dehydrogenase [ Roseobacter sp. AzwK-3b]9ZP_018 . . .149203764Phytoene dehydrogenase [ Roseovarius sp. TM1035]10ZP_017 . . .126734359Phytoene dehydrogenase [ Roseobacter sp. CCS2]11ZP_015 . . .118735466Phytoene dehydrogenase-related protein [ Dinoroseobacter shibaeDFL 12]12EBA75398134340305hypothetical protein GOS_348183 [marine metagenome]13ZP_010 . . .85703533Phytoene dehydrogenase [ Roseovarius sp. 217]14ZP_010 . . .84514966Phytoene dehydrogenase [ Loktanella vestfoldensis SKA53]15EDJ26541144155062hypothetical protein GOS_1726264 [marine metagenome]16AAM4864621328640phytoene dehydrogenase [uncultured proteobacterium]17EBF29285135068871hypothetical protein GOS_9621672 [marine metagenome]18EDH88525143962357hypothetical protein GOS_524801 [marine metagenome]19ABD5306088862183phytoene dehydrogenase [ Jannaschia sp. CCS1]20ECX23858142320992hypothetical protein GOS_2574166 [marine metagenome]21EDD83467143241615hypothetical protein GOS_1236491 [marine metagenome]22ECW60413142235101hypothetical protein GOS_2690740 [marine metagenome]23EDB24382142880994hypothetical protein GOS_1857800 [marine metagenome]24EDC65629143078396hypothetical protein GOS_1437717 [marine metagenome]25EDC66763143079940hypothetical protein GOS_1435710 [marine metagenome]26EBF73535135137918hypothetical protein GOS_9549173 [marine metagenome]27EDB61897142933299hypothetical protein GOS_1624464 [marine metagenome]28EDH58399143920581hypothetical protein GOS_579274 [marine metagenome]29ECV46406142084909hypothetical protein GOS_2893885 [marine metagenome]30EBG03643135184853hypothetical protein GOS_9500102 [marine metagenome]31ECW11301142170256hypothetical protein GOS_2778421 [marine metagenome]32EDG30167143690631hypothetical protein GOS_805431 [marine metagenome]33EBF89344135162533hypothetical protein GOS_9523433 [marine metagenome]34EDG14791143664156hypothetical protein GOS_832322 [marine metagenome]35ECW44302142213461hypothetical protein GOS_2720548 [marine metagenome]36EDC28179143027347hypothetical protein GOS_1503868 [marine metagenome]37EBF91518135165888hypothetical protein GOS_9519783 [marine metagenome]38EBG06098135188689hypothetical protein GOS_9496261 [marine metagenome]39YP_001 . . .121998398Phytoene dehydrogenase-related protein [ Halorhodospirahalophila SL1]40ABC2129883574747Phytoene desaturase [ Rhodospirillum rubrum ATCC 11170]41EDD45555143188703hypothetical protein GOS_1301547 [marine metagenome]42EBF89879135163364hypothetical protein GOS_9522488 [marine metagenome]43EDA94958142836512hypothetical protein GOS_1907603 [marine metagenome]44EBE40240134934911hypothetical protein GOS_9769793 [marine metagenome]45ABQ38355146409849Phytoene dehydrogenase (Phytoene desaturase) [ Bradyrhizobiumsp. BTAi1]46ECV53668142093711hypothetical protein GOS_2880588 [marine metagenome]47EDJ05722144126667hypothetical protein GOS_1762374 [marine metagenome]48EDJ52003144189327hypothetical protein GOS_1681048 [marine metagenome]49CAL75489146191484Phytoene dehydrogenase (Phytoene desaturase) [ Bradyrhizobiumsp. ORS278]50ZP_011 . . .88706670phytoene dehydrogenase [gamma proteobacterium KT 71]51ABD8682390104786amine oxidase [ Rhodopseudomonas palustris BisB18]52ZP_019 . . .149922641amine oxidase [ Plesiocystis pacifica SIR-1]53ECW14126142173943hypothetical protein GOS_2773516 [marine metagenome]54ABJ05267115517283amine oxidase [ Rhodopseudomonas palustris BisA53]55ZP_020 . . .156449192Zeta-phytoene desaturase [ Methylobacterium chloromethanicumCM4]56ZP_020 . . .153900167FAD-dependent pyridine nucleotide-disulphide oxidoreductase[ Methylobacterium extorquens PA1]57EDO75157157409160Zeta-phytoene desaturase [ Methylobacterium populi BJ001]58EBF26787135064945hypothetical protein GOS_9625603 [marine metagenome]59EBM47492136188235hypothetical protein GOS_8404015 [marine metagenome]60BAA940637416814phytoene dehydrogenase [ Rubrivivax gelatinosus ]61AAO9313529893506phytoene dehydrogenase; CrtI [ Rubrivivax gelatinosus ]62ABE4098791684685amine oxidase [ Rhodopseudomonas palustris BisB5]63ABC4446783756354phytoene dehydrogenase [ Salinibacter ruber DSM 13855]64NP_94686039934584phytoene dehydrogenase CrtI [ Rhodopseudomonas palustrisCGA009]65EDK95498148522573Phytoene dehydrogenase-related protein [ Methylobacterium sp. 4-46]66AAX4818961653236phytoene dehydrogenase [uncultured proteobacteriumDelRiverFos06H03]67ABD0870486574147Amine oxidase [ Rhodopseudomonas palustris HaA2]68ECV97125142151708hypothetical protein GOS_2803067 [marine metagenome]69EBF91320135165576hypothetical protein GOS_9520100 [marine metagenome]70EDG74671143780072hypothetical protein GOS_728533 [marine metagenome]71AAR3780240062931phytoene dehydrogenase [uncultured bacterium 442]72ZP_016 . . .119504131amine oxidase [marine gamma proteobacterium HTCC2080]73EBY63975138260458hypothetical protein GOS_5033312 [marine metagenome]74ECW52975142225047hypothetical protein GOS_2704529 [marine metagenome]75EDB07926142858428hypothetical protein GOS_1885673 [marine metagenome]76ECX08477142300457hypothetical protein GOS_2602107 [marine metagenome]77EBE08763134887517hypothetical protein GOS_9823078 [marine metagenome]78EDG53739143740094hypothetical protein GOS_764800 [marine metagenome]79AAR3785540062985phytoene dehydrogenase [uncultured bacterium 443]80EBE55393134957668hypothetical protein GOS_9744377 [marine metagenome]81EBK49247135888345hypothetical protein GOS_8723699 [marine metagenome]82YP_001 . . .154247504Zeta-phytoene desaturase [ Xanthobacter autotrophicus Py2]83EBJ38620135714057hypothetical protein GOS_8907038 [marine metagenome]84EBO29607136458570hypothetical protein GOS_8104065 [marine metagenome]85EDI63495144067673hypothetical protein GOS_399405 [marine metagenome]86ECH51213139794606hypothetical protein GOS_4963038 [marine metagenome]87ZP_014 . . .113941052amine oxidase [ Herpetosiphon aurantiacus ATCC 23779]88P5497885700409Phytoene dehydrogenase (Phytoene desaturase)89AAY2842063034218phytoene desaturase [ Paracoccus haeundaensis ]90YP_001 . . .148655097Phytoene dehydrogenase-related protein [ Roseiflexus sp. RS-1]91AAT3522247531118fusion of carotene synthesis proteins [synthetic construct]92CAB560625912295phytoene desaturase [ Paracoccus marcusii ]93ZP_016 . . .119484684phytoene dehydrogenase CrtI [ Lyngbya sp. PCC 8106]94YP_001 . . .156932562hypothetical protein ESA_00343 [ Enterobacter sakazakii ATCCBAA-894]95CAL34121112702901phytoene dehydrogenase CRTI [ Enterobacter sakazakii ]96ZP_014 . . .114705593phytoene dehydrogenase (phytoene desaturase) [ Fulvimarinapelagi HTCC2506]97ABU57678156232895Zeta-phytoene desaturase [ Roseiflexus castenholzii DSM 13941]98EDJ24172144151864hypothetical protein GOS_1730347 [marine metagenome]99EBP04886136575764hypothetical protein GOS_7976019 [marine metagenome]100EDJ19941144146057hypothetical protein GOS_1737754 [marine metagenome]101EDE02809143268695hypothetical protein GOS_1202430 [marine metagenome]102EDA02972142711842hypothetical protein GOS_2076612 [marine metagenome]103AAC448501842244phytoene desaturase104ECI48880139936452hypothetical protein GOS_4592564 [marine metagenome]105ECW29436142194003hypothetical protein GOS_2746710 [marine metagenome]106CAE7959339575425Phytoene dehydrogenase [ Bdellovibrio bacteriovorus HD100]107EDJ16294144141089hypothetical protein GOS_1744028 [marine metagenome]108ABC5011484043362phytoene desaturase [ Brevundimonas vesicularis ]109CAE1671436787607phytoene dehydrogenase (phytoene desaturase) [ Photorhabdusluminescens subsp. laumondii TTO1]110AAZ7314272536076phytoene desaturase [ Enterobacteriaceae bacterium DC416]111ECC15254138850366hypothetical protein GOS_5005338 [marine metagenome]112EBF96527135173721hypothetical protein GOS_9511771 [marine metagenome]113AAZ7313072536062phytoene desaturase [ Enterobacteriaceae bacterium DC260]114AAW7281492430259CrtI [ Pantoea sp. C1B1Y]115EBF63722135122709hypothetical protein GOS_9565260 [marine metagenome]116EDJ33653144164568hypothetical protein GOS_1713484 [marine metagenome]117BAB7960318143448crtI [ Pantoea agglomerans pv. milletiae ]118AAZ7313672536069phytoene desaturase [ Enterobacteriaceae bacterium DC404]119ABD7328189475493phytoene dehydrogenase [ Pantoea agglomerans ]120AAF782018650417phytoene desaturase [ Bradyrhizobium sp. ORS278]121ZP_010 . . .84704558phytoene dehydrogenase (phytoene desaturase) [ Parvularculabermudensis HTCC2503]122EBF30985135071529hypothetical protein GOS_9618780 [marine metagenome]123EDJ11107144133947hypothetical protein GOS_1752989 [marine metagenome]124YP_001 . . .146284185phytoene desaturase [ Pseudomonas stutzeri A1501]125EDB39933142902995hypothetical protein GOS_1830750 [marine metagenome]126ZP_013 . . .94496006amine oxidase [ Sphingomonas sp. SKA58]127P22871117514Phytoene dehydrogenase (Phytoene desaturase)128ECD12151139058277hypothetical protein GOS_4688757 [marine metagenome]129AAA64981551855phytoene dehydrogenase [ Pantoea agglomerans ]130ECS36705141558903hypothetical protein GOS_4990354 [marine metagenome]131ECJ26724140055135hypothetical protein GOS_5004115 [marine metagenome]132ECY06051142435846hypothetical protein GOS_2424849 [marine metagenome]133ZP_007 . . .76261240Amine oxidase: FAD dependent oxidoreductase [ Chloroflexusaurantiacus J-10-fl]134BAD9940867003497phytoene desaturase [ Brevundimonas sp. SD212]135ZP_015 . . .118048084amine oxidase [ Chloroflexus aggregans DSM 9485]136EAS4980190336053phytoene dehydrogenase [ Aurantimonas sp. SI85-9A1]137EDF88410143616932hypothetical protein GOS_877736 [marine metagenome]138AAN8559927228293Phytoene Desaturase [ Pantoea stewartii ]139EDI65706144070706hypothetical protein GOS_395761 [marine metagenome]140AAA21263148397phytoene dehydrogenase [ Pantoea agglomerans ]141P21685117515Phytoene dehydrogenase (Phytoene desaturase)142AAZ7314972536084phytoene desaturase [ Enterobacteriaceae bacterium DC413]143ZP_016 . . .119476622phytoene dehydrogenase [marine gamma proteobacteriumHTCC2143]144ABL97778119713729crtI phytoene dehydrogenase [uncultured marine bacteriumHF10_29C11]145ABL97829119713781crtI/crtB [uncultured marine bacterium HF10_49E08]146EDB02259142846369hypothetical protein GOS_1894993 [marine metagenome]147ECQ63324141245988hypothetical protein GOS_4882732 [marine metagenome]148EAS4819590333025phytoene dehydrogenase [marine gamma proteobacteriumHTCC2207]149EAU13549113732481Amine oxidase: FAD dependent oxidoreductase [ Caulobacter sp.K31]150ECV72481142118377hypothetical protein GOS_2846587 [marine metagenome]151ECZ41342142625145hypothetical protein GOS_2188322 [marine metagenome]152EDF61582143556399hypothetical protein GOS_924048 [marine metagenome]153EBN79105136382241hypothetical protein GOS_8187951 [marine metagenome]154YP_001 . . .156974447hypothetical protein VIBHAR_02162 [ Vibrio harveyi ATCCBAA-1116]155BAA202762130971phytoene desaturase [ Erythrobacter longus ]156EBC81369134685202hypothetical protein GOS_10270 [marine metagenome]157ECS97023141726243hypothetical protein GOS_8923124 [marine metagenome]158ECY38926142480300hypothetical protein GOS_2368541 [marine metagenome]159YP_632230108758926putative phytoene dehydrogenase [ Myxococcus xanthus DK 1622]160EDB72930142948834hypothetical protein GOS_1603748 [marine metagenome]161EDJ54243144192357hypothetical protein GOS_1677113 [marine metagenome]162EAR5513089049570phytoene dehydrogenase [ Photobacterium sp. SKA34]163EDF01226143447606hypothetical protein GOS_1030671 [marine metagenome]164EDD12651143142675hypothetical protein GOS_1354831 [marine metagenome]165EDI08258143990952hypothetical protein GOS_491661 [marine metagenome]166EDI22441144010457hypothetical protein GOS_467843 [marine metagenome]167ABF5483798978686amine oxidase [ Sphingopyxis alaskensis RB2256]168EBL74107136074962hypothetical protein GOS_8521797 [marine metagenome]169EBX98247138142760hypothetical protein GOS_6427327 [marine metagenome]170ECV76618142124100hypothetical protein GOS_2839194 [marine metagenome]171EBP18308136596794hypothetical protein GOS_7953009 [marine metagenome]172YP_26554771082828phytoene dehydrogenase [ Candidatus Pelagibacter ubiqueHTCC1062]173EAS8520191718551phytoene dehydrogenase [ Candidatus Pelagibacter ubiqueHTCC1002]174EDG91241143827295hypothetical protein GOS_699208 [marine metagenome]175ECV24805142059343hypothetical protein GOS_2935833 [marine metagenome]176AAY8731368164584predicted phytoene desaturase [uncultured bacterium BAC17H8]177EBD43768134788236hypothetical protein GOS_9929916 [marine metagenome]178EDG35515143701587hypothetical protein GOS_796054 [marine metagenome]179ZP_018 . . .149185744Phytoene dehydrogenase [ Erythrobacter sp. SD-21]180ABL60986119094156phytoene dehydrogenase CrtI [uncultured marine bacteriumHF10_19P19]181ECZ18273142592252hypothetical protein GOS_2227647 [marine metagenome]182ABD2625687135514amine oxidase [ Novosphingobium aromaticivorans DSM 12444]183EDG45712143723898hypothetical protein GOS_778645 [marine metagenome]184EBE76519134988930hypothetical protein GOS_9708797 [marine metagenome]185EDC75856143092398hypothetical protein GOS_1419598 [marine metagenome]186EDF35075143504771hypothetical protein GOS_970643 [marine metagenome]187ZP_014 . . .114771897phytoene dehydrogenase [alpha proteobacterium HTCC2255]188EDG12368143659594hypothetical protein GOS_836451 [marine metagenome]189AAT9032050952787putative phytoene dehydrogenase [uncultured proteobacteriumeBACred25D05]190EBV02567137608266hypothetical protein GOS_6968229 [marine metagenome]191ECB29435138684670hypothetical protein GOS_4941392 [marine metagenome]192EDI67354144073017hypothetical protein GOS_393156 [marine metagenome]193AAY7859467633343predicted phytoene dehydrogenase [uncultured bacteriumMedeBAC82F10]194ECY07797142438219hypothetical protein GOS_2421570 [marine metagenome]195EDI16519144002234hypothetical protein GOS_477455 [marine metagenome]196EDH58504143920724hypothetical protein GOS_579102 [marine metagenome]197EAU52387114549505phytoene dehydrogenase CrtI [alpha proteobacterium HTCC2255]198ECX42733142346738hypothetical protein GOS_2540243 [marine metagenome]199EBE06505134884139hypothetical protein GOS_9826927 [marine metagenome]200EDB92338142976670hypothetical protein GOS_1568269 [marine metagenome]201EBN30363136310418hypothetical protein GOS_8268666 [marine metagenome] TABLE 18Examples of phytoene synthase and lycopene cyclase polypeptides.AccessionGINumberNumberDescription1613414C227040crtB geneA495581076590phytoene synthase 2 precursor - tomato (fragment)AAA19428506623phytoene synthase [ Neurospora crassa ]AAA32836413732phytoene synthaseAAA64982148413phytoene synthase [ Pantoea agglomerans ]AAB8773829893495phytoene synthase [ Rubrivivax gelatinosus ]AAC448491842243phytoene synthaseAAD3805113542332phytoene synthase [ Citrus × paradisi ]AAF782028650418phytoene synthase [ Bradyrhizobium sp. ORS278]AAF826169081847phytoene synthase [ Tagetes erecta ]AAG104279971814phytoene synthase [ Tagetes erecta ]AAG2870111066678CrtB [ Streptomyces griseus ]AAK0773418476085phytoene synthase [ Oryza sativa ( japonica cultivar-group)]AAK0773518476089phytoene synthase [ Oryza sativa ( japonica cultivar-group)]AAK1562113195243phytoene synthase [ Haematococcus pluvialis ]AAL0200115553721phytoene synthase [ Xanthobacter sp. Py2]AAL7634618645045phytoene synthase [uncultured proteobacterium]AAL8257821326700phytoene synthase radicle isoform [ Oryza sativa ( indica cultivar-group)]AAM4537921360353phytoene synthase [ Tagetes erecta ]AAM4864721328641phytoene synthase [uncultured proteobacterium]AAM6278721553694phytoene synthase [ Arabidopsis thaliana ]AAM9436322296799phytoene synthase [ Agromyces mediolanus ]AAN8560027228294Phytoene Synthase [ Pantoea stewartii ]AAO2476727903500phytoene synthase [ Citrus maxima ]AAO3983528403302phytoene synthase [ Citrus sinensis ]AAO4689537729028lycopene cyclase/phytoene synthase [ Blakeslea trispora ]AAO4757033465823phytoene-beta carotene synthase [ Xanthophyllomyces dendrorhous ]AAO7381633465821crtYB [ Xanthophyllomyces dendrorhous ]AAP2203830349414phytoene synthase 2 [ Zea mays ]AAP5545132350232phytoene synthase 2 [ Zea mays ]AAP5545332350236phytoene synthase 2 [ Zea mays ]AAP5546132350252phytoene synthase 2 [ Zea mays ]AAP5547132350272phytoene synthase 2 [ Zea mays ]AAP5548432350298phytoene synthase 2 [ Zea mays ]AAP5548632350302phytoene synthase 2 [ Zea mays ]AAP5608332349564phytoene synthase [ Zea mays ]AAP5612432349646phytoene synthase [ Zea mays ]AAP5612732349652phytoene synthase [ Zea mays ]AAP5613632349670phytoene synthase [ Zea mays ]AAP5614832349694phytoene synthase [ Zea mays ]AAP5615532349708phytoene synthase [ Zea mays ]AAP5615632349710phytoene synthase [ Zea mays ]AAP5615732349712phytoene synthase [ Zea mays ]AAP5615832349714phytoene synthase [ Zea mays ]AAP7917632307542phytoene synthase [ Bigelowiella natans ]AAQ9183737499616phytoene synthase 2 [ Zea mays ]AAR0844538037628chloroplast phytoene synthase 1 [ Zea mays ]AAR3188539842609chloroplast phytoene synthase [ Zea mays ]AAR3780340062932phytoene synthase [uncultured bacterium 442]AAR3785640062986phytoene synthase [uncultured bacterium 443]AAR8610440456029phytoene synthase [ Momordica charantia var. abbreviata ]AAR8786840557193phytoene synthase [ Oncidium cv. ‘Gower Ramsey’]AAR9849241018901phytoene synthase [ Bradyrhizobium sp. ORS278]AAS0228441394357phytoene synthase 2 [ Zea mays ]AAS1700942491736phytoene synthase 2 [ Oryza sativa ( japonica cultivar-group)]AAS1830742521626phytoene synthase 1; PSY1 [ Oryza sativa ( indica cultivar-group)]AAT2818447498515phytoene synthase [ Dunaliella salina ]AAT3522247531118fusion of carotene synthesis proteins [synthetic construct]AAT3847347779181chloroplast phytoene synthase precursor [ Chlamydomonasreinhardtii ]AAT4606948686711phytoene synthase [ Dunaliella salina ]AAT7458150313418PSY [ Citrus sinensis ]AAT9031950952786putative phytoene synthase [uncultured proteobacteriumeBACred25D05]AAV7439456122551phytoene synthase [ Adonis palaestina ]AAW2316256698928phytoene synthase [ Rhodococcus erythropolis ]AC203525366683phytoene synthase [imported] - Nostoc sp. (strain PCC 7120)AC203525366683phytoene synthase [imported] - Nostoc sp. (strain PCC 7120)BAB1851411344507phytoene synthase [ Citrus unshiu ]BAB7960418143449crtB [ Pantoea agglomerans pv. milletiae ]BAD0727840809739phytoene synthase [ Citrus sinensis ]BAD0728640809755phytoene synthase [ Citrus limon ]BAD6210654291340phytoene synthase [ Oryza sativa ( japonica cultivar-group)]BAD6210754291341phytoene synthase-like [ Oryza sativa ( japonica cultivar-group)]C9006125506636squalene desaturase [imported] - Staphylococcus aureus (strainN315)CAA4762519347mutant phytoene synthase [ Lycopersicon esculentum ]CAA6857519341unnamed protein product [ Lycopersicon esculentum ]CAB079581934837unknown [ Bacillus subtilis ]CAB387404490590phytoene synthase [ Rhodobacter sphaeroides ]CAB519495690074phytoene-beta carotene synthase [ Xanthophyllomyces dendrorhous ]CAB560635912296phytoene synthase [ Paracoccus marcusii ]CAB863887453011phytoene synthase/lycopene cyclase [ Phycomyces blakesleeanus ]CAB936618250520lycopene cyclase/phytoene synthase [ Phycomyces blakesleeanus ]CAB947958574392phytoene synthase [ Mycobacterium aurum ]CAC1956711990226phytoene synthase [ Helianthus annuus ]CAC2738312584564phytoene synthase [ Helianthus annuus ]CAD1998818307500carotene cyclase [ Gibberella fujikuroi ]CAD2928457282088putative phytoene synthase [ Oryza sativa ]CAE7660938567321geranylgeranyl-diphosphate geranylgeranyltransferase (AL-2)[ Neurospora crassa ]E3780295606crtB protein - Erwinia uredovoraE8432025410251phytoene synthase [imported] - Halobacterium sp. NRC-1EAA9875842863045unknown [environmental sequence]EAB0196542869439unknown [environmental sequence]EAB0417042873822unknown [environmental sequence]EAB0713842879858unknown [environmental sequence]EAB0979142885235unknown [environmental sequence]EAB1982642905452unknown [environmental sequence]EAB3502942936011unknown [environmental sequence]EAB4137542948740unknown [environmental sequence]EAB7870643024004unknown [environmental sequence]EAB9258643052355unknown [environmental sequence]EAC0694943081493unknown [environmental sequence]EAC1836043104624unknown [environmental sequence]EAC2579343119723unknown [environmental sequence]EAC2988343128092unknown [environmental sequence]EAC3281343133973unknown [environmental sequence]EAC3310543134560unknown [environmental sequence]EAC3848643145552unknown [environmental sequence]EAC5223343173313unknown [environmental sequence]EAC6002943189028unknown [environmental sequence]EAC6802643204953unknown [environmental sequence]EAC9619743261031unknown [environmental sequence]EAD0870143285745unknown [environmental sequence]EAD2086643310220unknown [environmental sequence]EAD3275543334458unknown [environmental sequence]EAD3800843345761unknown [environmental sequence]EAD5015243370658unknown [environmental sequence]EAD5040243371147unknown [environmental sequence]EAD8112343452903unknown [environmental sequence]EAD9388243478303unknown [environmental sequence]EAE1286043516265unknown [environmental sequence]EAE1612143522884unknown [environmental sequence]EAE3108443552634unknown [environmental sequence]EAE3566543561764unknown [environmental sequence]EAE4471743579862unknown [environmental sequence]EAE4662743583580unknown [environmental sequence]EAE4784643586023unknown [environmental sequence]EAE7226443635190unknown [environmental sequence]EAE7600943642573unknown [environmental sequence]EAE8633543662748unknown [environmental sequence]EAE8958143669163unknown [environmental sequence]EAF1888143728007unknown [environmental sequence]EAF6427743819669unknown [environmental sequence]EAF6793143827263unknown [environmental sequence]EAF8474543861327unknown [environmental sequence]EAF9400443880040unknown [environmental sequence]EAG0608343903395unknown [environmental sequence]EAG2195043933540unknown [environmental sequence]EAG4362543973477unknown [environmental sequence]EAG5017143985555unknown [environmental sequence]EAG5751743999205unknown [environmental sequence]EAG6278744009110unknown [environmental sequence]EAG6558044014171unknown [environmental sequence]EAG6811044018715unknown [environmental sequence]EAG7228344026322unknown [environmental sequence]EAG7875044037938unknown [environmental sequence]EAG8044544041116unknown [environmental sequence]EAG9322044064453unknown [environmental sequence]EAH0492744085694unknown [environmental sequence]EAH0897244093217unknown [environmental sequence]EAH1037744095788unknown [environmental sequence]EAH2215144117864unknown [environmental sequence]EAH3146144134654unknown [environmental sequence]EAH5003344169323unknown [environmental sequence]EAH6448044196848unknown [environmental sequence]EAH7904044223009unknown [environmental sequence]EAH9997644255671unknown [environmental sequence]EAI0278644259828unknown [environmental sequence]EAI0278744259829unknown [environmental sequence]EAI0357544260943unknown [environmental sequence]EAI0590044264266unknown [environmental sequence]EAI6100444344824unknown [environmental sequence]EAI7066944358327unknown [environmental sequence]EAI8393844377067unknown [environmental sequence]EAJ0511044406802unknown [environmental sequence]EAJ0556944407471unknown [environmental sequence]EAJ0887644412338unknown [environmental sequence]EAJ3515644449986unknown [environmental sequence]EAJ3890044455130unknown [environmental sequence]EAJ4964544470504unknown [environmental sequence]EAJ5435744477026unknown [environmental sequence]EAJ6047544485647unknown [environmental sequence]EAJ6412544492007unknown [environmental sequence]EAJ6749944497025unknown [environmental sequence]EAJ7647144510405unknown [environmental sequence]EAJ7695044511114unknown [environmental sequence]EAJ7863744513596unknown [environmental sequence]EAJ7878744513824unknown [environmental sequence]EAJ7961644515082unknown [environmental sequence]EAJ8035644516200unknown [environmental sequence]EAJ8191444518489unknown [environmental sequence]EAJ8741744526623unknown [environmental sequence]EAK0851444557109unknown [environmental sequence]EAK0852344557119unknown [environmental sequence]EAK1290144563097unknown [environmental sequence]EAK2218044576315unknown [environmental sequence]EAK2485944580262unknown [environmental sequence]EAK2834544585276unknown [environmental sequence]EAK3473244594324unknown [environmental sequence]EAK3473644594329unknown [environmental sequence]EAK3729644597942unknown [environmental sequence]EAK3752144598256unknown [environmental sequence]EAK5633544624430unknown [environmental sequence]G8436325410528hypothetical protein ggt [imported] - Halobacterium sp. NRC-1NP_27419515677043phytoene synthase, putative [ Neisseria meningitidis MC58]NP_28408515794263poly-isoprenyl transferase [ Neisseria meningitidis Z2491]NP_29458615805888phytoene synthase [ Deinococcus radiodurans R1]NP_38896116078144hypothetical protein BSU10810 [ Bacillus subtilis subsp. subtilis str.168]NP_44116816330440phytoene synthase [ Synechocystis sp. PCC 6803]NP_44376316519643Y4aC [ Rhizobium sp. NGR234]NP_62452321218744putative phytoene synthase [ Streptomyces coelicolor A3(2)]NP_63083221225053putative phytoene synthase [ Streptomyces coelicolor A3(2)]NP_66227321674208phytoene desaturase [ Chlorobium tepidum TLS]NP_68235022299103phytoene synthase [ Thermosynechococcus elongatus BP-1]NP_69338123099915phytoene synthase [ Oceanobacillus iheyensis HTE831]NP_78652528379633phytoene synthase [ Lactobacillus plantarum WCFS1]NP_82219929827565phytoene synthase [ Streptomyces avermitilis MA-4680]NP_82282929828195squalene/phytoene synthase [ Streptomyces avermitilis MA-4680]NP_85152730795077putative phytoene synthase [ Streptomyces rochei ]NP_86879932475805probable phytoene synthase [ Rhodopirellula baltica SH 1]NP_87456033239618Phytoene synthase, CrtB [ Prochlorococcus marinus subsp. marinusstr. CCMP1375]NP_87999233592348putative phytoene synthase [ Bordetella pertussis Tohama I]NP_88410133596458putative phytoene synthase [ Bordetella parapertussis 12822]NP_88980933602249putative phytoene synthase [ Bordetella bronchiseptica RB50]NP_89226433860703Squalene and phytoene synthases [ Prochlorococcus marinus subsp.pastoris str. CCMP1986]NP_89582833864268Squalene and phytoene synthases [ Prochlorococcus marinus str. MIT9313]NP_89834533866786phytoene synthases [ Synechococcus sp. WH 8102]NP_90264834498433probable geranylgeranyl-diphosphate geranylgeranyltransferase[ Chromobacterium violaceum ATCC 12472NP_90264934498434probable phytoene synthase-related protein [ Chromobacteriumviolaceum ATCC 12472]NP_92469037521313phytoene synthase [ Gloeobacter violaceus PCC 7421]NP_93151637528171phytoene synthase [ Photorhabdus luminescens subsp. laumondiiTTO1]NP_94686139934585CrtB phytoene synthase [ Rhodopseudomonas palustris CGA009]NP_94907939936803putative poly-isoprenyl transferase [ Rhodopseudomonas palustrisCGA009]NP_96200541409169hypothetical protein MAP3071 [ Mycobacterium avium subsp.paratuberculosis str. k10]NP_96860142523221phytoene synthase [ Bdellovibrio bacteriovorus HD100]O073333913360Phytoene synthaseP08196585746Phytoene synthase 1, chloroplast precursor (Fruit ripening specificprotein pTOM5)P2168330923192Phytoene synthaseP37269585009Phytoene synthaseP3727127735222Phytoene synthase, chloroplast precursorP37272585749Phytoene synthase, chloroplast precursorP537971709885Phytoene synthase, chloroplast precursorP549751706137Phytoene synthaseP549771706139Phytoene synthaseP6586054041032Probable phytoene synthaseQ9SSU88928282Phytoene synthase, chloroplast precursorQ9UUQ634922667CarRP protein [Includes: Lycopene cyclase; Phytoene synthase]S224747489041phytoene synthase (EC 2.5.1.—) - tomatoS32170321671phytoene synthetase - Myxococcus xanthusS525871073300prephytoene pyrophosphate synthase - Erwinia herbicolaS566682129505geranylgeranyl-diphosphate geranylgeranyltransferase (EC 2.5.1.32)precursor - muskmelonS683072130144phytoene synthase - maizeT107027484346phytoene synthase (EC 2.5.1.—) - green alga ( Dunaliella bardawil )T4659411291807phytoene synthase (EC 2.5.1.—) [validated] - MycobacteriummarinumT5074611356347phytoene synthase (EC 2.5.1.—) [imported] - Rhodobacter sphaeroidesT5089511291816prephytoene pyrophosphate synthase [imported] - RubrivivaxgelatinosusXP_32476532408567PHYTOENE SYNTHASE [ Neurospora crassa ]XP_38324246114448hypothetical protein FG03066.1 [ Gibberella zeae PH-1]XP_40390249080862hypothetical protein UM06287.1 [ Ustilago maydis 521]YP_00604046255128phytoene synthase [ Thermus thermophilus HB27]YP_10312653723680phytoene synthase, putative [ Burkholderia mallei ATCC 23344]YP_11234253723357squalene/phytoene synthase [ Burkholderia pseudomallei K96243]YP_11794554023703putative phytoene synthase [ Nocardia farcinica IFM 10152]YP_12061154026369putative phytoene synthase [ Nocardia farcinica IFM 10152]YP_13662855378778lycopene cyclase [ Haloarcula marismortui ATCC 43049]YP_13662955378779phytoene synthase [ Haloarcula marismortui ATCC 43049]YP_14534055978284phytoene synthase [ Thermus thermophilus HB8]YP_14534355978287phytoene synthase-related protein [ Thermus thermophilus HB8]YP_16091756479328probable terpenoid synthase-related protein [ Azoarcus sp. EbN1]YP_16091856479329putative terpenoid synthase [ Azoarcus sp. EbN1]YP_16260556551766phytoene/squalene synthetase [ Zymomonas mobilis subsp. mobilisZM4]YP_17282256752121phytoene synthase [ Synechococcus elongatus PCC 6301]YP_18736957652299dehydrosqualene synthase [ Staphylococcus aureus subsp. aureusCOL]YP_19264858040684Putative phytoene synthase [ Gluconobacter oxydans 621H]ZP_00004422956752COG1562: Phytoene/squalene synthetase [ Rhodobacter sphaeroides2.4.1]ZP_00109153688068COG1562: Phytoene/squalene synthetase [ Nostoc punctiforme PCC73102]ZP_00159153763709COG1562: Phytoene/squalene synthetase [ Anabaena variabilis ATCC29413]ZP_00165745514234COG1562: Phytoene/squalene synthetase [ Ralstonia eutrophaJMP134]ZP_00169046132223COG1562: Phytoene/squalene synthetase [ Ralstonia eutrophaJMP134]ZP_00174645523280COG1562: Phytoene/squalene synthetase [ Crocosphaera watsoniiWH 8501]ZP_00183753771530COG1562: Phytoene/squalene synthetase [ Exiguobacterium sp. 255-15]ZP_00186745546711COG1562: Phytoene/squalene synthetase [ Rubrobacter xylanophilusDSM 9941]ZP_00209646204978COG1562: Phytoene/squalene synthetase [ Magnetospirillummagnetotacticum MS-1]ZP_00224846324513COG1562: Phytoene/squalene synthetase [ Burkholderia cepaciaR1808]ZP_00245047575031COG1562: Phytoene/squalene synthetase [ Rubrivivax gelatinosusPM1]ZP_00268048763469COG1562: Phytoene/squalene synthetase [ Rhodospirillum rubrum ]ZP_00271048766450COG1562: Phytoene/squalene synthetase [ Rhodospirillum rubrum ]ZP_00279148782680COG1562: Phytoene/squalene synthetase [ Burkholderia fungorumLB400]ZP_00289248832182COG1562: Phytoene/squalene synthetase [ Magnetococcus sp. MC-1]ZP_00291648834623COG1562: Phytoene/squalene synthetase [ Thermobifida fusca ]ZP_00303648849426COG1562: Phytoene/squalene synthetase [ Novosphingobiumaromaticivorans DSM 12444]ZP_00326948893702COG1562: Phytoene/squalene synthetase [ Trichodesmiumerythraeum IMS101]ZP_00335152007802COG1562: Phytoene/squalene synthetase [ Thiobacillus denitrificansATCC 25259]ZP_00348753730362COG1562: Phytoene/squalene synthetase [ Dechloromonas aromaticaRCB]ZP_00350153759405COG1562: Phytoene/squalene synthetase [ Methylobacillusflagellatus KT]ZP_00359153798896COG1562: Phytoene/squalene synthetase [ Chloroflexus aurantiacus ]ZP_00362854030691COG1562: Phytoene/squalene synthetase [ Polaromonas sp. JS666] TABLE 19Examples of carotenoid ketolase polypeptides.AccessionGINumberNumberDescriptionAAA99932609575fatty acid desaturaseAAB486681870215ORF [ Emericella nidulans ]AAC256112541936unknown [ Pseudomonas syringae ]AAF782038650419beta-carotene ketolase [ Bradyrhizobium sp. ORS278]AAH16427167411582210008A03Rik protein [ Mus musculus ]AAN0348422597194BKT [ Haematococcus pluvialis ]AAN8549726541510putative fatty acid desaturase [ Streptomyces atroolivaceus ]AAN8603033439708beta-carotene C4 oxygenase [ Brevundimonas aurantiaca ]AAO6439928976134putative beta-carotene ketolase [ Nodularia spumigena ]AAQ2313933621091CrtW/CrtY fusion protein [synthetic construct]AAT3522247531118fusion of carotene synthesis proteins [synthetic construct]AAT3555547558911beta-carotene ketolase [ Haematococcus pluvialis ]AAV4137255139370beta-carotene ketolase/oxygenase [‘ Chlorella ’ zofingiensis ]AB230725530134hypothetical protein alr4009 [imported] - Nostoc sp. (strain PCC7120)AF220425533132beta-carotene ketolase [imported] - Nostoc sp. (strain PCC 7120)BAB5499914028447mlr9395 [ Mesorhizobium loti MAFF303099]BAB5887914270087membrane fatty acid desaturase [ Toxoplasma gondii ]BAC9836637360914alkane hydroxylase [ Alcanivorax borkumensis ]CAA604782654318beta-carotene C-4 oxygenase (ketolase) [ Haematococcus pluvialis ]CAB560595912292beta-carotene C-4-oxygenase (ketolase) [ Paracoccus marcusii ]D8767325398945conserved hypothetical protein CC3422 [imported] - CaulobactercrescentusEAA7930442823978unknown [environmental sequence]EAA8036342826055unknown [environmental sequence]EAA8140342828115unknown [environmental sequence]EAA8471142834481unknown [environmental sequence]EAB8238043031476unknown [environmental sequence]EAB8662443040184unknown [environmental sequence]EAC0575543079085unknown [environmental sequence]EAD1221943292778unknown [environmental sequence]EAD7118243427899unknown [environmental sequence]EAD9492743480380unknown [environmental sequence]EAF1158243712986unknown [environmental sequence]EAF9807243888329unknown [environmental sequence]EAG1934543928738unknown [environmental sequence]EAG3827343963688unknown [environmental sequence]EAG7980044039853unknown [environmental sequence]EAG9647444070318unknown [environmental sequence]EAH0034944077315unknown [environmental sequence]EAH3644844143633unknown [environmental sequence]EAH4068344151265unknown [environmental sequence]EAH5318044175316unknown [environmental sequence]EAH9664844250729unknown [environmental sequence]EAI0526044263397unknown [environmental sequence]EAI1746844281329unknown [environmental sequence]EAI5300944333409unknown [environmental sequence]EAI5405444334878unknown [environmental sequence]EAI6781844354362unknown [environmental sequence]EAI6815344354875unknown [environmental sequence]EAI8968444384943unknown [environmental sequence]EAJ2767444439188unknown [environmental sequence]EAJ4558944464684unknown [environmental sequence]EAJ4558944464684unknown [environmental sequence]EAJ6711844496466unknown [environmental sequence]EAJ7422144507022unknown [environmental sequence]EAJ7465344507662unknown [environmental sequence]EAJ8839644528064unknown [environmental sequence]EAJ8888744528792unknown [environmental sequence]EAK0606944553531unknown [environmental sequence]EAK1146744561166unknown [environmental sequence]EAK1682444568733unknown [environmental sequence]EAK2882844585942unknown [environmental sequence]EAK2882844585942unknown [environmental sequence]EAK3111244589271unknown [environmental sequence]EAK4259144605441unknown [environmental sequence]NP_04506311465545fatty-acid desaturase [ Cyanidium caldarium ]NP_08157527754029sphingolipid delta 4 desaturase/C-4 hydroxylase [ Mus musculus ]NP_33820415843167fatty acid desaturase, putative/ferredoxin reductase, electron transfercomponent [ Mycobacterium tuberculosis CDC1551]NP_44078816330060b-carotene hydroxylase [ Synechocystis sp. PCC 6803]NP_44122016330492hypothetical protein sl11611 [ Synechocystis sp. PCC 6803]NP_68269022299443beta-carotene hydroxylase [ Thermosynechococcus elongatus BP-1]NP_77072127379192hypothetical protein blr4081 [ Bradyrhizobium japonicum USDA 110]NP_84896430468077beta-carotene hydroxylase [ Cyanidioschyzon merolae strain 10D]NP_85722331794730POSSIBLE ELECTRON TRANSFER PROTEIN FDXB[ Mycobacterium bovis AF2122/97]NP_88176033594116putative fatty acid desaturase [ Bordetella pertussis Tohama I]NP_88246933594826putative fatty acid desaturase [ Bordetella parapertussis 12822]NP_88665733599097putative fatty acid desaturase [ Bordetella bronchiseptica RB50]NP_89564333864083beta carotene hydroxylase [ Prochlorococcus marinus str. MIT 9313]NP_89638633864827beta-carotene hydroxylase [ Synechococcus sp. WH 8102]NP_89746133865902possible beta-carotene ketolase [ Synechococcus sp. WH 8102]NP_92467437521297beta-carotene ketolase [ Gloeobacter violaceus PCC 7421]NP_92752537524181hypothetical protein plu0159 [ Photorhabdus luminescens subsp.laumondii TTO1]NP_94707539934799Fatty acid desaturase family [ Rhodopseudomonas palustris CGA009]P549721706150Beta-carotene ketolase (Beta-carotene oxygenase)Q399822498257Beta-carotene ketolase (Beta-carotene oxygenase)Q442612498256Beta-carotene ketolase (Beta-carotene oxygenase)T3112311361063hypothetical protein 15 - Sphingomonas aromaticivorans plasmidpNL1XP_33078032420673hypothetical protein [ Neurospora crassa ]XP_36885239974923hypothetical protein MG00392.4 [ Magnaporthe grisea 70-15]XP_38019446102628hypothetical protein FG00018.1 [ Gibberella zeae PH-1]XP_38375846115480hypothetical protein FG03582.1 [ Gibberella zeae PH-1]XP_40510049086048hypothetical protein AN0963.2 [ Aspergillus nidulans FGSC A4]XP_40922249095522hypothetical protein AN5085.2 [ Aspergillus nidulans FGSC A4]YP_10241753725671alkane-1 monooxygenase [ Burkholderia mallei ATCC 23344]YP_10894553719959putative alkane monooxygenase [ Burkholderia pseudomallei K96243]YP_13241454302421hypothetical putative delta-9 fatty acid desaturase [ Photobacteriumprofundum SS9]YP_15467056459389Fatty-acid desaturase [ Idiomarina loihiensis L2TR]YP_16668256696325fatty acid desaturase family protein [ Silicibacter pomeroyi DSS-3]YP_16884656698471fatty acid desaturase family protein [ Silicibacter pomeroyi DSS-3]YP_17237756751676beta-carotene hydroxylase [ Synechococcus elongatus PCC 6301]ZP_00106823124870COG3239: Fatty acid desaturase [ Nostoc punctiforme PCC 73102]ZP_00111253688676COG3239: Fatty acid desaturase [ Nostoc punctiforme PCC 73102]ZP_00160753764743COG3239: Fatty acid desaturase [ Anabaena variabilis ATCC 29413]ZP_00175746118877COG3239: Fatty acid desaturase [ Crocosphaera watsonii WH 8501]ZP_00178753736018COG3239: Fatty acid desaturase [ Crocosphaera watsonii WH 8501]ZP_00221846321435COG3239: Fatty acid desaturase [ Burkholderia cepacia R1808]ZP_00245647575608COG3239: Fatty acid desaturase [ Rubrivivax gelatinosus PM1]ZP_00302848848557COG3239: Fatty acid desaturase [ Novosphingobium aromaticivoransDSM 12444]ZP_00310748856640COG3239: Fatty acid desaturase [ Cytophaga hutchinsonii ]ZP_00326448893204COG3239: Fatty acid desaturase [ Trichodesmium erythraeumIMS101]ZP_00345853688805hypothetical protein Npun02000865 [ Nostoc punctiforme PCC73102]ZP_00351353763576COG3239: Fatty acid desaturase [ Anabaena variabilis ATCC 29413] TABLE 20Examples of carotenoid hydroxylase polypeptides.AccessionGINumberNumberDescriptionAAC448521842246b-carotene hydroxylaseAAC494431575296beta-carotene hydroxylase [ Arabidopsis thaliana ]AAD542435852870carotenoid hydroxylase [ Haematococcus pluvialis ]AAG104309971820beta hydroxylase [ Tagetes erecta ]AAG107939988836beta-carotene hydroxylase [ Citrus unshiu ]AAG3363611245486beta-carotene hydroxylase [ Citrus unshiu ]AAL8000619071768beta carotene hydroxylase [ Sandersonia aurantiaca ]AAM4497121280903putative beta-carotene hydroxylase [ Arabidopsis thaliana ]AAM5130021436107putative beta-carotene hydroxylase [ Arabidopsis thaliana ]AAM7700721734857beta-carotene hydroxylase [ Vitis vinifera ]AAN8560127228295Beta-Carotene Hydroxylase [ Pantoea stewartii ]AAO5329528911949carotenoid hydroxylase [ Haematococcus pluvialis ]AAS4809744887642beta-carotene hydroxylase [ Citrus sinensis ]AAS5555245184599putative beta-carotene hydroxylase [ Brassica rapa ]AAS8842646326968beta-carotene hydroxylase [ Glycine max ]AAT4874149036137beta-carotene hydroxylase [ Citrus sinensis ]AAT8440850844570beta carotene hydroxylase [ Crocus sativus ]AAV8545256267980beta-ring oxygenase AdKeto1 [ Adonis palaestina ]AAV8545356267982beta-ring oxygenase AdKeto2 [ Adonis palaestina ]BAA14129216687crtZ [ Pantoea ananatis ]BAB7960518143450crtZ [ Pantoea agglomerans pv. milletiae ]BAC7767031790567gamma-carotene hydroxylase [ marine bacterium P99-3]BAD0728340809749beta-ring hydroxylase [ Citrus sinensis ]BAD0729140809765beta-ring hydroxylase [ Citrus limon ]CAA704272956671beta-carotene hydrolase [ Capsicum annuum ]CAA708882956717beta-carotene hydroxylase 2 [ Capsicum annuum ]CAB556255870598beta-carotene hydroxylase [ Lycopersicon esculentum ]CAB556265870600beta-carotene hydroxylase [ Lycopersicon esculentum ]CAB560605912293carotene hydroxylase [ Paracoccus marcusii ]CAC067129968545beta-carotene hydroxylase [ Narcissus pseudonarcissus ]CAC9513033145986beta-carotene hydroxylase [ Crocus sativus ]EAB3012842926157unknown [environmental sequence]EAC4946243167766unknown [environmental sequence]EAC8612943241003unknown [environmental sequence]EAD6108943395962unknown [environmental sequence]EAD7615643443111unknown [environmental sequence]EAD8864043467793unknown [environmental sequence]EAE2790343546376unknown [environmental sequence]EAE2820343546980unknown [environmental sequence]EAE7874343647896unknown [environmental sequence]EAF1217343714211unknown [environmental sequence]EAH2937044130906unknown [environmental sequence]EAH4420244158360unknown [environmental sequence]EAI0076644256844unknown [environmental sequence]EAI2901744298625unknown [environmental sequence]EAJ3084444443849unknown [environmental sequence]EAJ7252444504516unknown [environmental sequence]EAK1061144559981unknown [environmental sequence]EAK5345544620561unknown [environmental sequence]EAK6395544635271unknown [environmental sequence]H9046925394049beta carotene hydroxylase (crtZ) [imported] - SulfolobussolfataricusNP_74538926989964beta-carotene hydroxylase [ Pseudomonas putida KT2440]NP_92250337536402putative beta-carotene hydroxylase [ Oryza sativa ( japonicacultivar-group)]P549731706152Beta-carotene hydroxylaseQ442622498258Beta-carotene hydroxylaseS529821073291beta-carotene hydroxylase - Erwinia herbicolaXP_47361150928167OSJNBa0011J08.7 [ Oryza sativa ( japonica cultivar-group)]YP_02430948478603beta carotene hydroxylase [ Picrophilus torridus DSM 9790]ZP_00305548851297COG3000: Sterol desaturase [ Novosphingobium aromaticivoransDSM 12444]ZP_00310748856620COG3000: Sterol desaturase [ Cytophaga hutchinsonii ] TABLE 21Examples of astaxanthin synthase polypeptides and putative astaxanthin synthasepolypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAM5628821501451Astaxanthin synthase [ Xanthophyllomyces dendrorhous ]XP_57127658268240Cytochrome P450, putative [ Cryptococcus neoformans var. neoformansJEC21]EAL2001350257304hypothetical protein CNBF3400 [ Cryptococcus neoformans var.neoformans B-3501A]XP_40180449075484hypothetical protein UM04189.1 [ Ustilago maydis 521]XP_39781749067054hypothetical protein UM00202.1 [ Ustilago maydis 521]XP_39959549070612hypothetical protein UM01980.1 [ Ustilago maydis 521]XP_40327949079218hypothetical protein UM05664.1 [ Ustilago maydis 521]XP_38229446110473hypothetical protein FG02118.1 [ Gibberella zeae PH-1]XP_40602149088382hypothetical protein AN1884.2 [ Aspergillus nidulans FGSC A4]XP_38122446108332hypothetical protein FG01048.1 [ Gibberella zeae PH-1]XP_39147946139577hypothetical protein FG11303.1 [ Gibberella zeae PH-1]XP_56926158264210conserved hypothetical protein [ Cryptococcus neoformans var.neoformans JEC21]EAL2284150260180hypothetical protein CNBB0620 [ Cryptococcus neoformans var.neoformans B-3501A]XP_35986639940658hypothetical protein MG04911.4 [ Magnaporthe grisea 70-15] TABLE 22Examples of carotenoid epsilon hydroxylase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONABB5207679155148putative epsilon-ring carotene hydroxylase [ Daucus carotasubsp. sativus]BAD9413662319017Cytochrom P450-like protein [ Arabidopsis thaliana ]ABD2856587162770E-class P450, group I [ Medicago truncatula ]AAT2822247498772putative 97B2-like cytochrome P450 [ Ginkgo biloba ]ABC6839685001685cytochrome P450 monooxygenase CYP97A [ Glycine max ]ABC5911084514203cytochrome P450 monooxygenase CYP97B [ Medicagotruncatula ]NP_19088142565881LUT1 (LUTEIN DEFICIENT 1); oxygen binding[ Arabidopsis thaliana ]ABB4795478708979cytochrome P450 monooxygenase, putative [ Oryza sativa( japonica cultivar-group)]NP_92260437536604putative cytochrome P450 monooxygenase [ Oryza sativa( japonica cultivar-group)] TABLE 23Examples of lycopene cyclase polypeptides, beta and epsilon subunits.ACCESSIONGIPROTEIN DESCRIPTIONXP_001422490145356548predicted protein [ Ostreococcus lucimarinus CCE9901]BAE9403694481238lycopene epsilon cyclase ( Diospyros kaki )AAK0743112746307lycopene epsilon-cyclase [ Adonis palaestina ]ABB5207379154988putative lycopene epsilon cyclase [ Daucus carota subsp.sativus ]Q3893227735211Lycopene epsilon cyclase, chloroplast precursorAAB533361399181lycopene epsilon cyclaseAAG104289971816epsilon cyclase [ Tagetes erecta ]AAK0743412746313lycopene epsilon-cyclase [ Lactuca sativa ]AAM4538221360359epsilon cyclase [ Tagetes erecta ]O6583711132841Lycopene epsilon cyclase, chloroplast precursorAAL6939418419661lycopene epsilon-cyclase [ Spinacia oleracea ]BAE7954987299433lycopene epsilon-cyclase [ Chrysanthemum x morifolium ]XP_46335150901836putative lycopene epsilon-cyclase [ Oryza sativa ( japonicacultivar-group)]AAS4809644887640epsilon lycopene cyclase [ Citrus sinensis ]AAX9267962638188lycopene epsilon cyclase [ Citrus maxima ]AAL9211419569601lycopene epsilon-cyclase [ Citrus x paradisi ]AAK0743312746311lycopene epsilon-cyclase [ Solanum tuberosum ]AAL4701917864021lycopene epsilon-cyclase [ Citrus sinensis ]AAT4606548686703chloroplast lycopene epsilon-cyclase precursor[ Chlamydomonas reinhardtii ]BAD0729340809769lycopene epsilon-cyclase [ Citrus limon ]BAD0728540809753lycopene epsilon-cyclase [ Citrus sinensis ]BAD0727740809737lycopene epsilon-cyclase [ Citrus unshiu ]EAJ6283944489138unknown [environmental sequence]BAE4354773993068putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4355073993074putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4355773993088putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4355873993090putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4355373993080putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4354573993064putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4355673993086putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4355273993078putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4356073993094putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4355473993082putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4355173993076putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4351973993012putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4353573993044putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354173993056putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354273993058putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4351773993008putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4353473993042putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4353773993048putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4353373993040putative lycopene beta cyclase [ Cryptomeria japonica ]BAD0277438603277putative lycopene beta cyclase [ Cryptomeria japonica ]BAD0276638603261putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354073993054putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4351473993002putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354473993062putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4353873993050putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4352873993030putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354673993066putative lycopene beta cyclase [ Taxodium distichum var.distichum ]BAE4352673993026putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354373993060putative lycopene beta cyclase [ Cryptomeria japonica ]BAD0274238603213putative lycopene beta cyclase [ Cryptomeria japonica ]BAD0277038603269putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4352273993018putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4355973993092putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4352773993028putative lycopene beta cyclase [ Cryptomeria japonica ]BAE4354873993070putative lycopene beta cyclase [ Taxodium distichum var.distichum ]AAF4470014550425lycopene beta-cyclase [ Citrus sinensis ]BAE4355573993084putative lycopene beta cyclase [ Taxodium distichum var.imbricarium ]BAE4354973993072putative lycopene beta cyclase [ Taxodium distichum var.distichum ]AAU1414451922063lycopene beta-cyclase [ Citrus sinensis ]AAN8606027261727lycopene cyclase [ Citrus unshiu ]AAR8963240756518lycopene-beta-cyclase [ Citrus maxima ]AAM2115220530862lycopene beta-cyclase [ Citrus sinensis ]AAD3804913959731lycopene cyclase [ Citrus x paradisi ]AAU0514651511939lycopene beta-cyclase [ Citrus sinensis ]AAU0514551511937lycopene beta-cyclase [ Citrus sinensis ]AAK0743012746305lycopene beta-cyclase [ Adonis palaestina ]ABB7244382394885lycopene beta-cyclase [ Citrus sinensis ]BAE7954487299423lycopene beta-cyclase [ Chrysanthemum x morifolium ]BAE7847185717882lycopene beta cyclase [ Taraxacum officinale ]Q4341511133019Lycopene beta cyclase, chloroplast precursorAAF230136665782lycopene epsilon-cyclase [ Daucus carota ]ABB5207179154899putative lycopene beta cyclase [ Daucus carota subsp.sativus ]AAW8838259665024lycopene beta-cyclase [ Lycium barbarum ]AAG104299971818beta cyclase [ Tagetes erecta ]AAM4538121360357beta cyclase [ Tagetes erecta ]AAM1433520259239putative lycopene beta cyclase [ Arabidopsis thaliana ]AAO1866127728515lycopene beta-cyclase [ Zea mays ]AAA81880735882lycopene cyclaseQ4350311133022Lycopene beta cyclase, chloroplast precursorS663502129931lycopene beta-cyclase (EC 5.5.1. - ) - tomatoXP_46440950905841putative lycopene beta-cyclase [ Oryza sativa ( japonicacultivar-group)]CAD7056545237491lycopene cyclase [ Bixa orellana ]Q4357811133025Lycopene beta cyclase, chloroplast precursorAAL9217519569782beta-lycopene cyclase [ Sandersonia aurantiaca ]AAX5490661742130putative chloroplast lycopene beta cyclase precursor[ Chlamydomonas reinhardtii ]S663492129954lycopene beta-cyclase (EC 5.5.1. - ) - common tobaccoAAG2113310644119chromoplast-specific lycopene beta-cyclase [ Lycopersiconesculentum ]CAB929778247354neoxanthin synthase [ Solanum tuberosum ]CAB933428249885neoxanthin synthase [ Lycopersicon esculentum ]Q9SEA011131528Capsanthin/capsorubin synthase, chloroplast precursorQ4243512643508Capsanthin/capsorubin synthase, chloroplast precursorAAO6497737730608lycopene beta cyclase [ Haematococcus pluvialis ]Q4042411133011Lycopene beta cyclase, chloroplast precursorABB5207279154940putative capsanthin-capsorubin synthase [ Daucus carotasubsp. sativus ]AAQ0266833304511lycopene cyclase [ Setaria italica ]CAA54961840729putative chromoplastic oxydo-reductase [ Capsicumannuum ]EAJ6283844489136unknown [environmental sequence]YP_40107981300871Lycopene cyclase, beta and epsilon [ Synechococcuselongatus PCC 7942]YP_17274156752040lycopene cyclase [ Synechococcus elongatus PCC 6301]ZP_011 . . .88808972lycopene beta cyclase [ Synechococcus sp. WH 7805]EAK5005244615956unknown [environmental sequence]NP_89275133861190putative lycopene epsilon cyclase [ Prochlorococcusmarinus subsp. pastoris str. CCMP1986]NP_87518233240240Lycopene epsilon cyclase [ Prochlorococcus marinus subsp.marinus str. CCMP1375]YP_38223778213458Lycopene cyclase, beta and epsilon [ Synechococcus sp.CC9605]YP_39713078779018Lycopene cyclase, beta and epsilon [ Prochlorococcusmarinus str. MIT 9312]NP_89682133865262lycopene beta cyclase [ Synechococcus sp. WH 8102]YP_39757078779458Lycopene cyclase, beta and epsilon [ Prochlorococcusmarinus str. MIT 9312]ZP_010 . . .87302144lycopene cyclase [ Synechococcus sp. WH 5701]EAK1714944569190unknown [environmental sequence]YP_29188272382527lycopene cyclase, beta and epsilon [ Prochlorococcusmarinus str. NATL2A]NP_87552833240586Lycopene beta cyclase related dehydrogenase[ Prochlorococcus marinus subsp. marinus str. CCMP1375]NP_89318133861620putative lycopene beta cyclase [ Prochlorococcus marinussubsp. pastoris str. CCMP1986]NP_89560033864040putative lycopene epsilon cyclase [ Prochlorococcusmarinus str. MIT 9313]EAI4745644325573unknown [environmental sequence]YP_29126872381913lycopene cyclase, beta and epsilon [ Prochlorococcusmarinus str. NATL2A]ZP_010 . . .84517806Lycopene beta cyclase related dehydrogenase[ Prochlorococcus marinus str. MIT 9211]AAF341916970079lycopene epsilon cyclase [ Daucus carota ]ZP_010 . . .84518202Lycopene epsilon cyclase [ Prochlorococcus marinus str.MIT 9211]YP_37673678184301Lycopene cyclase, beta and epsilon [ Synechococcus sp.CC9902]ZP_003 . . .66796756Lycopene cyclase, beta and epsilon [ Deinococcusgeothermalis DSM 11300]NP_89495433863394putative lycopene beta cyclase [ Prochlorococcus marinusstr. MIT 9313]AAT7605150365502lycopene cyclase [ Citrus clementina ]EAK2204744576122unknown [ environmental sequence ]NP_29452515805827lycopene cyclase [ Deinococcus radiodurans R1] TABLE 24Examples of carotenoid glucosyltransferase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAA21261148395CrtX [ Pantoea agglomerans ]AAN8559727228291Zeaxanthin Glucosyl Transferase [ Pantoea stewartii ]BAB7960118143446crtX [ Pantoea agglomerans pv. milletiae ]AAZ7314772536082zeaxanthin glucosyl transferase [ Enterobacteriaceae bacteriumDC413]AAZ7312872536060zeaxanthin glucosyl transferase [ Enterobacteriaceae bacteriumDC260]AAZ7314072536074zeaxanthin glucosyl transferase [ Enterobacteriaceae bacteriumDC416]Q01330231911Zeaxanthin glucosyl transferaseZP_006 . . .71674312UDP-glycosyltransferase, MGT [ Trichodesmium erythraeumIMS101]NP_43997216329244zeaxanthin glucosyl transferase [ Synechocystis sp. PCC 6803]EAH2936844130903unknown [environmental sequence]ZP_005 . . .67926135zeaxanthin glucosyl transferase, hypothetical protein[ Crocosphaera watsonii WH 8501]YP_37876378188425hypothetical protein Cag_0447 [ Chlorobium chlorochromatiiCaD3]ZP_005 . . .68549418Glycosyl transferase, group 1 [ Pelodictyon phaeoclathratiformeBU-1]ZP_010 . . .85713606glycosyl transferase, group 1 [ Nitrobacter sp. Nb-311A]YP_31717175674750glycosyl transferase, group 1 [ Nitrobacter winogradskyi Nb-255]ZP_006 . . .69929171Glycosyl transferase, group 1 [ Nitrobacter hamburgensis X14]ZP_009 . . .84500589hypothetical protein OB2597_11541 [ Oceanicola batsensisHTCC2597]ZP_009 . . .83953176hypothetical protein NAS141_12746 [ Sulfitobacter sp. NAS-14.1]ZP_009 . . .83942121hypothetical protein EE36_07793 [ Sulfitobacter sp. EE-36]YP_50802089052569glycosyl transferase, group 1 [ Jannaschia sp. CCS1]ZP_010 . . .85704103hypothetical protein ROS217_13931 [ Roseovarius sp. 217]ZP_009 . . .83370850probable glycosyltransferase [ Rhodobacter sphaeroides ATCC17025]ZP_006 . . .69934465Glycosyl transferase, group 1 [ Paracoccus denitrificansPD1222]ZP_009 . . .83949880probable glycosyltransferase [ Roseovarius nubinhibens ISM]YP_37623778183803putative glycosyltransferase [ Synechococcus sp. CC9902]YP_37612978183695probable glycosyltransferase [ Synechococcus sp. CC9902]YP_37429678186253hypothetical protein Plut_0365 [ Pelodictyon luteolum DSM273]ZP_010 . . .87301651Putative glycosyltransferase [ Synechococcus sp. WH 5701]ZP_011 . . .88809938Putative glycosyltransferase [ Synechococcus sp. WH 7805]BAE4747178483937carotenoid glucosyltransferase [ Paracoccus sp. N81106]ZP_010 . . .87303273probable glycosyltransferase [ Synechococcus sp. WH 5701]YP_37612778183693probable glycosyltransferase [ Synechococcus sp. CC9902]YP_50133488196509hypothetical protein SAOUHSC_02880 [ Staphylococcusaureus subsp. aureus NCTC 8325]YP_18737057652300glycosyl transferase, group 2 family protein [ Staphylococcusaureus subsp. aureus COL]CAA666271340131unnamed protein product [ Staphylococcus aureus ]YP_04198749484763putative glycosyl transferase [ Staphylococcus aureus subsp.aureus MRSA252]YP_41788582752144hypothetical protein SAB2436c [ Staphylococcus aureusRF122]YP_25240470725490hypothetical protein SH0489 [ Staphylococcus haemolyticusJCSC1435]NP_69337923099913hypothetical protein OB2458 [ Oceanobacillus iheyensisHTE831]ZP_008 . . .82501285conserved hypothetical protein [ Caldicellulosiruptorsaccharolyticus DSM 8903]ZP_010 . . .87303565hypothetical protein WH5701_09900 [ Synechococcus sp. WH5701] TABLE 25Examples of acyl CoA:diacyglycerol acyltransferase (DGAT) polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONXP_95702285082953hypothetical protein [ Neurospora crassa N150]XP_38686446124621hypothetical protein FG06688.1 [ Gibberella zeae PH-1]XP_75517271000982diacylglycerol O-acyltransferase DGAT [ Aspergillusfumigatus Af293]XP_66376367539978hypothetical protein AN6159.2 [ Aspergillus nidulans FGSCA4]BAE6530283775179unnamed protein product [ Aspergillus oryzae ]XP_50255750550169hypothetical protein [ Yarrowia lipolytica ]AAS7866256199782diacylglycerol acyltransferase [ Glycine max ]ABB8438382582915diacylglycerol acyltransferase [ Jatropha curcas ]AAV31083541454591,2-diacyl-sn-glycerol:acyl-CoA acyltransferase [ Euonymusalatus ]AAG2369610803053diacylglycerol acyltransferase [ Perilla frutescens ]AAF640657576941putative diacylglycerol acyltransferase [ Brassica napus ]AAS0160641387497acyl-CoA:diacylglycerol acyltransferase 1 [ Olea europaea ]AAT7362950299542acyl CoA:diacylglycerol acyltransferase [ Glycine max ]AAM0334067043496putative diacylglycerol acyltransferase [ Tropaeolum majus ]XP_64563366824557hypothetical protein DDB0202877 [ Dictyosteliumdiscoideum ]AAF193456625653diacylglycerol acylCoA acyltransferase [ Nicotiana tabacum ]AAY4078563376239diacylglycerol acyltransferase DGAT2 [ Brassica juncea ]AAW4758157231736diacylglycerol acyltransferase [ Oryza sativa ( japonicacultivar-group)]AAR1147938146080diacylglycerol acyltransferase [ Ricinus communis ]AAY4078463376226diacylglycerol acyltransferase DGAT1 [ Brassica juncea ]AAP6832231711932At2g19450 [ Arabidopsis thaliana ]AAW5145657545061diacylglycerol acyltransferase [ Lotus corniculatus var.japonicus ]AAD455365579408putative diacylglycerol acyltransferase [ Brassica napus ]BAD5376253791817putative acyl-CoA:diacylglycerol acyltransferase [ Oryzasativa (japonica cultivar-group)]NP_95602441054343hypothetical protein LOC325875 [ Danio rerio ]AAL4996218642598diacylglycerol acyltransferase 1 [ Bos taurus ]XP_93088489028385similar to Diacylglycerol O-acyltransferase 1 (Diglycerideacyltransferase) (ACAT-related gene) [ Homo sapiens ]NP_77711827819636diacylglycerol O-acyltransferase 1 [ Bos taurus ]Q9GMF118202926Diacylglycerol O-acyltransferase 1 (Diglycerideacyltransferase)NP_0362116912332diacylglycerol O-acyltransferase 1 [ Homo sapiens ]AAH0626334782946DGAT1 protein [ Homo sapiens ]XP_78051572006039similar to Diacylglycerol O-acyltransferase 1[ Strongylocentrotus purpuratus ]AAD408815225382putative diacylglycerol acyltransferase [ Brassica napus ]XP_53921473974769similar to Diacylglycerol O-acyltransferase 1 (ACAT relatedgene product 1) isoform 1 [ Canis familiaris ]AAZ2240371063860diacylglycerol O-acyltransferase 1 [ Bubalus bubalis ]NP_99921647522918diacylglycerol acyltransferase [ Sus scrofa ]NP_001 . . .50539976hypothetical protein LOC436731 [ Danio rerio ]XP_84917673974767similar to Diacylglycerol O-acyltransferase 1 (ACAT relatedgene product 1) isoform 2 [ Canis familiaris ]NP_50582871997360H19N07.4 [ Caenorhabditis elegans ]AAF824109049538diacylglycerol acyltransferase [ Caenorhabditis elegans ]CAE7517039591950Hypothetical protein CBG23107 [ Caenorhabditis briggsae ]XP_62633766358318diacylglycerol acyltransferase 1 [ Cryptosporidium parvumIowa II]XP_66840267624239acyl-CoA:diacylglycerol acyltransferase 1-related enzyme[ Cryptosporidium hominis TU502]AAP9420833113253acyl-CoA:diacylglycerol acyltransferase 1-related enzyme[ Toxoplasma gondii ]AAP9420933113255acyl-CoA:diacylglycerol acyltransferase 1-related enzyme[ Toxoplasma gondii ]XP_57955762652535PREDICTED: diacylglycerol O-acyltransferase 1 [ Rattusnorvegicus ]BAC6617129170489diacylglycerol acyltransferase [ Mus musculus ]Q9ERM318202872Diacylglycerol O-acyltransferase 1 (Diglycerideacyltransferase)AAL7836618698659acyl coenzyme A:diacylglycerol acyltransferase [ Drosophilamelanogaster ]NP_99572445552403CG31991-PD, isoform D [ Drosophila melanogaster ]NP_72401724584734CG31991-PC, isoform C [ Drosophila melanogaster ]XP_85806273974765similar to Diacylglycerol O-acyltransferase 1 (ACAT relatedgene product 1) isoform 3 [ Canis familiaris ]XP_72898482915156hypothetical protein PY01256 [ Plasmodium yoelii yoelii str.17XNL]CAG1194447225461unnamed protein product [ Tetraodon nigroviridis ]BAD2752650199438acyl-CoA:diacylglycerol acyltransferase [eukaryotic syntheticconstruct]XP_31765631226099ENSANGP00000002281 [ Anopheles gambiae str. PEST]AAV5945755733950putative diacylglycerol acyltransferase [ Oryza sativa( japonica cultivar-group)]EAL3359354644853GA16599-PA [ Drosophila pseudoobscura ]XP_67875368073677diacylglycerol O-acyltransferase [ Plasmodium berghei strainANKA]XP_52001455631434PREDICTED: similar to Diacylglycerol O-acyltransferase 1(Diglyceride acyltransferase) [ Pan troglodytes ]CAG1081547219451unnamed protein product [ Tetraodon nigroviridis ]XP_62475466522700PREDICTED: similar to ENSANGP00000002281 [ Apismellifera ]CAC6988415620769diacylglycerol acyltransferase I [ Rattus norvegicus ]XP_68618168363630PREDICTED: similar to Diacylglycerol O-acyltransferase 1(Diglyceride acyltransferase) [ Danio rerio ]XP_73400870921323diacylglycerol O-acyltransferase [ Plasmodium chabaudichabaudi ]XP_67312868062248hypothetical protein PB300300.00.0 [ Plasmodium bergheistrain ANKA]AAS7237645642963acyl-CoA:cholesterol acyltransferase beta [ Toxoplasmagondii ]AAS7237545642961acyl-CoA:cholesterol acyltransferase alpha [ Toxoplasmagondii ]NP_58614519074639STEROL O-ACYLTRANSFERASE [ Encephalitozooncuniculi GB-M1]XP_64028066812202hypothetical protein DDB0205259 [ Dictyosteliumdiscoideum ]AAY4078363376221diacylglycerol acyltransferase [ Brassica juncea ]XP_76577471032265diacylglycerol O-acyltransferase [ Theileria parva strainMuguga ]Q876L234582301Sterol O-acyltransferase 2 (Sterol-ester synthase 2)XP_57126058268208sterol O-acyltransferase [ Cryptococcus neoformans var.neoformans JEC21]EAL2003250257323hypothetical protein CNBF3580 [ Cryptococcus neoformansvar. neoformans B-3501A]XP_95447884999514acyl transferase [ Theileria annulata strain Ankara ]XP_50508650555355hypothetical protein [ Yarrowia lipolytica ]NP_58855819076058hypothetical protein SPCP1E11.05c [ Schizosaccharomycespombe 972h-]AAC494411389739acyl-CoA: sterol acyltransferaseNP_0144166324346Acyl-CoA: sterol acyltransferase, isozyme of Are1p; Are2p[ Saccharomyces cerevisiae ]XP_75035470991010sterol o-acyltransferase APE2 [ Aspergillus fumigatus Af293]XP_38219246110268hypothetical protein FG02016.1 [ Gibberella zeae PH-1]BAE5493483764790unnamed protein product [ Aspergillus oryzae ]XP_88591476617939similar to Sterol O-acyltransferase 2 (Cholesterolacyltransferase 2) (ACAT-2) isoform 2 [ Bos taurus ]XP_59125176617937similar to Sterol O-acyltransferase 2 (Cholesterolacyltransferase 2) (ACAT-2) isoform 1 [ Bos taurus ]BAC0084621392392AcylCoA: Cholesterol Acyltransferase 2 [ Rattus norvegicus ]NP_64981628571583CG8112-PA [ Drosophila melanogaster ]NP_66617622122547sterol O-acyltransferase 2 [ Mus musculus ]O8890818202245Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)(ACAT-2)XP_76150271022545hypothetical protein UM05355.1 [ Ustilago maydis 521]NP_71495040254723sterol O-acyltransferase 2 [ Rattus norvegicus ]EAQ8609488178626hypothetical protein CHGG_07347 [ Chaetomium globosumCBS 148.51]XP_46139550425599hypothetical protein DEHA0F25652g [ Debaryomyceshansenii CBS767]XP_66181267527926hypothetical protein AN4208.2 [ Aspergillus nidulans FGSCA4]AAH9609164654094Sterol O-acyltransferase 2 [ Homo sapiens ]O7590818202149Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)(ACAT-2)AAH9609064652990Sterol O-acyltransferase 2 [ Homo sapiens ]AAK4882913898623acyl coenzyme A: cholesterol acyltransferase-2 [ Homosapiens ]XP_54363773996435PREDICTED: similar to sterol O-acyltransferase 2 [ Canisfamiliaris ]O7775918202176Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2)(ACAT-2)AAO3247428564191ARE2 [ Saccharomyces castellii ]XP_32348532405744hypothetical protein [ Neurospora crassa ]NP_98260645184888AAR065Cp [ Eremothecium gossypii ]NP_59370819114620hypothetical protein SPAC13G7.06 [ Schizosaccharomycespombe 972h-]AAO3255428564940ARE2 [ Saccharomyces kluyveri ]EAL2896254639560GA20833-PA [ Drosophila pseudoobscura ]XP_44980650294790hypothetical protein CAGL0M10571g [ Candida glabrataCBS138]NP_03325684619697sterol O-acyltransferase 1 [ Mus musculus ]Q6126318202591Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)(ACAT-1)BAC3492526342537unnamed protein product [ Mus musculus ]XP_45260750305295unnamed protein product [ Kluyveromyces lactis ]NP_001 . . .77735363hypothetical protein LOC504287 [ Bos taurus ]Q6045718202585Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)(ACAT-1)XP_32032158393811ENSANGP00000016512 [ Anopheles gambiae str. PEST]XP_32032058393809ENSANGP00000016486 [ Anopheles gambiae str. PEST]O7053618202126Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)(ACAT-1)XP_71477668482533acyl-CoA cholesterol acyltransferase [ Candida albicansSC5314]P8428556404462Sterol O-acyltransferase 2 (Sterol-ester synthase) (ASAT)AAH7791650416229Soat1-prov protein [ Xenopus laevis ]XP_69285568364838PREDICTED: similar to Soat1-prov protein [ Danio rerio ]CAI1357455960156sterol O-acyltransferase (acyl-Coenzyme A: cholesterolacyltransferase) 1 [ Homo sapiens ]AAL5622718028942cholesterol acyltransferase 1 [ Gorilla gorilla ]AAL5622818028944cholesterol acyltransferase 1 [ Pongo pygmaeus ]AAC375324878022acyl-coenzyme A: cholesterol acyltransferase [ Homo sapiens ]2201440A1585676acyl-CoA/cholesterol acyltransferaseQ876L334582302Sterol O-acyltransferase 1 (Sterol-ester synthase 1)BAE0104867969393unnamed protein product [ Macaca fascicularis ]XP_51403055588858PREDICTED: hypothetical protein XP_514030 [ Pantroglodytes ]XP_54744573961286similar to Sterol O-acyltransferase 1 (Cholesterolacyltransferase 1) (ACAT-1) [ Canis familiaris ]EAQ8461988177151hypothetical protein CHGG_08633 [ Chaetomium globosumCBS 148.51]O7776118202178Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1)(ACAT-1)XP_42226750751122PREDICTED: similar to Sterol O-acyltransferase 1(Cholesterol acyltransferase 1) (ACAT-1) [ Gallus gallus ]XP_69328468392980PREDICTED: similar to Sterol O-acyltransferase 1(Cholesterol acyltransferase 1) (ACAT-1) [ Danio rerio ]AAT9294051013293YCR048W [ Saccharomyces cerevisiae ]XP_95657685080625hypothetical protein [ Neurospora crassa N150]XP_62469166564061PREDICTED: similar to ENSANGP00000016486 [ Apismellifera ]CAF9651447222847unnamed protein product [ Tetraodon nigroviridis ]XP_78820972085563PREDICTED: similar to sterol O-acyltransferase 1[ Strongylocentrotus purpuratus ]XP_44530750285757unnamed protein product [ Candida glabrata ]CAE7000239596364Hypothetical protein CBG16409 [ Caenorhabditis briggsae ]CAG0799047225647unnamed protein product [ Tetraodon nigroviridis ]NP_51062317549960B0395.2 [ Caenorhabditis elegans ]AAX2833176157393SJCHGC04421 protein [ Schistosoma japonicum ]CAI9615866347204Diacylglycerol O-acyltransferase [ Bubalus bubalis ]XP_39003946136695hypothetical protein FG09863.1 [ Gibberella zeae PH-1]XP_64316966819019hypothetical protein DDB0203882 [ Dictyosteliumdiscoideum ]AAO5309528850306hypothetical protein [ Dictyostelium discoideum ]AAB069591515472acyl-CoA: cholesterol acyltransferase [ Oryctolagus cuniculus ]NP_94561939933343putative alginate o-acetyltransferase AlgI[ Rhodopseudomonas palustris CGA009]ZP_008 . . .77691302Membrane bound O-acyl transferase, MBOAT[ Rhodopseudomonas palustris BisB5]XP_46554650908115putative wax synthase [ Oryza sativa ( japonica cultivar-group)] TABLE 29Examples of Prenyldiphosphate synthase polypeptidesAccessionGIDescription29A: Bacteria Proteins that require a mitochondrial targeting sequenceZP_009 . . .83373595Trans-hexaprenyltranstransferase [ Rhodobacter sphaeroides ATCC17029]ZP_009 . . .83371280Trans-hexaprenyltranstransferase [ Rhodobacter sphaeroides ATCC17025]CAD2441720429105decaprenyl diphosphate synthase [ Paracoccus zeaxanthinifaciens ]ZP_010 . . .85705714Geranylgeranyl pyrophosphate synthase/Polyprenyl synthetase[ Roseovarius sp. 217]ZP_010 . . .84515724decaprenyl diphosphate synthase [ Loktanella vestfoldensis SKA53]YP_16558256695234decaprenyl diphosphate synthase [ Silicibacter pomeroyi DSS-3]ZP_010 . . .86139019decaprenyl diphosphate synthase [ Roseobacter sp. MED193]ZP_009 . . .83941379decaprenyl diphosphate synthase [ Sulfitobacter sp. EE-36]ZP_009 . . .83854856decaprenyl diphosphate synthase [ Sulfitobacter sp. NAS-14.1]ZP_006 . . .69299873Farnesyltranstransferase [ Silicibacter sp. TM1040]ZP_010 . . .84683979Geranylgeranyl pyrophosphate synthase/Polyprenyl synthetase[ Rhodobacterales bacterium HTCC2654]ZP_009 . . .84500217decaprenyl diphosphate synthase [ Oceanicola batsensis HTCC2597]ZP_009 . . .83952381decaprenyl diphosphate synthase [ Roseovarius nubinhibens ISM]ZP_006 . . .69937106Trans-hexaprenyltranstransferase [ Paracoccus denitrificans PD1222]ZP_005 . . .68180845Trans-hexaprenyltranstransferase [ Jannaschia sp. CCS1]ZP_008 . . .78495595Polyprenyl synthetase [ Rhodopseudomonas palustris BisB18]AAY8236867866738decaprenyl diphosphate synthase [ Agrobacterium tumefaciens ]NP_35365615887975hypothetical protein AGR_C_1125 [ Agrobacterium tumefaciens str.C58]ZP_008 . . .77688465Farnesyltranstransferase [ Rhodopseudomonas palustris BisB5]NP_53133417934544octaprenyl-diphosphate synthase [ Agrobacterium tumefaciens str.C58]YP_48470986748213Farnesyltranstransferase [ Rhodopseudomonas palustris HaA2]AAP5624037903500decaprenyl diphosphate synthase [ Agrobacterium tumefaciens ]YP_19238858040424Decaprenyl diphosphate synthase [ Gluconobacter oxydans 621H]29B: Subunit 1 - Proteins that contain mitochondrial targeting sequenceT4319311279237trans-pentaprenyltranstransferase homolog - fission yeast( Schizosaccharomyces pombe )AAD285594732024trans-prenyltransferase [ Homo sapiens ]AAI0727578070698Trans-prenyltransferase [ Mus musculus ]BAE4821681157931subunit 1 of decaprenyl diphosphate synthase [ Homo sapiens ]AAH4921129165656PDSS1 protein [ Homo sapiens ]Q33DR285700953Decaprenyl-diphosphate synthase subunit 1 (Solanesyl-diphosphatesynthase subunit 1) (Trans-prenyltransferase)XP_50770655633583PREDICTED: similar to TPRT protein [ Pan troglodytes ]XP_58671776632198PREDICTED: similar to trans-prenyltransferase [ Bos taurus ]XP_84990873948851PREDICTED: similar to trans-prenyltransferase [ Canis familiaris ]29C: Subunit 2 - Proteins that contain mitochondrial targeting sequenceO1385160389474Decaprenyl-diphosphate synthase subunit 2 (Decaprenylpyrophosphate synthetase subunit 2)BAE4821881157935subunit 2 of solanesyl diphosphate synthase [ Mus musculus ]BAE4821781157933subunit 2 of decaprenyl diphosphate synthase [ Homo sapiens ] TABLE 30Examples of PHB-Polyprenyltransferase polypeptidesGIPROTEIN DESCRIPTION51013645YNR041C [ Saccharomyces cerevisiae ]50285815unnamed protein product [ Candida glabrata ]50311051unnamed protein product [ Kluyveromyces lactis ]45200866AGL231Wp [ Eremothecium gossypii ]50555263hypothetical protein [ Yarrowia lipolytica ]68473193para-hydroxybenzoate: polyprenyl transferase [ Candida albicans SC5314]50410039hypothetical protein DEHA0A14212g [ Debaryomyces hansenii CBS767]83769349unnamed protein product [ Aspergillus oryzae ]70994900para-hydroxybenzoate-polyprenyltransferase precursor [ Aspergillus fumigatusAf293]19114131hypothetical protein SPAC56F8.04c [ Schizosaccharomyces pombe 972h-]39973573hypothetical protein MG01067.4 [ Magnaporthe grisea 70-15]85078920protein related to para-hydroxybenzoate polyprenyltransferase precursor[ Neurospora crassa N150]76660839PREDICTED: similar to para-hydroxybenzoate-polyprenyltransferase,mitochondrial [ Bos taurus ]52138578para-hydroxybenzoate-polyprenyltransferase, mitochondrial [ Homo sapiens ]18088424COQ2 protein [ Homo sapiens ]47221448unnamed protein product [ Tetraodon nigroviridis ]58385249ENSANGP00000012220 [ Anopheles gambiae str. PEST]50746583PREDICTED: similar to hypothetical protein CL640 [ Gallus gallus ]54638587GA21912-PA [ Drosophila pseudoobscura ]21355567CG9613-PA [ Drosophila melanogaster ]71005862hypothetical protein UM01450.1 [ Ustilago maydis 521] TABLE 31Examples of soluble transydrogenase polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAD406915163507soluble pyridine nucleotide transhydrogenase [ Azotobactervinelandii2ZP_013 . . .107102541hypothetical protein PaerPA_01003605 [ Pseudomonasaeruginosa PACS2]3ZP_012 . . .94416745hypothetical protein PaerP_01001583 [ Pseudomonas aeruginosaPA7]4O0513911135075Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])5YP_25907770729340soluble pyridine nucleotide transhydrogenase [ Pseudomonasfluorescens Pf-5]6YP_34959077460083soluble pyridine nucleotide transhydrogenase [ Pseudomonasfluorescens PfO-1]7YP_27408771735155soluble pyridine nucleotide transhydrogenase [ Pseudomonassyringae pv. phaseolicola 1448A]8YP_23498366045142soluble pyridine nucleotide transhydrogenase [ Pseudomonassyringae pv. syringae B728a]9YP_609219104782721soluble pyridine nucleotide transhydrogenase (NAD(P)(+)transhydrogenase [B-specific]) [ Pseudomonas entomophila L48]10Q884I638258471Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])11ZP_009 . . .82739140soluble pyridine nucleotide transhydrogenase [ Pseudomonasputida F1]12YP_57362992113701pyridine nucleotide-disulphide oxidoreductase dimerisationregion [ Chromohalobacter salexigens DSM 3043]13ZP_008 . . .77951906NAD(P) transhydrogenase [ Marinobacter aquaeolei VT8]14YP_43390783645472Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzyme [ Hahella chejuensis KCTC 2396]15ZP_011 . . .89094310soluble pyridine nucleotide transhydrogenase [ Oceanospirillumsp. MED92]16ZP_013 . . .94499566Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzyme [ Oceanobacter sp. RED65]17ZP_011 . . .88800089soluble pyridine nucleotide transhydrogenase [ Reinekea sp.MED297]18ZP_010 . . .87121312soluble pyridine nucleotide transhydrogenase [ Marinomonas sp.MED121]19ZP_012 . . .90417525soluble pyridine nucleotide transhydrogenase [marine gammaproteobacterium HTCC2207]20Q7MQ8347606104Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])21YP_52727790021450regulatory protein, ArsR [ Saccharophagus degradans 2-40]22ZP_009 . . .83586194COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Escherichia coli 101-1]23YP_21900262182585soluble pyridine nucleotide transhydrogenase [ Salmonellaenterica subsp. enterica serovar Choleraesuis str. SC-B67]24YP_54349891213512soluble pyridine nucleotide transhydrogenase [ Escherichia coliUTI89]25Q87KN533301640Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])26YP_15303856415963soluble pyridine nucleotide transhydrogenase [ Salmonellaenterica subsp. enterica serovar Paratyphi A str. ATCC 9150]27YP_672034110644304soluble pyridine nucleotide transhydrogenase [ Escherichia coli536]28ZP_013 . . .106883834FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation region:FAD dependent oxidoreductase[ Psychromonas ingrahamii 37]29ZP_006 . . .75176647COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Shigella boydii BS512]30Q8FB9338258590Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])31ZP_007 . . .75197835COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Escherichia coli HS]32ZP_007 . . .75513852COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Escherichia coli 53638]33Q8X72721362954Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])34YP_26710071278420soluble pyridine nucleotide transhydrogenase [ Colwelliapsychrerythraea 34H]35Q83MI139932373Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])36ZP_007 . . .75238410COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Escherichia coli E110019]37ZP_007 . . .75854141COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Vibrio sp. Ex25]38YP_05232950123162soluble pyridine nucleotide transhydrogenase [ Erwiniacarotovora subsp. atroseptica SCRI1043]39ZP_008 . . .77973002COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Yersinia frederiksenii ATCC 33641]40ZP_008 . . .77957412COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Yersinia bercovieri ATCC 43970]41ZP_008 . . .78702791NAD(P) transhydrogenase (B-specific) [ Alkalilimnicolaehrlichei MLHE-1]42YP_645986108810219soluble pyridine nucleotide transhydrogenase [ Yersinia pestisNepal516]43ZP_007 . . .75828016COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Vibrio cholerae O395]44Q7MBG947606102Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])45ZP_008 . . .77976809COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Yersinia intermedia ATCC 29909]46ZP_008 . . .77961066COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Yersinia mollaretii ATCC 43969]47ZP_010 . . .86148649soluble pyridine nucleotide transhydrogenase [ Vibrio sp.MED222]48YP_20582259713046soluble pyridine nucleotide transhydrogenase [ Vibrio fischeriES114]49ZP_009 . . .84394322pyridine nucleotide-disulfide oxidoreductase, class I [ Vibriosplendidus 12B01]50ZP_011 . . .89074500soluble pyridine nucleotide transhydrogenase [ Photobacteriumsp. SKA34]51YP_15471456459433soluble pyridine nucleotide transhydrogenase [ Idiomarinaloihiensis L2TR]52YP_04688550085375soluble pyridine nucleotide transhydrogenase [ Acinetobacter sp.ADP1]53ZP_012 . . .90581098soluble pyridine nucleotide transhydrogenase [ Vibrio angustumS14]54YP_693290110834431NAD(P) transhydrogenase [ Alcanivorax borkumensis SK2]55ZP_011 . . .88795508soluble pyridine nucleotide transhydrogenase [ Alteromonasmacleodii ‘Deep ecotype’]56ZP_012 . . .90407259soluble pyridine nucleotide transhydrogenase [ Psychromonas sp.CNPT3]57E652037431869probable dehydrogenase (EC 1.8.1.—) udhA - Escherichia coli(strain K-12)58YP_41026082546313putative oxidoreductase [ Shigella boydii Sb227]59YP_31288374314464putative oxidoreductase [ Shigella sonnei Ss046]60YP_13154154310521soluble pyridine nucleotide transhydrogenase [ Photobacteriumprofundum SS9]61AAC43068396309ORF_f444 [ Escherichia coli ]62H8608725284914probable oxidoreductase udhA [imported] - Escherichia coli(strain O157:H7, substrain EDL933)63ZP_012 . . .90414698soluble pyridine nucleotide transhydrogenase [ Photobacteriumprofundum 3TCK]64NP_70976656480495soluble pyridine nucleotide transhydrogenase [ Shigella flexneri2a str. 301]65YP_40523382778884putative oxidoreductase [ Shigella dysenteriae Sd197]66YP_691341110807821putative oxidoreductase [ Shigella flexneri 5 str. 8401]67NP_66766122124238soluble pyridine nucleotide transhydrogenase [ Yersinia pestisKIM]68YP_34137577361800soluble pyridine nucleotide transhydrogenase[ Pseudoalteromonas haloplanktis TAC125]69YP_45583785060135soluble pyridine nucleotide transhydrogenase [ Sodalisglossinidius str. ‘morsitans’]70ZP_012 . . .91771448FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation region:FAD dependent oxidoreductase[ Psychrobacter sp. PRwf-1]71ZP_011 . . .88861405soluble pyridine nucleotide transhydrogenase[ Pseudoalteromonas tunicata D2]72YP_26461771065890soluble pyridine nucleotide transhydrogenase [ Psychrobacterarcticus 273-4]73YP_58030193005864pyridine nucleotide-disulphide oxidoreductase dimerisationregion [ Psychrobacter cryohalolentis K5]74ZP_010 . . .85710769soluble pyridine nucleotide transhydrogenase [ Idiomarina balticaOS145]75ZP_012 . . .91227486soluble pyridine nucleotide transhydrogenase [ Vibrioalginolyticus 12G01]76ZP_007 . . .75814072COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Vibrio cholerae V52]77YP_666832110670275soluble pyridine nucleotide transhydrogenase [ Francisellatularensis subsp. tularensis FSC 198]78YP_16970056707804soluble pyridine nucleotide transhydrogenase [ Francisellatularensis subsp. tularensis SCHU S4]79YP_51367189256309soluble pyridine nucleotide transhydrogenase [ Francisellatularensis subsp. holarctica ]80CAA4682243237udhA [ Escherichia coli ]81ZP_005 . . .67929855FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation region [ Solibacter usitatus Ellin6076]82YP_59229894970250pyridine nucleotide-disulphide oxidoreductase [ Acidobacteriabacterium Ellin345]83NP_96176341408927soluble pyridine nucleotide transhydrogenase [ Mycobacteriumavium subsp. paratuberculosis K-10]84P6600654042093Probable soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])85ZP_007 . . .76783189COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Mycobacterium tuberculosis F11]86YP_716291111225497soluble pyridine nucleotide transhydrogenase [ Frankia alniACN14a]87ZP_005 . . .68235154FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation domain [ Frankia sp. EAN1pec]88ZP_012 . . .90205475FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation region [ Mycobacterium vanbaalenii PYR-1]89YP_48296286742562pyridine nucleotide-disulphide oxidoreductase dimerisationregion [ Frankia sp. CcI3]90NP_53234617935556soluble pyridine nucleotide transhydrogenase [ Agrobacteriumtumefaciens str. C58]91AAY8787368165826pyridine nucleotide-disulfide oxidoreductase class I [ Vibriocholerae ]92AAY8786368165806pyridine nucleotide-disulfide oxidoreductase class I [ Vibriocholerae ]93AAY8786568165810pyridine nucleotide-disulfide oxidoreductase class I [ Vibriocholerae ]94YP_46936586357473probable pyridine nucleotide transhydrogenase protein[ Rhizobium etli CFN 42]95ZP_010 . . .85706062soluble pyridine nucleotide transhydrogenase [ Roseovarius sp.217]96ZP_014 . . .113873124putative soluble pyridine nucleotide transhydrogenase[ Sinorhizobium medicae WSM419]97NP_38583515965482soluble pyridine nucleotide transhydrogenase [ Sinorhizobiummeliloti 1021]98YP_16901656698639soluble pyridine nucleotide transhydrogenase [ Silicibacterpomeroyi DSS-3]99ZP_009 . . .83951172soluble pyridine nucleotide transhydrogenase [ Roseovariusnubinhibens ISM]100YP_61168199078423pyridine nucleotide-disulphide oxidoreductase dimerisationregion [ Silicibacter sp. TM1040]101ZP_010 . . .86140117soluble pyridine nucleotide transhydrogenase [ Roseobacter sp.MED193]102BAB5393914027670soluble pyridine nucleotide transhydrogenase [ Mesorhizobiumloti MAFF303099]103YP_630631108762684NAD(P) transhydrogenase (B-specific) [ Myxococcus xanthusDK 1622]104YP_46703486160249FAD-dependent pyridine nucleotide-disulphide oxidoreductase[ Anaeromyxobacter dehalogenans 2CP-C]105YP_00772446446359soluble pyridine nucleotide transhydrogenase [ CandidatusProtochlamydia amoebophila UWE25]106YP_43330783644872Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzyme [ Hahella chejuensis KCTC 2396]107YP_52798890022161soluble pyridine nucleotide transhydrogenase [ Saccharophagusdegradans 2-40]108ZP_005 . . .67931474FAD-dependent pyridine nucleotide-disulphideoxidoreductase:Pyridine nucleotide-disulphide oxidoreductasedimerisation region [ Solibacter usitatus Ellin6076]109YP_57588792116158Dihydrolipoamide dehydrogenase [ Nitrobacter hamburgensisX14]110NP_53906317986429dihydrolipoamide dehydrogenase [ Brucella melitensis 16M]111NP_69889523502768dihydrolipoamide dehydrogenase [ Brucella suis 1330]112YP_41525882700684Pyridine nucleotide-disulphide oxidoreductase, class-II:NADbinding site:Adrenodoxin reductase:Mercuric reductase:Pyridinenu... [ Brucella melitensis biovar Abortus 2308]113ZP_011 . . .88945707Dihydrolipoamide dehydrogenase [ Desulfotomaculum reducensMI-1]114YP_675936110635728dihydrolipoamide dehydrogenase [ Mesorhizobium sp. BNC1]115YP_48389686747400Dihydrolipoamide dehydrogenase [ Rhodopseudomonas palustrisHaA2]116ZP_006 . . .71836831Dihydrolipoamide dehydrogenase [ Pelobacter propionicus DSM2379]117BAB5098514024381ferric leghemoglobin reductase-2 precursor, dihydrolipoamidedehydrogenase [ Mesorhizobium loti MAFF303099]118ZP_011 . . .88946629Dihydrolipoamide dehydrogenase [ Desulfotomaculum reducensMI-1]119YP_03285449474812dihydrolipoamide dehydrogenase [ Bartonella quintana str.Toulouse]120YP_31704475674623dihydrolipoamide dehydrogenase [ Nitrobacter winogradskyi Nb-255]121ZP_012 . . .904210392-oxoglutarate dehydrogenase, E3 component, lipoamidedehydrogenase [ Aurantimonas sp. SI85-9A1]122NP_53329717936507dihydrolipoamide dehydrogenase [ Agrobacterium tumefaciensstr. C58]123AAR21288384892062-oxoglutarate dehydrogenase E3 component [ Bartonellahenselae ]124YP_03434249476301dihydrolipoamide dehydrogenase [ Bartonella henselae str.Houston-1]125ZP_008 . . .78694497Dihydrolipoamide dehydrogenase [ Bradyrhizobium sp. BTAi1]126ZP_010 . . .85713709dihydrolipoamide dehydrogenase [ Nitrobacter sp. Nb-311A]127YP_47135586359463dihydrolipoamide dehydrogenase protein [ Rhizobium etli CFN42]128ZP_008 . . .77739670Dihydrolipoamide dehydrogenase [ Rhodopseudomonas palustrisBisA53]129NP_38715415966801dihydrolipoamide dehydrogenase [ Sinorhizobium meliloti 1021]130YP_56768991975030Dihydrolipoamide dehydrogenase [ Rhodopseudomonas palustrisBisB5]131ZP_009 . . .83750811COG1249: Pyruvate/2-oxoglutarate dehydrogenase complex,dihydrolipoamide dehydrogenase (E3) component, and relatedenzymes [ Bartonella bacilliformis KC583]132NP_76708927375560dihydrolipoamide dehydrogenase [ Bradyrhizobium japonicumUSDA 110]133ZP_014 . . .113873546dihydrolipoamide dehydrogenase [ Sinorhizobium medicaeWSM419]134ZP_011 . . .88801370Pyruvate/2-oxoglutarate dehydrogenase complex [ Polaribacterirgensii 23-P]135AAN0381722652790dihydrolipoamide dehydrogenase [ Methylobacteriumextorquens ]136NP_94553839933262dihydrolipoamide dehydrogenase [ Rhodopseudomonas palustrisCGA009]137ZP_010 . . .86142639Dihydrolipoyl dehydrogenase [ Flavobacterium sp. MED217]138YP_00566946200002dihydrolipoamide dehydrogenase [ Thermus thermophilus HB27]139ZP_012 . . .90589077Dihydrolipoamide dehydrogenase [ Flavobacterium johnsoniaeUW101]140YP_143553559802562-oxoglutarate dehydrogenase E3 component (dihydrolipoamidedehydrogenase) [ Thermus thermophilus HB8]141YP_679939110639729dihydrolipoyl dehydrogenanse [ Cytophaga hutchinsonii ATCC33406]142YP_53007790421707Dihydrolipoamide dehydrogenase [ Rhodopseudomonas palustrisBisB18]143YP_681916110678909dihydrolipoamide dehydrogenase [ Roseobacter denitrificansOCh 114]144ZP_010 . . .86135035dihydrolipoamide dehydrogenase [ Tenacibaculum sp. MED152]145ZP_011 . . .890681412-oxoglutarate dehydrogenase, E3 component, dihydrolipoamidedehydrogenase [ Oceanicola granulosus HTCC2516]146ZP_007 . . .75761004Dihydrolipoamide dehydrogenase [ Bacillus thuringiensis serovarisraelensis ATCC 35646]147ZP_010 . . .846842432-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Rhodobacterales bacteriumHTCC2654]148ZP_009 . . .845001992-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Oceanicola batsensisHTCC2597]149ZP_006 . . .71900956Dihydrolipoamide dehydrogenase [ Xylella fastidiosa Ann-1]150XP_82973074026328dihydrolipoyl dehydrogenase [ Trypanosoma brucei TREU927]151ZP_010 . . .86132778dihydrolipoamide dehydrogenase [ Cellulophaga sp. MED134]152P7131711135239Soluble pyridine nucleotide transhydrogenase (STH)(NAD(P)(+) transhydrogenase [B-specific])153ZP_012 . . .89891405dihydrolipoyl dehydrogenase (pyruvate 2-oxoglutaratedehydrogenase) [ Flavobacteria bacterium BBFL7]154ZP_009 . . .839504452-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Roseovarius nubinhibens ISM]155AAA21748472330dihydrolipoamide dehydrogenase156Q04933416906Dihydrolipoyl dehydrogenase (Dihydrolipoamidedehydrogenase)157ZP_011 . . .88805521Pyruvate/2-oxoglutarate dehydrogenase complex [ Robiginitaleabiformata HTCC2501]158YP_35139877461891dihydrolipoamide dehydrogenase [ Pseudomonas fluorescensPfO-1]159ZP_006 . . .71900678Dihydrolipoamide dehydrogenase [ Xylella fastidiosa Ann-1]160ZP_011 . . .88936095Dihydrolipoamide dehydrogenase [ Geobacter uraniumreducensRf4]161YP_43060783590598Dihydrolipoamide dehydrogenase [ Moorella thermoaceticaATCC 39073]162YP_165603566952572-oxoglutarate dehydrogenase, E3 component, dihydrolipoamidedehydrogenase [ Silicibacter pomeroyi DSS-3]163ZP_011 . . .89359154Dihydrolipoamide dehydrogenase [ Xanthobacter autotrophicusPy2]164YP_00715046445785dihydrolipoamide dehydrogenase [ Candidatus Protochlamydiaamoebophila UWE25]165YP_632394108758911alpha keto acid dehydrogenase complex, E3 component,lipoamide dehydrogenase [ Myxococcus xanthus DK 1622]166ZP_010 . . .857047992-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Roseovarius sp. 217]167NP_77897828198664dihydrolipoamide dehydrogenase [ Xylella fastidiosa Temecula1]168ZP_011 . . .88949385Dihydrolipoamide dehydrogenase [ Halorhodospira halophilaSL1]169XP_74934570988990dihydrolipoamide dehydrogenase [ Aspergillus fumigatus Af293]170YP_35956778044229alpha keto acid dehydrogenase complex, E3 component,lipoamide dehydrogenase [ Carboxydothermushydrogenoformans Z-2901]171XP_95953585092766hypothetical protein [ Neurospora crassa OR74A]172ZP_009 . . .83856665Dihydrolipoyl dehydrogenase [ Croceibacter atlanticusHTCC2559]173ZP_006 . . .69259929Dihydrolipoamide dehydrogenase [ Magnetococcus sp. MC-1]174NP_29883715838149dihydrolipoamide dehydrogenase [ Xylella fastidiosa 9a5c]175YP_50877989053328Dihydrolipoamide dehydrogenase [ Jannaschia sp. CCS1]176CAA721311854569dihydrolipoamide dehydrogenase [ Trypanosoma cruzi ]177ZP_011 . . .88713490Dihydrolipoyl dehydrogenase [ Flavobacteriales bacteriumHTCC2170]178P905976166121Dihydrolipoyl dehydrogenase (Dihydrolipoamidedehydrogenase)179ZP_009 . . .839444322-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Sulfitobacter sp. EE-36]180ZP_009 . . .839534732-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Sulfitobacter sp. NAS-14.1]181ZP_010 . . .86141935dihydrolipoamide dehydrogenase, E3 component of 2-oxoglutarate and pyruvate dehydrogenase complexes[ Flavobacterium sp. MED217]182XP_81879271663602dihydrolipoyl dehydrogenase [ Trypanosoma cruzi strain CLBrener]183XP_81229471422952dihydrolipoyl dehydrogenase [ Trypanosoma cruzi strain CLBrener]184CAA721321854571dihydrolipoamide dehydrogenase [ Trypanosoma cruzi ]185NP_62327120808100Dihydrolipoamide dehydrogenase/glutathione oxidoreductaseand related enzyme [ Thermoanaerobacter tengcongensis MB4]186YP_26565971082940Dihydrolipoyl dehydrogenase [ Candidatus Pelagibacter ubiqueHTCC1062]187ZP_012 . . .91762636Dihydrolipoyl dehydrogenase [ Candidatus Pelagibacter ubiqueHTCC1002]188CAA1155442103342-oxoglutarate dehydrogenase, E3 subunit [ Arabidopsis thaliana ]189NP_56657030684428LPD2 (LIPOAMIDE DEHYDROGENASE 2); FAD binding/dihydrolipoyl dehydrogenase/disulfide oxidoreductase/oxidoreductase [ Arabidopsis thaliana ]190ZP_010 . . .845158692-oxoglutarate dehydrogenase, E3 component,dihydrolipoamidedehydrogenase [ Loktanella vestfoldensisSKA53]191YP_355777779179622-oxoglutarate dehydrogenase complex, E3 component,lipoamide dehydrogenase [ Pelobacter carbinolicus DSM 2380]192AAS4770844804791dihydrolipoamide dehydrogenase [ Leishmania major ]193AAC260533309269ferric leghemoglobin reductase-2 precursor [ Glycine max ]194XP_71233468487571putative mitochondrial matrix dihydrolipoamide dehydrogenaseLpd1p [ Candida albicans SC5314]195ZP_008 . . .78702525Dihydrolipoamide dehydrogenase [ Alkalilimnicola ehrlicheiMLHE-1]196YP_00240345658317dihydrolipoamide dehydrogenase [ Leptospira interrogans serovarCopenhageni str. Fiocruz L1-130]197ZP_008 . . .82736566Dihydrolipoamide dehydrogenase [ Pseudomonas putida F1]198CAD6073627803033unnamed protein product [ Podospora anserina ]199NP_74746726992042dihydrolipoamide dehydrogenase [ Pseudomonas putida KT2440]200ZP_013 . . .106891371Dihydrolipoamide dehydrogenase [ Roseiflexus sp. RS-1]201EAQ9219288184724conserved hypothetical protein [ Chaetomium globosum CBS148.51] TABLE 32Examples of transhydrogenase subunit alpha polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1NP_41612016129561NAD(P) transhydrogenase subunit alpha [ Escherichia coli K12].2ZP_007 . . .75512964COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli 53638]3ZP_009 . . .83587938COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli 101-1]4YP_669455110641725NAD(P) transhydrogenase subunit alpha [ Escherichia coli 536]5YP_54080091210814NAD(P) transhydrogenase subunit alpha [ Escherichia coliUTI89]6ZP_007 . . .75236686COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli F11]7NP_75389026247850NAD(P) transhydrogenase subunit alpha [ Escherichia coliCFT073]8YP_31049174312072pyridine nucleotide transhydrogenase, alpha subunit [ Shigellasonnei Ss046]9ZP_007 . . .75234916COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli E110019]10YP_40317782776828pyridine nucleotide transhydrogenase, alpha subunit [ Shigelladysenteriae Sd197]11ZP_007 . . .75190643COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli E24377A]12ZP_009 . . .83570993COG3288: NAD/NADP transhydrogenase alpha subunit[ Shigella dysenteriae 1012]13ZP_007 . . .75257022COG3288: NAD/NADP transhydrogenase alpha subunit[ Escherichia coli E22]14YP_40797782544030pyridine nucleotide transhydrogenase, alpha subunit [ Shigellaboydii Sb227]15ZP_006 . . .75178502COG3288: NAD/NADP transhydrogenase alpha subunit[ Shigella boydii BS512]16YP_689096110805576pyridine nucleotide transhydrogenase, alpha subunit [ Shigellaflexneri 5 str. 8401]17NP_31033615831563NAD(P) transhydrogenase subunit alpha [ Escherichia coliO157:H7 str. Sakai]18YP_21648462180067NAD(P) transhydrogenase subunit alpha [ Salmonella entericasubsp. enterica serovar Choleraesuis str. SC-B67]19NP_46043916764824NAD(P) transhydrogenase subunit alpha [ Salmonellatyphimurium LT2]20NP_80519429141852NAD(P) transhydrogenase subunit alpha [ Salmonella entericasubsp. enterica serovar Typhi Ty2]21ABF71058102621428NADP transhydrogenase alpha subunit [ Enterobacter cloacae ]22ZP_008 . . .77963333COG3288: NAD/NADP transhydrogenase alpha subunit[ Yersinia mollaretii ATCC 43969]23ZP_008 . . .77958020COG3288: NAD/NADP transhydrogenase alpha subunit[ Yersinia bercovieri ATCC 43970]24ZP_008 . . .77975377COG3288: NAD/NADP transhydrogenase alpha subunit[ Yersinia frederiksenii ATCC 33641]25YP_647693108811926NAD(P) transhydrogenase alpha subunit [ Yersinia pestisNepal516]26YP_07074051596549NAD(P) transhydrogenase subunit alpha [ Yersiniapseudotuberculosis IP 32953]27ZP_007 . . .77629299COG3288: NAD/NADP transhydrogenase alpha subunit[ Yersinia pseudotuberculosis IP 31758]28YP_05029750121130NAD(P) transhydrogenase subunit alpha [ Erwinia carotovorasubsp. atroseptica SCRI1043]29ZP_008 . . .77979498COG3288: NAD/NADP transhydrogenase alpha subunit[ Yersinia intermedia ATCC 29909]30NP_92942737526083NAD(P) transhydrogenase subunit alpha [ Photorhabdusluminescens subsp. laumondii TTO1]31YP_45516885059466pyridine nucleotide transhydrogenase alpha subunit [ Sodalisglossinidius str. ‘morsitans’]32YP_20654459713769NAD(P) transhydrogenase subunit alpha [ Vibrio fischeri ES114]33ZP_007 . . .75831475COG3288: NAD/NADP transhydrogenase alpha subunit [ Vibriocholerae MO10]34ZP_010 . . .86147993NAD(P) transhydrogenase subunit alpha [ Vibrio sp. MED222]35ZP_009 . . .84393928NAD(P) transhydrogenase subunit alpha [ Vibrio splendidus12B01]36ZP_007 . . .75857576COG3288: NAD/NADP transhydrogenase alpha subunit [ Vibriosp. Ex25]37ZP_012 . . .91226112NAD(P) transhydrogenase subunit alpha [ Vibrio alginolyticus12G01]38NP_93686837676472NAD(P) transhydrogenase subunit alpha [ Vibrio vulnificusYJ016]39NP_80043228900777NAD(P) transhydrogenase subunit alpha [ Vibrioparahaemolyticus RIMD 2210633]40NP_76228727366760NAD(P) transhydrogenase subunit alpha [ Vibrio vulnificusCMCP6]41ZP_012 . . .90577759NAD(P) transhydrogenase subunit alpha [ Vibrio angustum S14]42ZP_011 . . .89073747NAD(P) transhydrogenase subunit alpha [ Photobacterium sp.SKA34]43NP_24569015602618NAD(P) transhydrogenase subunit alpha [ Pasteurella multocidasubsp. multocida str. Pm70]44YP_08841652425279NAD(P) transhydrogenase subunit alpha [ Mannheimiasucciniciproducens MBEL55E]45YP_718440113460378NAD(P)(+) transhydrogenase, alpha subunit (pyridinenucleotide transhydrogenase) [ Haemophilus somnus 129PT]46ZP_001 . . .32030098COG3288: NAD/NADP transhydrogenase alpha subunit[ Haemophilus somnus 2336]47ZP_005 . . .68545628NAD(P) transhydrogenase, alpha subunit [ Shewanellaamazonensis SB2B]48ZP_012 . . .90412639NAD(P) transhydrogenase subunit alpha [ Photobacteriumprofundum 3TCK]49ZP_007 . . .75429914NAD/NADP transhydrogenase alpha subunit [ Actinobacillussuccinogenes 130Z]50YP_24923568250123NAD(P) transhydrogenase subunit alpha [ Haemophilusinfluenzae 86-028NP]51YP_13257454302581NAD(P) transhydrogenase subunit alpha [ Photobacteriumprofundum SS9]52NP_43951316273272NAD(P) transhydrogenase subunit alpha [ Haemophilusinfluenzae Rd KW20]53ZP_009 . . .82741968NAD(P) transhydrogenase, alpha subunit [ Shewanella sp. W3-18-1]54ZP_014 . . .113949477NAD(P) transhydrogenase, alpha subunit [ Shewanella balticaOS195]55YP_56194291792291NAD(P) transhydrogenase, alpha subunit [ Shewanelladenitrificans OS217]56NP_71927924375236NAD(P) transhydrogenase subunit alpha [ Shewanella oneidensisMR-1]57NP_87404633152693NAD(P) transhydrogenase subunit alpha [ Haemophilus ducreyi35000HP]58YP_735209113971416NAD(P) transhydrogenase, alpha subunit [ Shewanella sp. MR-4]59ZP_008 . . .78686308NAD(P) transhydrogenase, alpha subunit [ Shewanella sp. ANA-3]60YP_736947114046397NAD(P) transhydrogenase, alpha subunit [ Shewanella sp. MR-7]61ZP_006 . . .69950756NAD(P) transhydrogenase, alpha subunit [ Shewanellafrigidimarina NCIMB 400]62ZP_007 . . .75818840COG3288: NAD/NADP transhydrogenase alpha subunit [ Vibriocholerae V51]63ZP_013 . . .106883669NAD(P) transhydrogenase, alpha subunit [ Psychromonasingrahamii 37]64NP_28394415794122NAD(P) transhydrogenase subunit alpha [ Neisseria meningitidisZ2491]65YP_43423683645801NAD(P) transhydrogenase, alpha subunit [ Hahella chejuensisKCTC 2396]66NP_27401715676872NAD(P) transhydrogenase subunit alpha [ Neisseria meningitidisMC58]67YP_20852259801810NAD(P) transhydrogenase subunit alpha [ Neisseria gonorrhoeaeFA 1090]68ZP_012 . . .90408904PntA [ Psychromonas sp. CNPT3]69YP_26851471281713NAD(P) transhydrogenase subunit alpha [ Colwelliapsychrerythraea 34H]70ZP_001 . . .32035329COG3288: NAD/NADP transhydrogenase alpha subunit[ Actinobacillus pleuropneumoniae serovar 1 str. 4074]71ZP_012 . . .90202099NAD(P) transhydrogenase, alpha subunit [ Mycobacteriumvanbaalenii PYR-1]72YP_34232277163797NAD(P) transhydrogenase subunit alpha [ Nitrosococcus oceaniATCC 19707]73ZP_009 . . .84495285NAD(P) transhydrogenase subunit alpha [ Janibacter sp.HTCC2649]74AAY8775568165590NAD(P) transhydrogenase alpha subunit [ Vibrio cholerae ]75ZP_011 . . .89340414NAD(P) transhydrogenase, alpha subunit [ Mycobacteriumflavescens PYR-GCK]76AAY8775168165582NAD(P) transhydrogenase alpha subunit [ Vibrio cholerae ]77AAY8775468165588NAD(P) transhydrogenase alpha subunit [ Vibrio cholerae ]78AAY8776268165604NAD(P) transhydrogenase alpha subunit [ Vibrio cholerae ]79YP_42218783311923NAD/NADP transhydrogenase alpha subunit [ Magnetospirillummagneticum AMB-1]80YP_637279108797082NAD(P) transhydrogenase, alpha subunit [ Mycobacterium sp.MCS]81YP_11516553803088NAD(P) transhydrogenase subunit alpha [ Methylococcuscapsulatus str. Bath]82NP_82157829826944NAD(P) transhydrogenase subunit alpha [ Streptomycesavermitilis MA-4680]83ZP_006 . . .69261416NAD(P) transhydrogenase, alpha subunit [ Magnetococcus sp.MC-1]84NP_44085616330128NAD(P) transhydrogenase subunit alpha [ Synechocystis sp.PCC 6803]85ZP_002 . . .46202292COG3288: NAD/NADP transhydrogenase alpha subunit[ Magnetospirillum magnetotacticum MS-1]86YP_29886073538493NAD(P) transhydrogenase subunit alpha [ Ralstonia eutrophaJMP134]87ZP_004 . . .66966825NAD(P) transhydrogenase, alpha subunit [ Arthrobacter sp.FB24]88ZP_006 . . .71366730NAD(P) transhydrogenase, alpha subunit [ Nocardioides sp.JS614]89YP_52498589902514NAD(P) transhydrogenase, alpha subunit [ Rhodoferaxferrireducens T118]90YP_05533950842112NAD(P) transhydrogenase subunit alpha [ Propionibacteriumacnes KPA171202]91NP_63166421225885NAD(P) transhydrogenase subunit alpha [ Streptomycescoelicolor A3(2)]92ZP_006 . . .74018096NAD(P) transhydrogenase, alpha subunit [ Burkholderiaambifaria AMMD]93CAJ96500113530153NAD(P) transhydrogenase subunit alpha [ Ralstonia eutrophaH16]94YP_36691678060341NAD(P) transhydrogenase subunit alpha [ Burkholderia sp. 383]95YP_57453892114610NAD(P) transhydrogenase, alpha subunit [ Chromohalobactersalexigens DSM 3043]96ZP_004 . . .67542770NAD(P) transhydrogenase, alpha subunit [ Burkholderiavietnamiensis G4]97YP_702683111019711NAD(P) transhydrogenase alpha subunit [ Rhodococcus sp.RHA1]98ZP_007 . . .75821435COG3288: NAD/NADP transhydrogenase alpha subunit [ Vibriocholerae RC385]99ZP_011 . . .88798022NAD(P) transhydrogenase subunit alpha [ Reinekea sp.MED297]100ZP_009 . . .83371049NAD(P) transhydrogenase, alpha subunit [ Rhodobactersphaeroides ATCC 17025]101ZP_006 . . .69933435NAD(P) transhydrogenase, alpha subunit [ Paracoccusdenitrificans PD1222]102YP_35331377463809NAD(P) transhydrogenase subunit alpha [ Rhodobactersphaeroides 2.4.1]103ZP_009 . . .83373326NAD(P) transhydrogenase, alpha subunit [ Rhodobactersphaeroides ATCC 17029]104ZP_010 . . .85704984NAD(P) transhydrogenase subunit alpha [ Roseovarius sp. 217]105YP_61270399080549NAD(P) transhydrogenase, alpha subunit [ Silicibacter sp.TM1040]106YP_683504110680497NAD(P) transhydrogenase, alpha subunit [ Roseobacterdenitrificans OCh 114]107AAQ8736936958944NAD(P) transhydrogenase subunit alpha [ Rhizobium sp.NGR234]108ZP_010 . . .86137634NAD(P) transhydrogenase subunit alpha [ Roseobacter sp.MED193]109XP_79912772030333PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Strongylocentrotus purpuratus ]110ZP_010 . . .84503572NAD(P) transhydrogenase subunit alpha [ Oceanicola batsensisHTCC2597]111ZP_010 . . .84516763NAD(P) transhydrogenase subunit alpha [ Loktanellavestfoldensis SKA53]112NP_53316417936374NAD(P) transhydrogenase subunit alpha [ Agrobacteriumtumefaciens str. C58]113XP_56293757968100ENSANGP00000025507 [ Anopheles gambiae str. PEST]114YP_51122489055773NAD(P) transhydrogenase, alpha subunit [ Jannaschia sp. CCS1]115ZP_009 . . .83942708NAD(P) transhydrogenase subunit alpha [ Sulfitobacter sp. EE-36]116YP_16802856697658NAD(P) transhydrogenase subunit alpha [ Silicibacter pomeroyiDSS-3]117EAT35199108870974nadp transhydrogenase [ Aedes aegypti ]118ZP_009 . . .83953947NAD(P) transhydrogenase subunit alpha [ Sulfitobacter sp. NAS-14.1]119ZP_009 . . .83949483NAD(P) transhydrogenase subunit alpha [ Roseovariusnubinhibens ISM]120XP_36762839972475hypothetical protein MG07539.4 [ Magnaporthe grisea 70-15]121NP_99992147550793nicotinamide nucleotide transhydrogenase [ Danio rerio ]122XP_96104785100871hypothetical protein (mitochondrial nicotinamide nucleotidetranshydrogenase-related protein [imported] - Neurospora crassaOR74A)123AAH8111751703526MGC83563 protein [ Xenopus laevis ]124CAF9932247223713unnamed protein product [ Tetraodon nigroviridis ]125CAB8857216416047related to mitochondrial nicotinamide nucleotidetranshydrogenase [ Neurospora crassa ]126AAI1054483405154Nicotinamide nucleotide transhydrogenase [ Homo sapiens ]127AAI1054583405537Nicotinamide nucleotide transhydrogenase [ Homo sapiens ]128NP_50902817550456Nicotinamide Nucleotide Transhydrogenase family member(nnt-1) [ Caenorhabditis elegans ]1292211247B1589396nicotinamide nucleotide transhydrogenase130ZP_010 . . .84686399NAD(P) transhydrogenase subunit alpha [ Rhodobacteralesbacterium HTCC2654]131NP_77636827806831nicotinamide nucleotide transhydrogenase [ Bos taurus ]132AAA21440163397nicotinamide nucleotide transhydrogenase133P11024128400NAD(P) transhydrogenase, mitochondrial precursor (Pyridinenucleotide transhydrogenase) (Nicotinamide nucleotidetranshydrogenase)134XP_53648173953769PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 1 [ Canisfamiliaris ]135XP_97038291083631PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Tribolium castaneum ]136NP_001 . . .61557127nicotinamide nucleotide transhydrogenase [ Rattus norvegicus ]137NP_89202233695086nicotinamide nucleotide transhydrogenase [ Homo sapiens ]138XP_86792873953777PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 5 [ Canisfamiliaris ]139NP_03647533695084nicotinamide nucleotide transhydrogenase [ Homo sapiens ]140XP_42478450761621PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Gallus gallus ]141XP_64684066826971NAD(P)+ transhydrogenase (AB-specific) [ Dictyosteliumdiscoideum AX4]142BAC4011326352966unnamed protein product [ Mus musculus ]143EAS3157090301939conserved hypothetical protein [ Coccidioides immitis RS]144XP_86792273953775PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 4 [ Canisfamiliaris ]145CAF9985647230663unnamed protein product [ Tetraodon nigroviridis ]146Q6194151338804NAD(P) transhydrogenase, mitochondrial precursor (Pyridinenucleotide transhydrogenase) (Nicotinamide nucleotidetranshydrogenase)1472211247A1589395nicotinamide nucleotide transhydrogenase148NP_03273631543330nicotinamide nucleotide transhydrogenase [ Mus musculus ]149BAE3529474198248unnamed protein product [ Mus musculus ]150XP_74806470985116nicotinamide nucleotide transhydrogenase [ Aspergillusfumigatus Af293]151XP_38918246130902hypothetical protein FG09006.1 [ Gibberella zeae PH-1]152CAE6887539598183Hypothetical protein CBG14838 [ Caenorhabditis briggsae ]153AAK1817913310152nicotinamide nucleotide transhydrogenase [ Acetabulariaacetabulum ]154AAG0224611597233NAD(P)H transhydrogenase [ Acetabularia acetabulum ]155AAC415776478876pyridine nucleotidetranshydrogenase [ Entamoeba histolytica ]156XP_62713666359916pyridine nucleotide/NAD(P) transhydrogenase alpha plus betasubunits, duplicated gene, [ Cryptosporidium parvum Iowa II]157XP_66649567602649transhydrogenase 7B2 [ Cryptosporidium hominis TU502]158BAE4057774219995unnamed protein product [ Mus musculus ]159CAH9007955726630hypothetical protein [ Pongo pygmaeus ]160AAA80188571367nicotinamide nucleotide transhydrogenase161EAQ8642488178956conserved hypothetical protein [ Chaetomium globosum CBS148.51]162AAA29077305062transhydrogenase163AAA29081158904transhydrogenase164YP_724141113478080NAD(P)(+) transhydrogenase (AB-specific) [ Trichodesmiumerythraeum IMS101]165NP_48745017230902nicotinamide nucleotide transhydrogenase, subunit alpha[ Nostoc sp. PCC 7120]166YP_32393275909636Alanine dehydrogenase/PNT-like [ Anabaena variabilis ATCC29413]167ZP_005 . . .67924536NAD(P)(+) transhydrogenase (AB-specific) [ Crocosphaerawatsonii WH 8501]168ZP_013 . . .110607624Alanine dehydrogenase/PNT-like [ Maricaulis maris MCS10]169ZP_012 . . .91222948NAD(P) transhydrogenase subunit alpha [ Psychroflexus torquisATCC 700755]170ZP_009 . . .82737423NAD/NADP transhydrogenase, NAD(H)-binding DI subunit[ Pseudomonas putida F1]171YP_00004645655960proton-translocating transhydrogenase, subunit alpha part 1[ Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130]172YP_25726770733627NAD(P) transhydrogenase, alpha subunit part 1 [ Pseudomonasfluorescens Pf-5]173ZP_001 . . .23130320COG3288: NAD/NADP transhydrogenase alpha subunit[ Nostoc punctiforme PCC 73102]174ZP_013 . . .110593183NAD(P)(+) transhydrogenase (AB-specific) [ Acidovorax sp.JS42]175ZP_009 . . .83859916nicotinamide nucleotide transhydrogenase, subunit[ Oceanicaulis alexandrii HTCC2633]176YP_52643090020603Glycogen/starch/alpha-glucan phosphorylase [ Saccharophagusdegradans 2-40]177ZP_012 . . .89362826nicotinamide nucleotide transhydrogenase, subunit alpha1[ Xanthobacter autotrophicus Py2]178YP_27717571737873NAD(P) transhydrogenase, subunit alpha part 1 [ Pseudomonassyringae pv. phaseolicola 1448A]179YP_23808166048240Alanine dehydrogenase/PNT, C-terminal:Alaninedehydrogenase/PNT, N-terminal [ Pseudomonas syringae pv.syringae B728a]180YP_675347110635139alanine dehydrogenase/PNT-like [ Mesorhizobium sp. BNC1]181YP_34584777456342NAD(P)(+) transhydrogenase (AB-specific) [ Pseudomonasfluorescens PfO-1]182AAQ8723736958769NAD(P) transhydrogenase subunit alpha [ Rhizobium sp.NGR234]183ZP_013 . . .94499798pyridine nucleotide transhydrogenase alpha subunit[ Oceanobacter sp. RED65]184NP_88148133593837NAD(P) transhydrogenase, subunit alpha part 1 [ Bordetellapertussis Tohama I]185P0C18691207608NAD(P) transhydrogenase subunit alpha part 1 (Pyridinenucleotide transhydrogenase subunit alpha 1) (Nicotinamidenucleotide transhydrogenase subunit alpha 1) (Proton-translocating transhydrogenase component 1) (dI)1861PTJB37927621Chain B, Crystal Structure Analysis Of The Di And DiiiComplex Of Transhydrogenase With A Thio-NicotinamideNucleotide Analogue187YP_48505686748560NAD(P)(+) transhydrogenase (AB-specific)[ Rhodopseudomonas palustris HaA2]188YP_620103107021776alanine dehydrogenase/PNT-like [ Burkholderia cenocepacia AU1054]189ZP_008 . . .77952426pyridine nucleotide transhydrogenase alpha subunit[ Marinobacter aquaeolei VT8]190NP_84093330248863Alanine dehydrogenase and pyridine nucleotidetranshydrogenase [ Nitrosomonas europaea ATCC 19718]1912FRDB90109601Chain B, Structure Of Transhydrogenase(Di.S138a.Nadh)2(Diii.Nadph)1 Asymmetric Complex192NP_88849133600931NAD(P) transhydrogenase, subunit alpha part 1 [ Bordetellabronchiseptica RB50]193XP_72644782596885NAD(P) transhydrogenase subunit beta [ Plasmodium yoeliiyoelii str. 17XNL]194YP_55132991790377NAD(P)(+) transhydrogenase (AB-specific) [ Polaromonas sp.JS666]195ZP_006 . . .71548985NAD(P)(+) transhydrogenase (AB-specific) [ Nitrosomonaseutropha C71]196YP_56855391975894NAD(P)(+) transhydrogenase (AB-specific)[ Rhodopseudomonas palustris BisB5]1972FSVB90109621Chain B, Structure Of Transhydrogenase (Di.D135n.Nad+)2(Diii.E155w.Nadp+)1 Asymmetric Complex1981NM5B42543078Chain B, R. Rubrum Transhydrogenase (Di.Q132n)2(Diii)1Asymmetric Complex1991L7DB27065343Chain B, Crystal Structure Of R. Rubrum TranshydrogenaseDomain I Without Bound Nad(H)200ZP_012 . . .90418769NAD(P) transhydrogenase, subunit alpha part 1 [ Aurantimonassp. SI85-9A1]2012FR8B90109598Chain B, Structure Of Transhydrogenase(Di.R127a.Nad+)2(Diii.Nadp+)1 Asymmetric Complex TABLE 33Examples of transhydrogenase subunit beta polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1NP_41611916129560pyridine nucleotide transhydrogenase [ Escherichia coli K12].2YP_669454110641724NAD(P) transhydrogenase subunit beta [ Escherichia coli 536]3ZP_007 . . .75234915COG1282: NAD/NADP transhydrogenase beta subunit[ Escherichia coli E110019]4ZP_007 . . .75230949COG1282: NAD/NADP transhydrogenase beta subunit[ Escherichia coli B7A]5YP_40797882544031pyridine nucleotide transhydrogenase, beta subunit [ Shigellaboydii Sb227]6YP_15063056413555pyridine nucleotide transhydrogenase [ Salmonella entericasubsp. enterica serovar Paratyphi A str. ATCC 9150]7YP_21648562180068pyridine nucleotide transhydrogenase [ Salmonella entericasubsp. enterica serovar Choleraesuis str. SC-B67]8ABF71059102621429NADP transhydrogenase beta subunit [ Enterobacter cloacae ]9NP_92942837526084pyridine nucleotide transhydrogenase [ Photorhabdusluminescens subsp. laumondii TTO1]10YP_05029850121131pyridine nucleotide transhydrogenase [ Erwinia carotovorasubsp. atroseptica SCRI1043]11ZP_008 . . .77979497COG1282: NAD/NADP transhydrogenase beta subunit[ Yersinia intermedia ATCC 29909]12ZP_008 . . .77975378COG1282: NAD/NADP transhydrogenase beta subunit[ Yersinia frederiksenii ATCC 33641]13ZP_008 . . .77958019COG1282: NAD/NADP transhydrogenase beta subunit[ Yersinia bercovieri ATCC 43970]14ZP_008 . . .77963332COG1282: NAD/NADP transhydrogenase beta subunit[ Yersinia mollaretii ATCC 43969]15YP_647692108811925NAD(P) transhydrogenase subunit beta [ Yersinia pestisNepal516]16YP_45516785059465pyridine nucleotide transhydrogenase beta subunit [ Sodalisglossinidius str. ‘morsitans’]17NP_71928024375237pyridine nucleotide transhydrogenase [ Shewanella oneidensisMR-1]18YP_736946114046396NAD(P) transhydrogenase, beta subunit [ Shewanella sp. MR-7]19ZP_009 . . .82741967NAD(P) transhydrogenase, beta subunit [ Shewanella sp. W3-18-1]20NP_24568915602617pyridine nucleotide transhydrogenase [ Pasteurella multocidasubsp. multocida str. Pm70]21ZP_005 . . .68541685NAD(P) transhydrogenase, beta subunit [ Shewanella balticaOS155]22ZP_012 . . .90412640putative NAD(P) transhydrogenase, beta subunit[ Photobacterium profundum 3TCK]23ZP_001 . . .53732668COG1282: NAD/NADP transhydrogenase beta subunit[ Haemophilus influenzae R2846]24YP_24923468250122pyridine nucleotide transhydrogenase [ Haemophilus influenzae86-028NP]25NP_43951416273273pyridine nucleotide transhydrogenase [ Haemophilus influenzaeRd KW20]26ZP_005 . . .68545629NAD(P) transhydrogenase, beta subunit [ Shewanellaamazonensis SB2B]27YP_13257554302582pyridine nucleotide transhydrogenase [ Photobacteriumprofundum SS9]28ZP_011 . . .89073748pyridine nucleotide transhydrogenase [ Photobacterium sp.SKA34]29NP_80043128900776pyridine nucleotide transhydrogenase [ Vibrio parahaemolyticusRIMD 2210633]30ZP_012 . . .90577760pyridine nucleotide transhydrogenase [ Vibrio angustum S14]31ZP_007 . . .75857577COG1282: NAD/NADP transhydrogenase beta subunit [ Vibriosp. Ex25]32NP_93686737676471pyridine nucleotide transhydrogenase [ Vibrio vulnificus YJ016]33ZP_007 . . .75818461COG1282: NAD/NADP transhydrogenase beta subunit [ Vibriocholerae V51]34ZP_007 . . .75831476COG1282: NAD/NADP transhydrogenase beta subunit [ Vibriocholerae MO10]35ZP_012 . . .91226113pyridine nucleotide transhydrogenase [ Vibrio alginolyticus12G01]36YP_20654359713768pyridine nucleotide transhydrogenase [ Vibrio fischeri ES114]37YP_08841552425278pyridine nucleotide transhydrogenase [ Mannheimiasucciniciproducens MBEL55E]38ZP_001 . . .32035330COG1282: NAD/NADP transhydrogenase beta subunit[ Actinobacillus pleuropneumoniae serovar 1 str. 4074]39ZP_006 . . .69950757NAD(P) transhydrogenase, beta subunit [ Shewanellafrigidimarina NCIMB 400]40ZP_010 . . .86147992pyridine nucleotide transhydrogenase [ Vibrio sp. MED222]41ZP_009 . . .84393927NAD(P) transhydrogenase, beta subunit [ Vibrio splendidus12B01]42ZP_007 . . .75429915NAD/NADP transhydrogenase beta subunit [ Actinobacillussuccinogenes 130Z]43NP_27401515676870pyridine nucleotide transhydrogenase [ Neisseria meningitidisMC58]44NP_28394215794120pyridine nucleotide transhydrogenase [ Neisseria meningitidisZ2491]45YP_20852459801812pyridine nucleotide transhydrogenase [ Neisseria gonorrhoeaeFA 1090]46YP_718441113460379NAD(P)(+) transhydrogenase, beta subunit (pyridine nucleotidetranshydrogenase) [ Haemophilus somnus 129PT]47NP_87404533152692pyridine nucleotide transhydrogenase [ Haemophilus ducreyi35000HP]48YP_56194191792290NAD(P) transhydrogenase, beta subunit [ Shewanelladenitrificans OS217]49YP_43423583645800NAD/NADP transhydrogenase beta subunit [ Hahella chejuensisKCTC 2396]50YP_26851571280969pyridine nucleotide transhydrogenase [ Colwelliapsychrerythraea 34H]51ZP_013 . . .106883670NAD(P) transhydrogenase, beta subunit [ Psychromonasingrahamii 37]52ZP_009 . . .84495284pyridine nucleotide transhydrogenase [ Janibacter sp.HTCC2649]53YP_637278108797081NAD(P) transhydrogenase, beta subunit [ Mycobacterium sp.MCS]54ZP_012 . . .90408905NAD(P) transhydrogenase subunit beta [ Psychromonas sp.CNPT3]55ZP_011 . . .89340413NAD(P) transhydrogenase, beta subunit [ Mycobacteriumflavescens PYR-GCK]56ZP_012 . . .90202100NAD(P) transhydrogenase, beta subunit [ Mycobacteriumvanbaalenii PYR-1]57NP_63166321225884NAD(P) transhydrogenase beta subunit [ Streptomycescoelicolor A3(2)]58NP_82157729826943pyridine nucleotide transhydrogenase, beta subunit[ Streptomyces avermitilis MA-4680]59YP_702682111019710NAD(P) transhydrogenase beta subunit [ Rhodococcus sp.RHA1]60YP_42218683311922NAD/NADP transhydrogenase beta subunit [ Magnetospirillummagneticum AMB-1]61ZP_006 . . .71366731NAD(P) transhydrogenase, beta subunit [ Nocardioides sp.JS614]62YP_11516453803089NAD(P) transhydrogenase, beta subunit [ Methylococcuscapsulatus str. Bath]63YP_52498489902513NAD(P) transhydrogenase, beta subunit [ Rhodoferaxferrireducens T118]64NP_44086016330132pyridine nucleotide transhydrogenase beta subunit[ Synechocystis sp. PCC 6803]65ZP_004 . . .66966824NAD(P) transhydrogenase, beta subunit [ Arthrobacter sp. FB24]66ZP_011 . . .88798021pyridine nucleotide transhydrogenase [ Reinekea sp. MED297]67YP_34232177163796NAD(P) transhydrogenase, beta subunit [ Nitrosococcus oceaniATCC 19707]68ZP_006 . . .69261415NAD(P) transhydrogenase, beta subunit [ Magnetococcus sp.MC-1]69ZP_004 . . .67542769NAD(P) transhydrogenase, beta subunit [ Burkholderiavietnamiensis G4]70YP_36691578060340NAD(P) transhydrogenase, beta subunit [ Burkholderia sp. 383]71ZP_006 . . .74018097NAD(P) transhydrogenase, beta subunit [ Burkholderia ambifariaAMMD]72YP_29885973538492NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]73YP_05534050842113NAD(P) transhydrogenase subunit beta [ Propionibacteriumacnes KPA171202]74ZP_009 . . .83949482NAD(P)+ transhydrogenase, beta subunit [ Roseovariusnubinhibens ISM]75CAJ96499113530152NAD(P) transhydrogenase subunit beta [ Ralstonia eutrophaH16]76ZP_006 . . .69933434NAD(P) transhydrogenase, beta subunit [ Paracoccusdenitrificans PD1222]77YP_16802756697657NAD(P)+ transhydrogenase, beta subunit [ Silicibacter pomeroyiDSS-3]78NP_53316517936375NAD(P)+ transhydrogenase beta chain [ Agrobacteriumtumefaciens str. C58]79AAQ8737036958945NAD(P) transhydrogenase subunit beta [ Rhizobium sp.NGR234]80ZP_009 . . .83942707NAD(P)+ transhydrogenase, beta subunit [ Sulfitobacter sp. EE-36]81ZP_009 . . .83953946NAD(P)+ transhydrogenase, beta subunit [ Sulfitobacter sp.NAS-14.1]82ZP_007 . . .75813705COG1282: NAD/NADP transhydrogenase beta subunit [ Vibriocholerae V52]83ZP_010 . . .84503573NAD(P)+ transhydrogenase, beta subunit [ Oceanicola batsensisHTCC2597]84ZP_010 . . .84686400NAD(P)+ transhydrogenase, beta subunit [ Rhodobacteralesbacterium HTCC2654]85YP_61270299080548NAD(P) transhydrogenase, beta subunit [ Silicibacter sp.TM1040]86ZP_010 . . .84516762NAD(P)+ transhydrogenase, beta subunit [ Loktanellavestfoldensis SKA53]87ZP_010 . . .86137633NAD(P)+ transhydrogenase, beta subunit [ Roseobacter sp.MED193]88YP_51122389055772NAD(P) transhydrogenase, beta subunit [ Jannaschia sp. CCS1]89ZP_010 . . .85704983NAD(P)+ transhydrogenase, beta subunit [ Roseovarius sp. 217]90ZP_007 . . .75822802COG1282: NAD/NADP transhydrogenase beta subunit [ Vibriocholerae RC385]91YP_683503110680496NAD(P) transhydrogenase, beta subunit [ Roseobacterdenitrificans OCh 114]92NP_94951639937240nicotinamide nucleotide transhydrogenase, subunit beta[ Rhodopseudomonas palustris CGA009]93YP_41847883269187NAD(P) transhydrogenase, beta subunit [ Brucella melitensisbiovar Abortus 2308]94YP_48505886748562NAD(P) transhydrogenase, beta subunit [ Rhodopseudomonaspalustris HaA2]95ZP_009 . . .83859918nicotinamide nucleotide transhydrogenase, subunit beta[ Oceanicaulis alexandrii HTCC2633]96ZP_008 . . .77740973NAD(P) transhydrogenase, beta subunit [ Rhodopseudomonaspalustris BisA53]97ZP_012 . . .89362731NAD(P) transhydrogenase, beta subunit [ Xanthobacterautotrophicus Py2]98ZP_008 . . .77814001NAD(P) transhydrogenase, beta subunit [ Shewanellaputrefaciens CN-32]99ZP_010 . . .84704197PntB, NAD(P) transhydrogenase, beta subunit [ Parvularculabermudensis HTCC2503]100YP_53381190425441NAD(P) transhydrogenase, beta subunit [ Rhodopseudomonaspalustris BisB18]101P0C18891207612NAD(P) transhydrogenase subunit beta (Pyridine nucleotidetranshydrogenase subunit beta) (Nicotinamide nucleotidetranshydrogenase subunit beta) (Proton-translocatingtranshydrogenase NADP(H)-binding component) (dIII)102YP_56855591975896NAD(P) transhydrogenase, beta subunit [ Rhodopseudomonaspalustris BisB5]103ZP_012 . . .90418771NAD(P) transhydrogenase, subunit beta [ Aurantimonas sp.SI85-9A1]104YP_52643290020605NAD(P) transhydrogenase, beta subunit [ Saccharophagusdegradans 2-40]105ZP_008 . . .78699497NAD(P)+ transhydrogenase beta chain [ Bradyrhizobium sp.BTAi1]106XP_42478450761621PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Gallus gallus ]107XP_79912772030333PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Strongylocentrotus purpuratus ]108ZP_010 . . .85716091NAD/NADP transhydrogenase beta subunit [ Nitrobacter sp. Nb-311A]109YP_605919104779421pyridine nucleotide transhydrogenase, beta subunit[ Pseudomonas entomophila L48]110YP_45735985373297PntB, NAD(P) transhydrogenase, beta subunit [ Erythrobacterlitoralis HTCC2594]111XP_97038291083631PREDICTED: similar to nicotinamide nucleotidetranshydrogenase [ Tribolium castaneum ]112BAB5167714025075nicotinamide nucleotide transhydrogenase, subunit beta[ Mesorhizobium loti MAFF303099]113ZP_012 . . .94413536hypothetical protein PaerP_01004711 [ Pseudomonas aeruginosaPA7]114ZP_011 . . .88938736NAD/NADP transhydrogenase beta subunit-like [ Acidiphiliumcryptum JF-5]115NP_79518828872569NAD(P) transhydrogenase, beta subunit [ Pseudomonas syringaepv. tomato str. DC3000]116YP_25726570733625NAD(P) transhydrogenase, beta subunit [ Pseudomonasfluorescens Pf-5]117NP_77376427382235NAD(P)+ transhydrogenase beta chain [ Bradyrhizobiumjaponicum USDA 110]118YP_57651792116788NAD(P) transhydrogenase, beta subunit [ Nitrobacterhamburgensis X14]119ZP_013 . . .107099186hypothetical protein PaerPA_01000196 [ Pseudomonasaeruginosa PACS2]120YP_55704591781839Putative NAD(P) transhydrogenase, beta subunit [ Burkholderiaxenovorans LB400]121ZP_009 . . .82737421pyridine nucleotide transhydrogenase, beta subunit[ Pseudomonas putida F1]122YP_34584577456340NAD(P) transhydrogenase, beta subunit [ Pseudomonasfluorescens PfO-1]123NP_99992147550793nicotinamide nucleotide transhydrogenase [ Danio rerio ]124YP_41184882702282NAD(P) transhydrogenase, beta subunit [ Nitrosospiramultiformis ATCC 25196]125CAF9985647230663unnamed protein product [ Tetraodon nigroviridis ]126YP_675345110635137NAD(P) transhydrogenase, beta subunit [ Mesorhizobium sp.BNC1]127EAT35199108870974nadp transhydrogenase [ Aedes aegypti ]128YP_27717771736851NAD(P) transhydrogenase, beta subunit [ Pseudomonas syringaepv. phaseolicola 1448A]129YP_26385271065125NAD(P) transhydrogenase, beta subunit [ Psychrobacter arcticus273-4]130NP_84093530248865NAD(P) transhydrogenase beta subunit [ Nitrosomonas europaeaATCC 19718]131XP_86792273953775PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 4 [ Canisfamiliaris ]132XP_86791673953773PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 3 [ Canisfamiliaris ]133XP_53648173953769PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 1 [ Canisfamiliaris ]134XP_86792873953777PREDICTED: similar to NAD(P) transhydrogenase,mitochondrial precursor (Pyridine nucleotide transhydrogenase)(Nicotinamide nucleotide transhydrogenase) isoform 5 [ Canisfamiliaris ]135NP_001 . . .61557127nicotinamide nucleotide transhydrogenase [ Rattus norvegicus ]136YP_23808366048242NAD(P) transhydrogenase, beta subunit [ Pseudomonas syringaepv. syringae B728a]137BAE4057774219995unnamed protein product [ Mus musculus ]138BAC3922626351179unnamed protein product [ Mus musculus ]139ZP_013 . . .94494989NAD(P) transhydrogenase, beta subunit [ Sphingomonas sp.SKA58]140NP_03273631543330nicotinamide nucleotide transhydrogenase [ Mus musculus]141BAC4011326352966unnamed protein product [ Mus musculus ]142ZP_004 . . .67155631NAD(P) transhydrogenase, beta subunit [ Azotobacter vinelandiiAvOP]143YP_57981293005375NAD(P) transhydrogenase, beta subunit [ Psychrobactercryohalolentis K5]144YP_29703173542511NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]145YP_58510794311897NAD(P) transhydrogenase, beta subunit [ Ralstoniametallidurans CH34]146YP_49711987199862NAD(P) transhydrogenase, beta subunit [ Novosphingobiumaromaticivorans DSM 12444]147AAQ8723936958771NAD(P) transhydrogenase subunit beta [ Rhizobium sp.NGR234]148NP_88848933600929NAD(P) transhydrogenase subunit beta [ Bordetellabronchiseptica RB50]149Q6194151338804NAD(P) transhydrogenase, mitochondrial precursor (Pyridinenucleotide transhydrogenase) (Nicotinamide nucleotidetranshydrogenase)150NP_77636827806831nicotinamide nucleotide transhydrogenase [ Bos taurus ]151NP_88472833597085NAD(P) transhydrogenase subunit beta [ Bordetella parapertussis12822]152AAA21440163397nicotinamide nucleotide transhydrogenase153YP_44180883721084NAD(P) transhydrogenase, beta subunit [ Burkholderiathailandensis E264]154AAI1054483405154Nicotinamide nucleotide transhydrogenase [ Homo sapiens ]155NP_89976934495554NAD(P) transhydrogenase, beta subunit [ Chromobacteriumviolaceum ATCC 12472]156NP_42209716127533NAD(P) transhydrogenase, beta subunit [ Caulobacter crescentusCB15]157XP_31285958383882ENSANGP00000016622 [ Anopheles gambiae str. PEST]158ZP_009 . . .84360819COG1282: NAD/NADP transhydrogenase beta subunit[ Burkholderia dolosa AUO158]159ZP_014 . . .113935785NAD(P) transhydrogenase, beta subunit [ Caulobacter sp. K31]160ZP_006 . . .71548983NAD(P) transhydrogenase, beta subunit [ Nitrosomonas eutrophaC71]161AAH8111751703526MGC83563 protein [ Xenopus laevis ]162CAH9007955726630hypothetical protein [ Pongo pygmaeus ]163BAE3529474198248unnamed protein product [ Mus musculus ]164ZP_014 . . .113872300probable NAD(P) transhydrogenase subunit beta transmembraneprotein [ Sinorhizobium medicae WSM419]165AAI1054583405537Nicotinamide nucleotide transhydrogenase [ Homo sapiens ]166NP_03647533695084nicotinamide nucleotide transhydrogenase [ Homo sapiens ]167YP_727574113869085NAD(P) transhydrogenase subunit beta [ Ralstonia eutrophaH16]1682211247B1589396nicotinamide nucleotide transhydrogenase1692211247A1589395nicotinamide nucleotide transhydrogenase170AAN6224624461677putative pyridine nucleotide transhydrogenase, beta subunit[ Pseudomonas aeruginosa]171P11024128400NAD(P) transhydrogenase, mitochondrial precursor (Pyridinenucleotide transhydrogenase) (Nicotinamide nucleotidetranshydrogenase)172NP_89202233695086nicotinamide nucleotide transhydrogenase [ Homo sapiens ]173NP_38696615966613PROBABLE NAD(P) TRANSHYDROGENASE SUBUNITBETA TRANSMEMBRANE PROTEIN [ Sinorhizobiummeliloti 1021]174YP_29991073539543NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]175ZP_012 . . .91769178NAD(P) transhydrogenase, beta subunit [ Psychrobacter sp.PRwf-1]176YP_29324172383887NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]177YP_29948073539113NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]178YP_29356772384213NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]179YP_725774113867285NAD(P) transhydrogenase subunit beta [ Ralstonia eutrophaH16]180YP_620105107021778NAD(P) transhydrogenase, beta subunit [ Burkholderiacenocepacia AU 1054]181YP_725367113866878NAD(P) transhydrogenase subunit beta [ Ralstonia eutrophaH16]182NP_52085417547452PROBABLE TRANSMEMBRANE NADPTRANSHYDROGENASE (BETA SUBUNIT)OXIDOREDUCTASE PROTEIN [ Ralstonia solanacearumGMI1000]183ZP_009 . . .83746755PntB [ Ralstonia solanacearum UW551]184ZP_013 . . .100235717hypothetical protein Bpse4_03000891 [ Burkholderiapseudomallei 406e]185YP_33476376809085NAD(P) transhydrogenase subunit beta [ Burkholderiapseudomallei 1710b]186ZP_013 . . .100917505hypothetical protein Bmal10_03001254 [ Burkholderia mallei10399]187ZP_004 . . .67667725NAD(P) transhydrogenase, beta subunit [ Burkholderiacenocepacia HI2424]188ZP_012 . . .91762289NAD(p) transhydrogenase subunit beta [ CandidatusPelagibacter ubique HTCC1002]189YP_47109386359201NAD(P)(+) transhydrogenase (AB-specific), beta subunitprotein [ Rhizobium etli CFN 42]190ZP_010 . . .85707884PntB, NAD(P) transhydrogenase, beta subunit [ Erythrobacter sp.NAP1]191YP_29326672383912NAD(P) transhydrogenase, beta subunit [ Ralstonia eutrophaJMP134]192ZP_009 . . .84356795COG1282: NAD/NADP transhydrogenase beta subunit[ Burkholderia cenocepacia PC184]193YP_26600071083281NAD(p) transhydrogenase subunit beta [ CandidatusPelagibacter ubique HTCC1062]194CAE6887539598183Hypothetical protein CBG14838 [ Caenorhabditis briggsae ]195YP_36803378065264NAD(P) transhydrogenase, beta subunit [ Burkholderia sp. 383]196YP_616428103486867NAD(P) transhydrogenase, beta subunit [ Sphingopyxisalaskensis RB2256]197YP_24607567458451NAD(p) transhydrogenase subunit beta [ Rickettsia felisURRWXCal2]198YP_53719491204839NAD(p) transhydrogenase subunit beta [ Rickettsia belliiRML369-C]199XP_64684066826971NAD(P)+ transhydrogenase (AB-specific) [ Dictyosteliumdiscoideum AX4]200ZP_009 . . .83747817NAD(P) transhydrogenase subunit beta [ Ralstonia solanacearumUW551]201YP_04759950086089pyridine nucleotide transhydrogenase, beta subunit[ Acinetobacter sp. ADP1] TABLE 34Examples of pox2 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_505264.150555712YlPOX2 [ Yarrowia lipolytica ].2O7493659799074Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)3XP_50447550554133YlPOX4 [ Yarrowia lipolytica ]4XP_50219950549457YlPOX5 [ Yarrowia lipolytica ]5O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)6XP_50470350554589YlPOX1 [ Yarrowia lipolytica ]7XP_50363250552444hypothetical protein [ Yarrowia lipolytica ]8XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]9XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]10XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]11P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)12Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)13OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast( Candida tropicalis )14BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]15XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]16BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]17OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )18AAA34362170912acyl-coenzyme A oxidase II precursor19Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)20XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]21AAA34361170910PXP-2 protein221306283A225549oxidase, fatty acyl23P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)24XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]25XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]26Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)27Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]29AAA34891172217acyl-coenzyme A oxidase30Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)31Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)32O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)331W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 134NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]35H714347488059probable apetala2 domain TINY - Arabidopsis thaliana36XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]37Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)38Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)39NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]40AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]41CAH9069155727877hypothetical protein [ Pongo pygmaeus ]42AAL0188815553480acyl-CoA oxidase [ Glycine max ]43AAA19113458119acyl-CoA oxidase44AAA18595495475peroxisomal fatty acyl-coA oxidase45XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]46NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]47NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]48NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]49AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]50CAD9762231873262hypothetical protein [ Homo sapiens ]51I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human52NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]53CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]54Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)55B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human56AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]57CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]58AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]59XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]60AAH9710167678187Zgc: 92584 protein [ Danio rerio ]61AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]622DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate63Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal64AAH6372739795632MGC68531 protein [ Xenopus laevis ]65NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]66AAH6889146250227MGC83074 protein [ Xenopus laevis ]67AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]682FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)69ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]70XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]71AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae ]72AAL0188715553478acyl-CoA oxidase [ Glycine max ]73Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)74BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]75Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)76BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]77AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]78AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]79NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]80XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST]81AAH2133918204156Acox2 protein [ Mus musculus ]82BAE2579474188249unnamed protein product [ Mus musculus ]83Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)84XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]85EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]86NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]87XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]88CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]89XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]90BAC2616726324826unnamed protein product [ Mus musculus ]91XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]92AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]93XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]94XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]95EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]96CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]97NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]98EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]99XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]100O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)101AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]102CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]103EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]104CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]105XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum ]106CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]107NP_61126424654595CG5009-PA [ Drosophila melanogaster ]108AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]109Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)110EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]111AAH5472768262425Acox1 protein [ Mus musculus ]112XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]113XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521]114AAL2814416767852GH01266p [ Drosophila melanogaster ]115NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]116EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]117NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]118BAC3578274197284unnamed protein product [ Mus musculus ]119XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]120NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]121CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]122NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]123EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]124XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]125CAH9186455730283hypothetical protein [ Pongo pygmaeus ]126NP_49911917552648C48B4.1 [ Caenorhabditis elegans ]127ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]128BAE5553783765394unnamed protein product [ Aspergillus oryzae ]129XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]130BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]131EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]132CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]hypothetical protein DDBDRAFT_0188084 [ Dictyostelium133XP_63660566805767discoideum AX4]134XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]135EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]136NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]137XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]138AAL3994417862934SD03592p [ Drosophila melanogaster ]139NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]140XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]141EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]142Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor143O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)144AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]145CAH9112055728762hypothetical protein [ Pongo pygmaeus ]146EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]147XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]148O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)149NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]150O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)151AAL4801017944231LD22081p [ Drosophila melanogaster ]152ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]153XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]154EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]155NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]156YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]157AAH4472528703869Acox3 protein [ Mus musculus ]158NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]159YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]160AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]161AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]162XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]163XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]164YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]165EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]166Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)167XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]168EAL2664854637245GA21981-PA [ Drosophila pseudoobscura ]169BAC2613626324764unnamed protein product [ Mus musculus ]170CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]171BAE4255374143079unnamed protein product [ Mus musculus ]172YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]173XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]174NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]175NP_57237124640268CG4586-PA [ Drosophila melanogaster ]176NP_96103541408199hypothetical protein MAP2101 [ Mycobacterium avium subsp.paratuberculosis K-10]177EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]178ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]179ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]180BAE6016683770031unnamed protein product [ Aspergillus oryzae ]181ZP_011 . . .89339305Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium flavescensPYR-GCK]182NP_60902745550141CG9527-PA [ Drosophila melanogaster ]183EAT48670108884445acyl-CoA oxidase [ Aedes aegypti ]184ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS]185AAH1705316877606ACOX3 protein [ Homo sapiens ]186ZP_004 . . .66967405Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal[ Arthrobacter sp. FB24]187NP_50803617560134F25C8.1 [ Caenorhabditis elegans ]188ZP_011 . . .88854811acyl-CoA oxidase [ marine actinobacterium PHSC20C1]189AAL4895017945806RE34879p [ Drosophila melanogaster ]190YP_640598108800401acyl-CoA dehydrogenase-like protein [ Mycobacterium sp.MCS]191NP_72418124585195CG17544-PC, isoform C [ Drosophila melanogaster ]192AAL1400316186117SD05719p [ Drosophila melanogaster ]193XP_64266966817952hypothetical protein DDBDRAFT_0169270 [ Dictyosteliumdiscoideum AX4]194CAA969171945301POX1 [ Saccharomyces cerevisiae ]195NP_50094317540842F58F9.7 [ Caenorhabditis elegans ]196XP_66436967541190hypothetical protein AN6765.2 [ Aspergillus nidulans FGSC A4] TABLE 35Examples of pox1a polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50470350554589YlPOX1 [ Yarrowia lipolytica ].2O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)3O7493659799074Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)4XP_50219950549457YlPOX5 [ Yarrowia lipolytica ]5O7493559799073Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)6XP_50363250552444hypothetical protein [ Yarrowia lipolytica ]7XP_50447550554133YlPOX4 [ Yarrowia lipolytica ]8XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]9XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]10XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]11P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)12OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast( Candida tropicalis )13Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)14Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)15XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]16AAA34362170912acyl-coenzyme A oxidase II precursor17XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]18BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]19BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]20OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )21AAA34361170910PXP-2 protein22XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]231306283A225549oxidase, fatty acyl24P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)25XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]26Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)27Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)29Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)30NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]31AAA34891172217acyl-coenzyme A oxidase32O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)331W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 134H714347488059probable apetala2 domain TINY - Arabidopsis thaliana35NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]36Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal37AAL0188815553480acyl-CoA oxidase [ Glycine max ]38CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]39AAL0188715553478acyl-CoA oxidase [ Glycine max ]40BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]41NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]42AAH6889146250227MGC83074 protein [ Xenopus laevis ]432FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)44NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]45AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]46XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]47AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae]48Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)49ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]50NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]51Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)52AAA18595495475peroxisomal fatty acyl-coA oxidase53AAA19113458119acyl-CoA oxidase54NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]55AAH6372739795632MGC68531 protein [ Xenopus laevis ]56AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]57NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]58BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]59Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)60AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]61AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]62CAH9069155727877hypothetical protein [ Pongo pygmaeus ]63CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]64AAH9710167678187Zgc: 92584 protein [ Danio rerio ]65NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]66AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]67CAD9762231873262hypothetical protein [ Homo sapiens ]68B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human692DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate70XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]71I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human72AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]73NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]74AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]75Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)76XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]77Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)78XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]79AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]80XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]81XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST]82EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]83BAC2616726324826unnamed protein product [ Mus musculus ]84EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]85XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]86XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]87CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]88AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]89CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]90AAH2133918204156Acox2 protein [ Mus musculus ]91BAE2579474188249unnamed protein product [ Mus musculus ]92EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]93BAE5553783765394unnamed protein product [ Aspergillus oryzae ]94Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)95NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]96XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]97XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum]98XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]99AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]100CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]101O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)102NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]103XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]104EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]105CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]106XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521]107CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]108XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]109NP_49911917552648C48B4.1 [ Caenorhabditis elegans]110XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]111XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]112XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]113XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]114XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]115EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]116AAH5472768262425Acox1 protein [ Mus musculus ]117BAC3578274197284unnamed protein product [ Mus musculus ]118NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]119AAF146356503198acyl-CoA oxidase [ Petroselinum crispum ]120CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]121AAL3994417862934SD03592p [ Drosophila melanogaster ]122NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]123ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]124AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]125XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]126AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]127NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]128NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]129CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]130AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]131O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)132EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]133EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]134XP_63660566805767hypothetical protein DDBDRAFT_0188084 [ Dictyosteliumdiscoideum AX4]135O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)136NP_61126424654595CG5009-PA [ Drosophila melanogaster ]137NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]138AAH4472528703869Acox3 protein [ Mus musculus ]139NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]140XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]141XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]142EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]143NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]144YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]145AAL2814416767852GH01266p [ Drosophila melanogaster ]146YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]147EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]148XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]149EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]150NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]151CAH9186455730283hypothetical protein [ Pongo pygmaeus ]152Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)153AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]154XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]155O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)156Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)157NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]158ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]159EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]160EAL2664854637245GA21981-PA [ Drosophila pseudoobscura]161EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]162BAE4255374143079unnamed protein product [ Mus musculus]163BAC2613626324764unnamed protein product [ Mus musculus]164XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]165XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]166YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]167CAH9112055728762hypothetical protein [ Pongo pygmaeus ]168EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]169AAL4801017944231LD22081p [ Drosophila melanogaster ]170XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]171ZP_011 . . .88854811acyl-CoA oxidase [ marine actinobacterium PHSC20C1]172NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]173BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]174EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]175CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]176ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]177Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor178XP_39548666564429PREDICTED: similar to CG9527-PA [ Apis mellifera]179YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]180ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]181AAL4895017945806RE34879p [ Drosophila melanogaster ]182NP_60902745550141CG9527-PA [ Drosophila melanogaster ]183ZP_006 . . .71369913Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal:Acyl-CoA dehydrogenase, central region:Acyl-CoA dehydrogenase,N-terminal [ Nocardioides sp. JS614]184ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS]185EAT48670108884445acyl-CoA oxidase [ Aedes aegypti]186XP_31744658390030ENSANGP00000011863 [ Anopheles gambiae str. PEST]187EAS3652390306892hypothetical protein CIMG_01877 [ Coccidioides immitis RS]188NP_57237124640268CG4586-PA [ Drosophila melanogaster ]189XP_64266966817952hypothetical protein DDBDRAFT_0169270 [ Dictyosteliumdiscoideum AX4]190CAA969171945301PDX1 [ Saccharomyces cerevisiae ]191ZP_011 . . .89339305Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium flavescensPYR-GCK]192ZP_003 . . .62426247COG1960: Acyl-CoA dehydrogenases [ Brevibacterium linensBL2]193YP_640598108800401acyl-CoA dehydrogenase-like protein [ Mycobacterium sp.MCS]194NP_72418124585195CG17544-PC, isoform C [ Drosophila melanogaster ]195AAL1400316186117SD05719p [ Drosophila melanogaster ]196AAH1705316877606ACOX3 protein [ Homo sapiens ]197EAL3291254644170GA21857-PA [ Drosophila pseudoobscura ] TABLE 36Examples of pox4 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_504475.150554133YlPOX4 [ Yarrowia lipolytica ]2O7493559799073Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)3O7493659799074Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)4XP_50219950549457YlPOX5 [ Yarrowia lipolytica ]5O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)6XP_50470350554589YlPOX1 [ Yarrowia lipolytica ]7XP_50363250552444hypothetical protein [ Yarrowia lipolytica ]8XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]9XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]10XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]11BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]12BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]13OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )14XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]15AAA34362170912acyl-coenzyme A oxidase II precursor16P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)17OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast( Candida tropicalis )18Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)19XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]20P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)211306283A225549oxidase, fatty acyl22AAA34361170910PXP-2 protein23XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]24Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)25XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]26Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)27Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]29AAA34891172217acyl-coenzyme A oxidase30Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)31Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)32O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)33CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]341W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 135AAL0188815553480acyl-CoA oxidase [ Glycine max ]36H714347488059probable apetala2 domain TINY - Arabidopsis thaliana37NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]38AAH6372739795632MGC68531 protein [ Xenopus laevis ]39AAL0188715553478acyl-CoA oxidase [ Glycine max ]40AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]41BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]42Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal43NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]44ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]45NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]46NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]47AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]482FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)49NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]50AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae ]51Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)52XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]53Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)54NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]55AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]56AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]57AAH9710167678187Zgc: 92584 protein [ Danio rerio ]58XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]59AAA19113458119acyl-CoA oxidase60AAA18595495475peroxisomal fatty acyl-coA oxidase61Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)62Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)63AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]64AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]65CAH9069155727877hypothetical protein [ Pongo pygmaeus ]66CAD9762231873262hypothetical protein [ Homo sapiens ]67AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]68NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]69I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human70BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]71CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]72Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)73AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]74B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human75XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST]76BAE2579474188249unnamed protein product [ Mus musculus ]77AAH2133918204156Acox2 protein [ Mus musculus ]782DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate79Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)80AAH6889146250227MGC83074 protein [ Xenopus laevis ]81XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]82XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]83XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]84NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]85EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]86XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]87NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]88XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum ]89CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]90XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]91XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]92XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]93AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]94AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]95CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]96NP_49911917552648C48B4.1 [ Caenorhabditis elegans ]97CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]98XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]99NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]100NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]101EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]102NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]103CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]104EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]105BAC2616726324826unnamed protein product [ Mus musculus ]106CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]107O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)108NP_61126424654595CG5009-PA [ Drosophila melanogaster ]109CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]110XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521]111EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]112XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]113AAL2814416767852GH01266p [ Drosophila melanogaster ]114XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]115EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]116XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]117CAH9186455730283hypothetical protein [ Pongo pygmaeus ]118NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]119Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)120AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]121AAL3994417862934SD03592p [ Drosophila melanogaster ]122NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]123AAH5472768262425Acox1 protein [ Mus musculus ]124BAC3578274197284unnamed protein product [ Mus musculus ]125BAE5553783765394unnamed protein product [ Aspergillus oryzae ]126CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]127XP_63660566805767hypothetical protein DDBDRAFT_0188084 [ Dictyosteliumdiscoideum AX4]128NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]129NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]130EAL2664854637245GA21981-PA [ Drosophila pseudoobscura ]131AAF146356503198acyl-CoA oxidase [ Petroselinum crispum ]132XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]133EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]134AAL4801017944231LD22081p [ Drosophila melanogaster ]135ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]136CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]137Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor138EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]139YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]140XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]141BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]142XP_31744658390030ENSANGP00000011863 [ Anopheles gambiae str. PEST]143XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]144XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]145YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]146EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]147EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]148O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)149NP_50803617560134F25C8.1 [ Caenorhabditis elegans ]150NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]151EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]152EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]153EAT48670108884445acyl-CoA oxidase [ Aedes aegypti ]154CAH9112055728762hypothetical protein [ Pongo pygmaeus ]155EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]156ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]157O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)158XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]159AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]160O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)161XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]162YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]163XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]164EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]165XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]166NP_57237124640268CG4586-PA [ Drosophila melanogaster ]167EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]168AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]169NP_96103541408199hypothetical protein MAP2101 [ Mycobacterium avium subsp.paratuberculosis K-10]170ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]171AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]172XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]173YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]174ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]175EAS3652390306892hypothetical protein CIMG_01877 [ Coccidioides immitis RS]176NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]177CAA68661267444 kD translation product [ Candida tropicalis ]178ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS]179XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]180CAA969171945301POX1 [ Saccharomyces cerevisiae ]181BAE6016683770031unnamed protein product [ Aspergillus oryzae ]182ZP_011 . . .89339305Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium flavescensPYR-GCK]183YP_640598108800401acyl-CoA dehydrogenase-like protein [ Mycobacterium sp.MCS]184ZP_006 . . .71369913Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal:Acyl-CoA dehydrogenase, central region:Acyl-CoA dehydrogenase,N-terminal [ Nocardioides sp. JS614]185AAL1400316186117SD05719p [ Drosophila melanogaster ]186NP_72418124585195CG17544-PC, isoform C [ Drosophila melanogaster ]187AAH4472528703869Acox3 protein [ Mus musculus ]188NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]189EAL3333554644594GA14550-PA [ Drosophila pseudoobscura ]190ZP_004 . . .66967405Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal[ Arthrobacter sp. FB24]191NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]192XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]193Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)194NP_60902745550141CG9527-PA [ Drosophila melanogaster ]195ZP_006 . . .69287897Acyl-CoA dehydrogenase, C-terminal:Acyl-CoAdehydrogenase, central region [ Kineococcus radiotoleransSRS30216]196BAE4746278483008acyl-CoA oxidase [ Arthrobacter ureafaciens ] TABLE 37Examples of pox1 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50363250552444hypothetical protein [ Yarrowia lipolytica ].2O7493559799073Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)3O7493659799074Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)4XP_50219950549457YlPOX5 [ Yarrowia lipolytica ]5O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)6XP_50470350554589YlPOX1 [ Yarrowia lipolytica ]7XP_50447550554133YlPOX4 [ Yarrowia lipolytica ]8XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]9XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]10AAA34362170912acyl-coenzyme A oxidase II precursor11BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]12XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]13BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]14XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]15OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )16P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)17OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) PDX5, peroxisomal - yeast( Candida tropicalis )18XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]19AAA34361170910PXP-2 protein20Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)211306283A225549oxidase, fatty acyl22P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)23XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]24Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)25XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]26Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)27Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]29AAA34891172217acyl-coenzyme A oxidase30Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)31Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)32CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]331W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 134O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)35NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]36AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]37XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]38H714347488059probable apetala2 domain TINY - Arabidopsis thaliana392DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate40NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]41NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]42AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]43AAH9710167678187Zgc: 92584 protein [ Danio rerio ]44AAH6372739795632MGC68531 protein [ Xenopus laevis ]45NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]46AAL0188815553480acyl-CoA oxidase [ Glycine max ]47ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]48AAL0188715553478acyl-CoA oxidase [ Glycine max ]49BAE2579474188249unnamed protein product [ Mus musculus ]50NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]51XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]52BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]53Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)54AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]55AAA18595495475peroxisomal fatty acyl-coA oxidase56Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)572FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)58AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]59AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae ]60CAH9069155727877hypothetical protein [ Pongo pygmaeus ]61NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]62Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)63AAH2133918204156Acox2 protein [ Mus musculus ]64NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]65NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]66Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal67AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]68AAH6889146250227MGC83074 protein [ Xenopus laevis ]69Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)70XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]71AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]72CAD9762231873262hypothetical protein [ Homo sapiens ]73I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human74BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]75AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]76AAA19113458119acyl-CoA oxidase77B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human78Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)79Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)80CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]81XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]82XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]83XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]84AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]85NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]86XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]87NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]88XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]89CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]90CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]91XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]92AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]93XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]94EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]95EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]96O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)97NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]98XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]99EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]100XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST]101NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]102AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]103BAC2616726324826unnamed protein product [ Mus musculus ]104Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)105NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]106XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521 ]107XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]108EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]109XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]110NP_49911917552648C48B4.1 [ Caenorhabditis elegans ]111O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)112BAE5553783765394unnamed protein product [ Aspergillus oryzae ]113XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]114CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]115NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]116AAH5472768262425Acox1 protein [ Mus musculus ]117BAC3578274197284unnamed protein product [ Mus musculus ]118AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]119AAL3994417862934SD03592p [ Drosophila melanogaster ]120XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]121ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]122CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]123EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]124CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]125CAH9112055728762hypothetical protein [ Pongo pygmaeus ]126XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]127XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]128XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum ]129CAH9186455730283hypothetical protein [ Pongo pygmaeus ]130NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]131NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]132NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]133AAH4472528703869Acox3 protein [ Mus musculus ]134XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]135CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]136CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]137NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]138XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]139BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]140XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]141NP_61126424654595CG5009-PA [ Drosophila melanogaster ]142NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]143Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)144Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor145BAE4255374143079unnamed protein product [ Mus musculus ]146AAL2814416767852GH01266p [ Drosophila melanogaster ]147EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]148BAC2613626324764unnamed protein product [ Mus musculus ]149XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]150EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]151AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]152O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)153AAF146356503198acyl-CoA oxidase [ Petroselinum crispum ]154EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]155AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]156EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]157YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]158O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)159AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]160ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]161EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]162EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]163EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]164AAH1705316877606ACOX3 protein [ Homo sapiens ]165XP_63660566805767hypothetical protein DDBDRAFT_0188084 [ Dictyosteliumdiscoideum AX4]166YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]167EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]168NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]169YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]170XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]171XP_31751358390136ENSANGP00000010039 [ Anopheles gambiae str. PEST]172ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]173EAS3652390306892hypothetical protein CIMG_01877 [ Coccidioides immitis RS]174XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]175XP_39548666564429PREDICTED: similar to CG9527-PA [ Apis mellifera ]176ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]177XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]178ZP_003 . . .62426247COG1960: Acyl-CoA dehydrogenases [ Brevibacterium linensBL2]179YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]180NP_50094317540842F58F9.7 [ Caenorhabditis elegans ]181EAT39346108875121acyl-CoA oxidase [ Aedes aegypti ]182CAA969171945301POX1 [ Saccharomyces cerevisiae ]183NP_60902745550141CG9527-PA [ Drosophila melanogaster ]184CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]185AAL4801017944231LD22081p [ Drosophila melanogaster ]186EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]187CAE6157739584202Hypothetical protein CBG05491 [ Caenorhabditis briggsae ]188AAL4895017945806RE34879p [ Drosophila melanogaster ]189NP_72418124585195CG17544-PC, isoform C [ Drosophila melanogaster ]190AAL1400316186117SD05719p [ Drosophila melanogaster ]191XP_31744658390030ENSANGP00000011863 [ Anopheles gambiae str. PEST]192ZP_011 . . .89339305Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium flavescensPYR-GCK]193ZP_004 . . .66967405Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal[ Arthrobacter sp. FB24]194ZP_011 . . .88803915acyl-coenzyme A oxidase I, putative [ Robiginitalea biformataHTCC2501]195EAL3291254644170GA21857-PA [ Drosophila pseudoobscura ]196EAL2664854637245GA21981-PA [ Drosophila pseudoobscura ]197ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS] TABLE 38Examples of pox3 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50324450551539YlPOX3 [ Yarrowia lipolytica ]2XP_50219950549457YlPOX5 [ Yarrowia lipolytica ]3O7493559799073Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)4O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)5XP_50470350554589YlPOX1 [ Yarrowia lipolytica ]6XP_50447550554133YlPOX4 [ Yarrowia lipolytica ]7XP_50363250552444hypothetical protein [ Yarrowia lipolytica ]8XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]9XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]10XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]11Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)12BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]13OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )14BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]15AAA34362170912acyl-coenzyme A oxidase II precursor16P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)17OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast( Candida tropicalis )18XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]19Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)20XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]21P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)22AAA34361170910PXP-2 protein231306283A225549oxidase, fatty acyl24XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]25XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]26Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)27Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)29Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)30NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]31AAA34891172217acyl-coenzyme A oxidase32CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]33BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]34O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)35H714347488059probable apetala2 domain TINY - Arabidopsis thaliana361W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 137NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]38AAH6889146250227MGC83074 protein [ Xenopus laevis ]39AAL0188815553480acyl-CoA oxidase [ Glycine max ]40ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]41Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal42CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]43BAE2579474188249unnamed protein product [ Mus musculus ]44AAL0188715553478acyl-CoA oxidase [ Glycine max ]45AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]462FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)47AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae ]48AAH2133918204156Acox2 protein [ Mus musculus ]49XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST]50Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)51XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]52NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]53AAH6372739795632MGC68531 protein [ Xenopus laevis ]54EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]55AAH9710167678187Zgc: 92584 protein [ Danio rerio ]56NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]57NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]58NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]59XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]60AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]61CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]62Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)63EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]64CAH9069155727877hypothetical protein [ Pongo pygmaeus ]65Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)66XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]67XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]68I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human69AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]70NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]71CAD9762231873262hypothetical protein [ Homo sapiens ]72NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]73Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)74NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]75NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]76B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human77AAA18595495475peroxisomal fatty acyl-coA oxidase78AAA19113458119acyl-CoA oxidase79AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]80XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521]81AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]82CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]83O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)84AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]85AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]86CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]872DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate88NP_49911917552648C48B4.1 [ Caenorhabditis elegans ]89XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]90XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]91XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]92XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]93Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)94AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]95AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]96XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]97XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]98NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]99XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum ]100CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]101NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]102Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)103EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]104BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]105Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)106EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]107AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]108AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]109XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]110NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]111CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]112NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]113CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]114BAC2616726324826unnamed protein product [ Mus musculus ]115XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]116BAE5553783765394unnamed protein product [ Aspergillus oryzae ]117NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]118CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]119EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]120NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]121EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]122O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)123XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]124XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]125BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]126XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]127XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]128Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor129AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]130CAH9186455730283hypothetical protein [ Pongo pygmaeus ]131NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]132AAL3994417862934SD03592p [ Drosophila melanogaster ]133NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]134EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]135AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]136AAL4801017944231LD22081p [ Drosophila melanogaster ]137EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]138YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]139EAL2664854637245GA21981-PA [ Drosophila pseudoobscura ]140O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)141AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]142AAF146356503198acyl-CoA oxidase [ Petroselinum crispum ]143XP_63660566805767hypothetical protein DDBDRAFT_0188084 [ Dictyosteliumdiscoideum AX4]144O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)145XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]146NP_61126424654595CG5009-PA [ Drosophila melanogaster ]147XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]148NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]149XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]150BAC3578274197284unnamed protein product [ Mus musculus ]151EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]152AAH4472528703869Acox3 protein [ Mus musculus ]153AAH5472768262425Acox1 protein [ Mus musculus ]154XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]155ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]156CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]157EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]158AAL2814416767852GH01266p [ Drosophila melanogaster ]159CAH9112055728762hypothetical protein [ Pongo pygmaeus ]160NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]161Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)162XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]163EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]164ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]165XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]166NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]167BAC2613626324764unnamed protein product [ Mus musculus ]168BAE4255374143079unnamed protein product [ Mus musculus ]169EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]170ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]171YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]172EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]173EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]174YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]175NP_50803617560134F25C8.1 [ Caenorhabditis elegans ]176NP_57237124640268CG4586-PA [ Drosophila melanogaster ]177ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]178XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]179YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]180ZP_011 . . .89339305Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium flavescensPYR-GCK]181XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]182BAE6016683770031unnamed protein product [ Aspergillus oryzae ]183ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS]184NP_96103541408199hypothetical protein MAP2101 [ Mycobacterium avium subsp.paratuberculosis K-10]185YP_640598108800401acyl-CoA dehydrogenase-like protein [ Mycobacterium sp.MCS]186XP_31744658390030ENSANGP00000011863 [ Anopheles gambiae str. PEST]187EAT48670108884445acyl-CoA oxidase [ Aedes aegypti ]188BAE4746278483008acyl-CoA oxidase [ Arthrobacter ureafaciens ]189ZP_003 . . .62426247COG1960: Acyl-CoA dehydrogenases [ Brevibacterium linensBL2]190AAH1705316877606ACOX3 protein [ Homo sapiens ]191ZP_011 . . .88854811acyl-CoA oxidase [ marine actinobacterium PHSC20C1]192ZP_006 . . .71369913Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal:Acyl-CoA dehydrogenase, central region:Acyl-CoA dehydrogenase,N-terminal [ Nocardioides sp. JS614]193ZP_009 . . .84496319hypothetical protein JNB_02330 [ Janibacter sp. HTCC2649]194ZP_004 . . .66967405Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal[ Arthrobacter sp. FB24]195ZP_011 . . .88803915acyl-coenzyme A oxidase I, putative [ Robiginitalea biformataHTCC2501]196CAA68661267444 kD translation product [ Candida tropicalis ] TABLE 39Examples of pox5 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50219950549457YlPOX5 [ Yarrowia lipolytica ].2O7493659799074Acyl-coenzyme A oxidase 3 (Acyl-CoA oxidase 3)3O7493459799072Acyl-coenzyme A oxidase 1 (Acyl-CoA oxidase 1)4XP_50470350554589YlPOX1 [ Yarrowia lipolytica ]5O7493559799073Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2)6XP_50447550554133YlPOX4 [ Yarrowia lipolytica ]7XP_50363250552444hypothetical protein [ Yarrowia lipolytica ]8XP_76047171020481hypothetical protein UM04324.1 [ Ustilago maydis 521]9XP_57176858269224Acyl-coenzyme A oxidase I [ Cryptococcus neoformans var.neoformans JEC21]10BAA834825763520acyl-CoA oxidase [ Candida tropicalis ]11BAA834835763522acyl-CoA oxidase [ Candida tropicalis ]12OXCKPM66060acyl-CoA oxidase (EC 1.3.3.6) PXP4, peroxisomal - yeast( Candida maltosa )13P0879017373073Acyl-coenzyme A oxidase 5 (Acyl-CoA oxidase 5) (PXP-5)14AAA34362170912acyl-coenzyme A oxidase II precursor15OXCKX566061acyl-CoA oxidase (EC 1.3.3.6) POX5, peroxisomal - yeast( Candida tropicalis )16XP_71799568475844putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]17Q9Y7B160391213Acyl-coenzyme A oxidase (Acyl-CoA oxidase)18XP_72161068468582putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]19AAA34361170910PXP-2 protein20XP_72161368468588putative fatty-acyl coenzyme A oxidase [ Candida albicansSC5314]21P0659817373023Acyl-coenzyme A oxidase 4 (Acyl-CoA oxidase 4) (PXP-4)(Peroxisomal fatty acyl-CoA oxidase)22Q6BRD559799027Acyl-coenzyme A oxidase (Acyl-CoA oxidase)231306283A225549oxidase, fatty acyl24XP_45772650417804hypothetical protein DEHA0C01155g [ Debaryomyces hanseniiCBS767]25XP_45923250421365hypothetical protein DEHA0D18667g [ Debaryomyces hanseniiCBS767]26Q004682498206Acyl-coenzyme A oxidase 2 (Acyl-CoA oxidase 2) (AOX 2)27Q756A960391210Acyl-coenzyme A oxidase (Acyl-CoA oxidase)28Q6FY6359799032Acyl-coenzyme A oxidase (Acyl-CoA oxidase)29NP_0113106321233Fatty-acyl coenzyme A oxidase, involved in the fatty acid beta-oxidation pathway; localized to the peroxisomal matrix; Pox1p[ Saccharomyces cerevisiae ]30AAA34891172217acyl-coenzyme A oxidase31Q6CKK759799028Acyl-coenzyme A oxidase (Acyl-CoA oxidase)321W07B58177067Chain B, Arabidopsis Thaliana Acyl-Coa Oxidase 133O6520262286589Acyl-coenzyme A oxidase 1, peroxisomal (AOX 1) (Long-chainacyl-CoA oxidase) (AtCX1)34CAA686602673acyl-coenzyme A oxidase [ Candida tropicalis ]35NP_56751318414744ACX1 (ACYL-COA OXIDASE 1) [ Arabidopsis thaliana ]36H714347488059probable apetala2 domain TINY - Arabidopsis thaliana37AAL0188815553480acyl-CoA oxidase [ Glycine max ]38AAL0188715553478acyl-CoA oxidase [ Glycine max ]39ABE8370692875906acyl-CoA oxidase [ Medicago truncatula ]40BAF18456113594582Os06g0103500 [ Oryza sativa ( japonica cultivar-group)]412FONC109157678Chain C, X-Ray Crystal Structure Of Leacx1, An Acyl-CoaOxidase From Lycopersicon Esculentum (Tomato)42AAW7868958531948peroxisomal acyl-CoA oxidase 1A [ Lycopersicon esculentum ]43AAW7869158531952peroxisomal acyl-CoA oxidase 1A [ Lycopersicon cheesmaniae ]44Q9ZQP262286640Putative acyl-coenzyme A oxidase 1.2, peroxisomal45NP_001 . . .54400372hypothetical protein LOC449662 [ Danio rerio ]46XP_59289276648807PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 1 [ Bos taurus ]47XP_87999676648809PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 6 [ Bos taurus ]48AAH6889146250227MGC83074 protein [ Xenopus laevis ]49AAH9710167678187Zgc: 92584 protein [ Danio rerio ]50XP_41440650754485PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Gallus gallus ]51NP_001 . . .55741614acyl-Coenzyme A oxidase 1, palmitoyl [ Gallus gallus ]52XP_32071758394415ENSANGP00000020118 [ Anopheles gambiae str. PEST ]53NP_51060317568313F59F4.1 [ Caenorhabditis elegans ]54BAE2579474188249unnamed protein product [ Mus musculus ]55CAE6973739596101Hypothetical protein CBG16008 [ Caenorhabditis briggsae ]56AAH2133918204156Acox2 protein [ Mus musculus ]57CAJ8330289271321acyl-Coenzyme A oxidase 2, branched chain [ Xenopustropicalis ]58XP_32071858394417ENSANGP00000020032 [ Anopheles gambiae str. PEST]59Q9QXD117367045Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)60AAH6372739795632MGC68531 protein [ Xenopus laevis ]61Q5RC1962286600Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)62AAW7869058531950peroxisomal acyl-CoA oxidase 1B [ Lycopersicon esculentum ]63XP_78282472015136PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]64AAH4770028839704Acyl-Coenzyme A oxidase 2, branched chain [ Homo sapiens ]65EAT39640108875415acyl-CoA oxidase [ Aedes aegypti ]66NP_001 . . .62751552MGC108278 protein [ Xenopus tropicalis ]67CAH9069155727877hypothetical protein [ Pongo pygmaeus ]68XP_001 . . .109118312PREDICTED: similar to acyl-Coenzyme A oxidase isoform b[ Macaca mulatta ]69Q1506717380467Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX) (Straight-chain acyl-CoA oxidase) (SCOX)70NP_00922330089974acyl-Coenzyme A oxidase isoform b [ Homo sapiens ]71AAA19113458119acyl-CoA oxidase72AAB300197689914peroxisomal acyl-coenzyme A oxidase [ Homo sapiens ]73XP_78521072015040PREDICTED: similar to Acyl-coenzyme A oxidase 1,peroxisomal (Palmitoyl-CoA oxidase) (AOX)[ Strongylocentrotus purpuratus ]74O0276717366131Acyl-coenzyme A oxidase 2, peroxisomal (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase) (3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoAoxidase) (Trihydroxycoprostanoyl-CoA oxidase) (THCCox)(THCA-CoA oxidase)75NP_00402630089972acyl-Coenzyme A oxidase isoform a [ Homo sapiens ]76AAA18595495475peroxisomal fatty acyl-coA oxidase77I380952117541acyl-CoA oxidase (EC 1.3.3.6), peroxisomal - human78AAH0876714250616Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]79B549421082171acyl-CoA oxidase (EC 1.3.3.6), peroxisomal splice form II -human80NP_001 . . .78369480acyl-Coenzyme A oxidase 1, palmitoyl [ Bos taurus ]81NP_49911917552648C48B4.1 [ Caenorhabditis elegans ]82NP_66571321955130acyl-Coenzyme A oxidase 2, branched chain [ Rattus norvegicus ]83CAD9762231873262hypothetical protein [ Homo sapiens ]84BAA868706429156peroxisomal acyl-CoA oxidase [ Mus musculus ]85NP_05654466793429acyl-Coenzyme A oxidase 1, palmitoyl [ Mus musculus ]86AAH8574355249685Acyl-Coenzyme A oxidase 1, palmitoyl [ Rattus norvegicus ]872DDHA93279231Chain A, Crystal Structure Of Acyl-Coa Oxidase ComplexedWith 3-Oh-Dodecanoate88Q9R0H051338830Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)89XP_75835571010163hypothetical protein UM02208.1 [ Ustilago maydis 521]90AAH1042514714578Acyl-Coenzyme A oxidase 1, palmitoyl [ Homo sapiens ]91AAB629262253380peroxisomal acyl-CoA oxidase [ Mus musculus ]92CAE6517139590798Hypothetical protein CBG10043 [ Caenorhabditis briggsae ]93XP_62513666556360PREDICTED: similar to CG5009-PA, partial [ Apis mellifera ]94XP_54044173965013PREDICTED: similar to acyl-Coenzyme A oxidase isoform a[ Canis familiaris ]95Q8HYL834098564Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)96CAE6347639592399Hypothetical protein CBG07943 [ Caenorhabditis briggsae ]97AAI0864883318302Unknown (protein for MGC: 131363) [ Xenopus laevis ]98XP_87982776648805PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) isoform 5 [ Bos taurus ]99AAF738438163758acyl-CoA oxidase ACX3 [ Arabidopsis thaliana ]100Q9LLH962286634Acyl-coenzyme A oxidase 3, peroxisomal precursor (AOX 3)(Medium-chain acyl-CoA oxidase) (AtCX3)101XP_97366091082769PREDICTED: similar to CG5009-PA [ Tribolium castaneum ]102EAS3161890301987hypothetical protein CIMG_07097 [ Coccidioides immitis RS]103EAR9556889297580Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]104Q9Z1N017367267Acyl-coenzyme A oxidase 1, peroxisomal (Palmitoyl-CoAoxidase) (AOX)105AAO1557727462768acyl-CoA oxidase type 2 [ Phascolarctos cinereus ]106XP_54182673985284PREDICTED: similar to Acyl-coenzyme A oxidase 2,peroxisomal (Branched-chain acyl-CoA oxidase) (BRCACox)(Trihydroxycoprostanoyl-CoA oxidase) (THCCox) (THCA-CoA oxidase) [ Canis familiaris ]107CAE6347939592402Hypothetical protein CBG07946 [ Caenorhabditis briggsae ]108XP_51169055645995PREDICTED: similar to hypothetical protein [ Pan troglodytes ]109BAC2616726324826unnamed protein product [ Mus musculus ]110CAE6347739592400Hypothetical protein CBG07944 [ Caenorhabditis briggsae ]111NP_49326417506535F08A8.4 [ Caenorhabditis elegans ]112Q9LMI762286635Putative acyl-coenzyme A oxidase 3.2, peroxisomal precursor113CAJ5849385539740Hypothetical protein F08A8.1c [ Caenorhabditis elegans ]114NP_001 . . .71983355F08A8.1b [ Caenorhabditis elegans ]115NP_001 . . .71983346F08A8.1a [ Caenorhabditis elegans ]116BAF19505113595631Os06g0354500 [ Oryza sativa ( japonica cultivar-group)]117NP_49326317506533F08A8.3 [ Caenorhabditis elegans ]118O6489462286587Acyl-coenzyme A oxidase, peroxisomal precursor (AOX)(Long-chain acyl-CoA oxidase)119NP_49326217506531F08A8.2 [ Caenorhabditis elegans ]120CAE6348039592403Hypothetical protein CBG07947 [ Caenorhabditis briggsae ]121AAF146356503198acyl-CoA oxidase [ Petroselinum crispum ]122BAE5553783765394unnamed protein product [ Aspergillus oryzae ]123NP_99831247085909pristanoyl acyl-Coenzyme A oxidase 3 [ Danio rerio ]124O6520162286588Acyl-coenzyme A oxidase 2, peroxisomal precursor (AOX 2)(Long-chain acyl-CoA oxidase) (AtCX2)125AAC134973044212acyl-CoA oxidase [ Arabidopsis thaliana ]126EAT87650111066530hypothetical protein SNOG_05259 [ Phaeosphaeria nodorumSN15]127XP_58715776620513PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Bos taurus ]128EAT48205108883980acyl-CoA oxidase [ Aedes aegypti ]129EAT87454111066334hypothetical protein SNOG_05063 [ Phaeosphaeria nodorumSN15]130XP_66435667541164hypothetical protein AN6752.2 [ Aspergillus nidulans FGSC A4]131AAB678831575556acyl-CoA oxidase homolog [ Phalaenopsis sp. ‘True Lady’]132AAR0058637699750acyl-CoA oxidase [ Phalaenopsis cv. ‘True Lady’]133CAH9186455730283hypothetical protein [ Pongo pygmaeus ]134XP_63660566805767hypothetical protein DDBDRAFT_0188084 [ Dictyosteliumdiscoideum AX4]135NP_61126424654595CG5009-PA [ Drosophila melanogaster ]136EAS0470489306716Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]137XP_63594666804335hypothetical protein DDBDRAFT_0188674 [ Dictyosteliumdiscoideum AX4]138O1525417366151Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)139AAL3994417862934SD03592p [ Drosophila melanogaster ]140NP_52380217647123acyl-Coenzyme A oxidase at 57D proximal CG9707-PA[ Drosophila melanogaster ]141AAL2814416767852GH01266p [ Drosophila melanogaster ]142XP_38246346110811hypothetical protein FG02287.1 [ Gibberella zeae PH-1]143EAL2635954636956GA18591-PA [ Drosophila pseudoobscura ]144CAA046882370232putative acyl-CoA oxidase [ Hordeum vulgare subsp. vulgare ]145XP_78345072111190PREDICTED: similar to acyl-Coenzyme A oxidase 1, palmitoyl[ Strongylocentrotus purpuratus ]146AAL4801017944231LD22081p [ Drosophila melanogaster ]147CAH9112055728762hypothetical protein [ Pongo pygmaeus ]148XP_64639566826081hypothetical protein DDBDRAFT_0216722 [ Dictyosteliumdiscoideum AX4]149XP_75811371007469hypothetical protein UM01966.1 [ Ustilago maydis 521]150EAR9963189301643Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]151EAR8926189291273Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]152XP_63761066807775hypothetical protein DDBDRAFT_0187085 [ Dictyosteliumdiscoideum AX4]153ABA94670108864573Acyl-coenzyme A oxidase 2, peroxisomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]154EAL2664754637244GA21980-PA [ Drosophila pseudoobscura ]155ZP_012 . . .90587482Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Flavobacterium johnsoniaeUW101]156BAC3578274197284unnamed protein product [ Mus musculus ]157EAS0271689304728Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]158YP_634556108758121putative acyl-CoA dehydrogenase [ Myxococcus xanthus DK1622]159AAH5472768262425Acox1 protein [ Mus musculus ]160YP_44582083816544acyl-coenzyme A oxidase I, putative [ Salinibacter ruber DSM13855]161AAH4472528703869Acox3 protein [ Mus musculus ]162NP_10964634328334acyl-Coenzyme A oxidase 3, pristanoyl [ Mus musculus ]163XP_54590873951751PREDICTED: similar to Acyl-coenzyme A oxidase 3,peroxisomal (Pristanoyl-CoA oxidase) [ Canis familiaris ]164NP_001 . . .79332306ACX2 (ACYL-COA OXIDASE 2); acyl-CoA oxidase[ Arabidopsis thaliana ]165EAR9858189300593Acyl-CoA oxidase family protein [ Tetrahymena thermophilaSB210]166XP_96951391093755PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Tribolium castaneum ]167ZP_012 . . .89890388acyl-CoA oxidase [ Flavobacteria bacterium BBFL7]168YP_29029572162638hypothetical protein Tfu_2239 [ Thermobifida fusca YX]169BAC2613626324764unnamed protein product [ Mus musculus ]170BAE4255374143079unnamed protein product [ Mus musculus ]171EAL2664854637245GA21981-PA [ Drosophila pseudoobscura ]172NP_44579116758056acyl-Coenzyme A oxidase 3, pristanoyl [ Rattus norvegicus ]173Q9EPL917366740Acyl-coenzyme A oxidase 3, peroxisomal (Pristanoyl-CoAoxidase) (Branched-chain acyl-CoA oxidase) (BRCACox)174XP_78602572005645PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]175XP_78608172005647PREDICTED: similar to pristanoyl acyl-Coenzyme A oxidase 3[ Strongylocentrotus purpuratus ]176EAL3232954643586GA18278-PA [ Drosophila pseudoobscura ]177NP_72418124585195CG17544-PC, isoform C [ Drosophila melanogaster ]178AAL1400316186117SD05719p [ Drosophila melanogaster ]179CAA68661267444 kD translation product [ Candida tropicalis ]180NP_57237124640268CG4586-PA [ Drosophila melanogaster ]181ZP_011 . . .88854811acyl-CoA oxidase [ marine actinobacterium PHSC20C1]182EAL3333554644594GA14550-PA [ Drosophila pseudoobscura ]183EAS3652390306892hypothetical protein CIMG_01877 [ Coccidioides immitis RS]184EAT48670108884445acyl-CoA oxidase [ Aedes aegypti ]185YP_702012111019040acyl-CoA oxidase [ Rhodococcus sp. RHA1]186ZP_003 . . .62426247COG1960: Acyl-CoA dehydrogenases [ Brevibacterium linensBL2]187XP_31744658390030ENSANGP00000011863 [ Anopheles gambiae str. PEST]188XP_31751358390136ENSANGP00000010039 [ Anopheles gambiae str. PEST]189AAH1705316877606ACOX3 protein [ Homo sapiens ]190ZP_012 . . .90205075Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium vanbaaleniiPYR-1]191ZP_011 . . .88803915acyl-coenzyme A oxidase I, putative [ Robiginitalea biformataHTCC2501]192XP_64266966817952hypothetical protein DDBDRAFT_0169270 [ Dictyosteliumdiscoideum AX4]193NP_50803617560134F25C8.1 [ Caenorhabditis elegans ]194ZP_006 . . .71369913Acyl-CoA oxidase:Acyl-CoA dehydrogenase, C-terminal:Acyl-CoA dehydrogenase, central region:Acyl-CoA dehydrogenase,N-terminal [ Nocardioides sp. JS614]195BAE6593483775815unnamed protein product [ Aspergillus oryzae ]196ZP_012 . . .92908524Acyl-CoA oxidase-like:Acyl-CoA dehydrogenase-like:Acyl-CoA dehydrogenase, central region [ Mycobacterium sp. JLS] TABLE 40Examples of triglyceride lipase (tgl4) polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50523050555644hypothetical protein [ Yarrowia lipolytica ].2XP_45955350421985hypothetical protein DEHA0E06127g [ Debaryomyces hanseniiCBS767]3XP_38773146126355hypothetical protein FG07555.1 [ Gibberella zeae H-1 ]4XP_71770468476486putative patatin-like phospholipase [ Candida albicans SC5314]5XP_95875085091127hypothetical protein [ Neurospora crassa OR74A]6NP_0130156322942Triacylglycerol lipase involved in triacylglycerol mobilizationand degradation; found in lipid particles; potential Cdc28psubstrate; Tgl4p [ Saccharomyces cerevisiae ]7XP_65931767522513hypothetical protein AN1713.2 [ Aspergillus nidulans FGSC A4]8NP_98432745188104ADR231Cp [ Eremothecium gossypii ]9CAD6056427764284unnamed protein product [ Podospora anserina ]10EAT92134111071014hypothetical protein SNOG_00639 [ Phaeosphaeria nodorumSN15]11BAE5922883769091unnamed protein product [ Aspergillus oryzae ]12XP_44646550288073unnamed protein product [ Candida glabrata ]13XP_75198270994310patatin-like serine hydrolase [ Aspergillus fumigatus Af293]14XP_45133650302799unnamed protein product [ Kluyveromyces lactis ]15EAS3009590300464hypothetical protein CIMG_08841 [ Coccidioides immitis RS]16EAQ8309288175624hypothetical protein CHGG_10910 [ Chaetomium globosumCBS 148.51]17NP_0147246324655Triacylglycerol lipase involved in TAG mobilization; localizesto lipid particles; potential Cdc28p substrate; Tgl5p[ Saccharomyces cerevisiae ]18XP_44847050292075unnamed protein product [ Candida glabrata ]19ABG79933110628937triacylglycerol lipase [ Magnaporthe grisea ]20NP_59319719114109hypothetical protein SPAC1A6.05c [ Schizosaccharomycespombe 972h- ]21EAR8606589288077Patatin-like phospholipase family protein [ Tetrahymenathermophila SB210]22XP_46344850902030P0512C01.22 [ Oryza sativa ( japonica cultivar-group)]23BAF06239113533856Os01g0762000 [ Oryza sativa ( japonica cultivar-group)]24YP_43386583645430predicted esterase of the alpha-beta hydrolase superfamily[ Hahella chejuensis KCTC 2396]25ZP_008 . . .77951643conserved hypothetical protein [ Marinobacter aquaeolei VT8]26AAM9713522531263putative protein [ Arabidopsis thaliana ]27BAF13581113550138Os03g0810900 [ Oryza sativa ( japonica cultivar-group)]28ABE7808892867978phospholipase, patatin family, putative [ Medicago truncatula ]29YP_693301110834442hypothetical protein ABO_1581 [ Alcanivorax borkumensisSK2]30NP_97444942572707unknown protein [ Arabidopsis thaliana ]31BAE5650783766364unnamed protein product [ Aspergillus oryzae ]32EAR8373889285729Patatin-like phospholipase family protein [ Tetrahymenathermophila SB210 ]33ABE9419492898449Patatin [ Medicago truncatula ]34XP_75227870995024patatin-like serine hydrolase [ Aspergillus fumigatus Af293]35YP_04602650084516hypothetical protein ACIAD1335 [ Acinetobacter sp. ADP1]36ZP_011 . . .88794068predicted esterase of the alpha-beta hydrolase superfamilyprotein [ Alteromonas macleodii ‘Deep ecotype’]37XP_38069646107274hypothetical protein FG00520.1 [ Gibberella zeae PH-1]38ZP_011 . . .88703608Patatin-like phospholipase [gamma proteobacterium KT 71]39EAT85718111064598hypothetical protein SNOG_07067 [ Phaeosphaeria nodorumSN15]40ZP_011 . . .88707125Patatin-like phospholipase [gamma proteobacterium KT 71]41XP_75716471004996hypothetical protein UM01017.1 [ Ustilago maydis 521]42YP_615253103485692Patatin [ Sphingopyxis alaskensis RB2256]43XP_96450285113293hypothetical protein [ Neurospora crassa OR74A]44NP_59402263054585hypothetical protein SPAC31G5.20c [ Schizosaccharomycespombe 972h-]45XP_50289850550851hypothetical protein [ Yarrowia lipolytica ]46XP_72255068466709putative patatin-like phospholipase [ Candida albicans SC5314]47EAS3168790302056hypothetical protein CIMG_07166 [ Coccidioides immitis RS]48BAE5796983767830unnamed protein product [ Aspergillus oryzae ]49XP_72241268466994putative patatin-like phospholipase [ Candida albicans SC5314]50EAQ9336288185894hypothetical protein CHGG_01597 [ Chaetomium globosumCBS 148.51]51ZP_010 . . .85708568hypothetical protein NAP1_04995 [ Erythrobacter sp. NAP1]52XP_45714150412575hypothetical protein DEHA0B04048g [ Debaryomyces hanseniiCBS767]53XP_65801267516253hypothetical protein AN0408.2 [ Aspergillus nidulans FGSC A4]54EAS3387390304242hypothetical protein CIMG_04897 [ Coccidioides immitis RS]55XP_80512671404931hypothetical protein [ Trypanosoma cruzi strain CL Brener]56CAB882267630152conserved hypothetical protein L5213T.05 [ Leishmania major ]57CAJ0643368127889hypothetical protein, conserved [ Leishmania major ]58XP_75024670990794patatin-like serine hydrolase [ Aspergillus fumigatus Af293]59ABG79934110628939triacylglycerol lipase [ Magnaporthe grisea ]60XP_38682146124535hypothetical protein FG06645.1 [ Gibberella zeae PH-1]61EAT92413111071293hypothetical protein SNOG_00918 [ Phaeosphaeria nodorumSN15]62NP_58831519075815hypothetical protein SPCC1450.16c [ Schizosaccharomycespombe 972h-]63EAQ9096588183497hypothetical protein CHGG_02900 [ Chaetomium globosumCBS 148.51]64XP_95726785084210hypothetical protein [ Neurospora crassa OR74A]65XP_45144550303015unnamed protein product [ Kluyveromyces lactis ]66CAB117042388971SPAC31G5.20c [ Schizosaccharomyces pombe ]67XP_62658766358818hypothetical protein cgd2_4050 [ Cryptosporidium parvum IowaII]68XP_66530867588018hypothetical protein Chro.20432 [ Cryptosporidium hominisTU502]69XP_44995250295082hypothetical protein CAGL0M13981g [ Candida glabrataCBS138]70XP_72276468466564putative lipid particle triacylglycerol lipase fragment [ Candidaalbicans SC5314]71NP_98633045200760AGL337Cp [ Eremothecium gossypii ]72CAE8440539722369Tgl3 protein [ Kluyveromyces delphensis ]73XP_80728371409928hypothetical protein [ Trypanosoma cruzi strain CL Brener]74XP_80701671409330hypothetical protein [ Trypanosoma cruzi strain CL Brener]75XP_50294450550941hypothetical protein [ Yarrowia lipolytica ]76NP_0140446323973Triacylglycerol lipase of the lipid particle, responsible for all theTAG lipase activity of the lipid particle; contains the consensussequence motif GXSXG, which is found in lipolytic enzymes;Tgl3p [ Saccharomyces cerevisiae ] TABLE 41Examples of triglyceride lipase (tgl3) polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50294450550941hypothetical protein [ Yarrowia lipolytica ].2XP_75227870995024patatin-like serine hydrolase [ Aspergillus fumigatus Af293]3BAE5650783766364unnamed protein product [ Aspergillus oryzae ]4EAT85718111064598hypothetical protein SNOG_07067 [ Phaeosphaeria nodorumSN15]5XP_38069646107274hypothetical protein FG00520.1 [ Gibberella zeae PH-1]6XP_96450285113293hypothetical protein [ Neurospora crassa OR74A]7EAQ9336288185894hypothetical protein CHGG_01597 [ Chaetomium globosumCBS 148.51]8XP_72276468466564putative lipid particle triacylglycerol lipase fragment [ Candidaalbicans SC5314]9NP_98633045200760AGL337Cp [ Eremothecium gossypii ]10CAE8440539722369Tgl3 protein [ Kluyveromyces delphensis ]11XP_44995250295082hypothetical protein CAGL0M13981g [ Candida glabrataCBS138]12XP_45144550303015unnamed protein product [ Kluyveromyces lactis ]13NP_0140446323973Triacylglycerol lipase of the lipid particle, responsible for all theTAG lipase activity of the lipid particle; contains the consensussequence motif GXSXG, which is found in lipolytic enzymes;Tgl3p [ Saccharomyces cerevisiae ]14EAS3168790302056hypothetical protein CIMG_07166 [ Coccidioides immitis RS]15EAT92134111071014hypothetical protein SNOG_00639 [ Phaeosphaeria nodorumSN15]16XP_38773146126355hypothetical protein FG07555.1 [ Gibberella zeae PH-1]17NP_58831519075815hypothetical protein SPCC1450.16c [ Schizosaccharomycespombe 972h-]18XP_75198270994310patatin-like serine hydrolase [ Aspergillus fumigatus Af293]19XP_95875085091127hypothetical protein [ Neurospora crassa OR74A]20EAQ8309288175624hypothetical protein CHGG_10910 [ Chaetomium globosumCBS 148.51]21BAE5922883769091unnamed protein product [ Aspergillus oryzae ]22YP_693301110834442hypothetical protein ABO_1581 [ Alcanivorax borkumensisSK2]23XP_65931767522513hypothetical protein AN1713.2 [ Aspergillus nidulans FGSC A4]24ZP_011 . . .88703608Patatin-like phospholipase [gamma proteobacterium KT 71]25BAF06239113533856Os01g0762000 [ Oryza sativa ( japonica cultivar-group)]26XP_46344850902030P0512C01.22 [ Oryza sativa ( japonica cultivar-group)]27EAS3009590300464hypothetical protein CIMG_08841 [ Coccidioides immitis RS]28YP_43386583645430predicted esterase of the alpha-beta hydrolase superfamily[ Hahella chejuensis KCTC 2396]29XP_45955350421985hypothetical protein DEHA0E06127g [ Debaryomyces hanseniiCBS767]30CAD6056427764284unnamed protein product [ Podospora anserina ]31ZP_008 . . .77951643conserved hypothetical protein [ Marinobacter aquaeolei VT8]32XP_50523050555644hypothetical protein [ Yarrowia lipolytica ]33XP_44646550288073unnamed protein product [ Candida glabrata ]34AAM9713522531263putative protein [ Arabidopsis thaliana ]35BAF13581113550138Os03g0810900 [ Oryza sativa ( japonica cultivar-group)]36ABG79933110628937triacylglycerol lipase [ Magnaporthe grisea ]37XP_71770468476486putative patatin-like phospholipase [ Candida albicans SC5314]38NP_0130156322942Triacylglycerol lipase involved in triacylglycerol mobilizationand degradation; found in lipid particles; potential Cdc28psubstrate; Tgl4p [ Saccharomyces cerevisiae ]39NP_59402263054585hypothetical protein SPAC31G5.20c [ Schizosaccharomycespombe 972h-]40EAR8373889285729Patatin-like phospholipase family protein [ Tetrahymenathermophila SB210]41NP_98432745188104ADR231Cp [ Eremothecium gossypii ]42EAR8606589288077Patatin-like phospholipase family protein [ Tetrahymenathermophila SB210]43NP_0147246324655Triacylglycerol lipase involved in TAG mobilization; localizesto lipid particles; potential Cdc28p substrate; Tgl5p[ Saccharomyces cerevisiae ]44YP_04602650084516hypothetical protein ACIAD1335 [ Acinetobacter sp. ADP1]45XP_45133650302799unnamed protein product [ Kluyveromyces lactis ]46ZP_011 . . .88794068predicted esterase of the alpha-beta hydrolase superfamilyprotein [ Alteromonas macleodii ‘Deep ecotype’]47XP_72255068466709putative patatin-like phospholipase [ Candida albicans SC5314]48XP_72241268466994putative patatin-like phospholipase [ Candida albicans SC5314]49EAS3387390304242hypothetical protein CIMG_04897 [ Coccidioides immitis RS]50ABG79934110628939triacylglycerol lipase [ Magnaporthe grisea ]51ZP_011 . . .88707125Patatin-like phospholipase [gamma proteobacterium KT 71]52NP_59319719114109hypothetical protein SPAC1A6.05c [ Schizosaccharomycespombe 972h-]53YP_615253103485692Patatin [ Sphingopyxis alaskensis RB2256]54ZP_010 . . .85708568hypothetical protein NAP1_04995 [ Erythrobacter sp. NAP1]55XP_65801267516253hypothetical protein AN0408.2 [ Aspergillus nidulans FGSC A4]56XP_44847050292075unnamed protein product [ Candida glabrata ]57XP_80728371409928hypothetical protein [ Trypanosoma cruzi strain CL Brener]58XP_38682146124535hypothetical protein FG06645.1 [ Gibberella zeae PH-1] TABLE 42Examples of acyl-coA-cholesterol polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_505086.150555355hypothetical protein [ Yarrowia lipolytica ].2XP_44980650294790hypothetical protein CAGL0M10571g [ Candida glabrataCBS138]3AAO3255428564940ARE2 [ Saccharomyces kluyveri ]4XP_46139550425599hypothetical protein DEHA0F25652g [ Debaryomyces hanseniiCBS767]5P8428556404462Sterol O-acyltransferase 2 (Sterol-ester synthase) (ASAT)6XP_71477668482533acyl-CoA cholesterol acyltransferase [ Candida albicansSC5314]7AAO3247428564191ARE2 [ Saccharomyces castellii ]8NP_98260645184888AAR065Cp [ Eremothecium gossypii ]9NP_0144166324346Acyl-CoA:sterol acyltransferase, isozyme of Are1p;endoplasmic reticulum enzyme that contributes the major sterolesterification activity in the presence of oxygen; Are2p[ Saccharomyces cerevisiae ]10AAC494411389739acyl-CoA:sterol acyltransferase11XP_45260750305295unnamed protein product [ Kluyveromyces lactis ]12Q876L234582301Sterol O-acyltransferase 2 (Sterol-ester synthase 2)13Q876L334582302Sterol O-acyltransferase 1 (Sterol-ester synthase 1)14AAT9294051013293YCR048W [ Saccharomyces cerevisiae ]15XP_44530750285757unnamed protein product [ Candida glabrata ]16NP_59370719114619hypothetical protein SPAC13G7.05 [ Schizosaccharomycespombe 972h-]17XP_37026839977761hypothetical protein MG06765.4 [ Magnaporthe grisea 70-15 ]18EAQ8461988177151hypothetical protein CHGG_08633 [ Chaetomium globosumCBS 148.51]19XP_96130085102248related to acyl-CoA sterol acyltransferase [ MIPS ] [ Neurosporacrassa OR74A]20XP_75035470991010sterol o-acyltransferase APE2 [ Aspergillus fumigatus Af293]21EAT80792111059672hypothetical protein SNOG_11748 [ Phaeosphaeria nodorumSN15]22XP_66181267527926hypothetical protein AN4208.2 [ Aspergillus nidulans FGSC A4]23BAE5493483764790unnamed protein product [ Aspergillus oryzae ]24EAT89521111068401predicted protein [ Phaeosphaeria nodorum SN15]25EAQ8609488178626hypothetical protein CHGG_07347 [ Chaetomium globosumCBS 148.51]26NP_58855819076058hypothetical protein SPCP1E11.05c [ Schizosaccharomycespombe 972h-]27XP_95657685080625hypothetical protein [ Neurospora crassa OR74A]28EAS3281590303184hypothetical protein CIMG_03839 [ Coccidioides immitis RS]29XP_38219246110268hypothetical protein FG02016.1 [ Gibberella zeae PH-1]30XP_76150271022545hypothetical protein UM05355.1 [ Ustilago maydis 521]31EAL2003250257323hypothetical protein CNBF3580 [ Cryptococcus neoformans var.neoformans B-3501A]32XP_57126058268208sterol O-acyltransferase [ Cryptococcus neoformans var.neoformans JEC21]33EAR8356189285549MBOAT family protein [ Tetrahymena thermophila SB210]34EAS0342489305436MBOAT family protein [ Tetrahymena thermophila SB210]35AAS7237545642961acyl-CoA:cholesterol acyltransferase alpha [ Toxoplasma gondii ]36AAS7237645642963acyl-CoA:cholesterol acyltransferase beta [ Toxoplasma gondii ]37XP_640280111226542hypothetical protein DDBDRAFT_0205259 [ Dictyosteliumdiscoideum AX4]38XP_64563366824557hypothetical protein DDBDRAFT_0202877 [ Dictyosteliumdiscoideum AX4]39EAS3550690305875hypothetical protein CIMG_00860 [ Coccidioides immitis RS]40XP_38686446124621hypothetical protein FG06688.1 [ Gibberella zeae PH-1]41NP_64981628571583CG8112-PA [ Drosophila melanogaster ]42CAE7517039591950Hypothetical protein CBG23107 [ Caenorhabditis briggsae ]43NP_03325684619697sterol O-acyltransferase 1 [ Mus musculus ]44BAC3492526342537unnamed protein product [ Mus musculus ]45XP_35945139939828hypothetical protein MG05326.4 [ Magnaporthe grisea 70-15]46Q6126318202591Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acylcoenzyme A:cholesterol acyltransferase 1) (ACAT-1)47XP_97514291083363PREDICTED: similar to CG31991-PA, isoform A [ Triboliumcastaneum ]48EAL2896254639560GA20833-PA [ Drosophila pseudoobscura ]49XP_95702285082953hypothetical protein [ Neurospora crassa OR74A]50XP_54744573961286PREDICTED: similar to Sterol O-acyltransferase 1 (Cholesterolacyltransferase 1) (Acyl coenzyme A:cholesterol acyltransferase1) (ACAT-1) [ Canis familiaris ]51EAQ8912488181656hypothetical protein CHGG_05743 [ Chaetomium globosumCBS 148.51]52EAT78735111057615hypothetical protein SNOG_13711 [ Phaeosphaeria nodorumSN15]53Q6045718202585Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acylcoenzyme A:cholesterol acyltransferase 1) (ACAT-1)54XP_624754110762262PREDICTED: similar to midway CG31991-PA, isoform A[ Apis mellifera ]55O7053618202126Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acylcoenzyme A:cholesterol acyltransferase 1) (ACAT-1)56XP_72898482915156hypothetical protein PY01256 [ Plasmodium yoelii yoelii str.17XNL]57NP_50582871997360H19N07.4 [ Caenorhabditis elegans ]58NP_001 . . .77735363hypothetical protein LOC504287 [ Bos taurus ]592201440A1585676acyl-CoA/cholesterol acyltransferase60XP_66376367539978hypothetical protein AN6159.2 [ Aspergillus nidulans FGSC A4]61CAI1357455960156sterol O-acyltransferase (acyl-Coenzyme A: cholesterolacyltransferase) 1 [ Homo sapiens ]62XP_51403055588858PREDICTED: hypothetical protein XP_514030 [ Pantroglodytes ]63AAL5622718028942cholesterol acyltransferase 1 [ Gorilla gorilla ]64AAL5622818028944cholesterol acyltransferase 1 [ Pongo pygmaeus ]65AAC375324878022acyl-coenzyme A: cholesterol acyltransferase [ Homo sapiens ]66EAT47694108883469sterol o-acyltransferase [ Aedes aegypti ]67XP_39003946136695hypothetical protein FG09863.1 [ Gibberella zeae PH-1]68BAE0104867969393unnamed protein product [ Macaca fascicularis ]69O7776118202178Sterol O-acyltransferase 1 (Cholesterol acyltransferase 1) (Acylcoenzyme A:cholesterol acyltransferase 1) (ACAT-1)70AAH0626334782946DGAT1 protein [ Homo sapiens ]71XP_31765631226099ENSANGP00000002281 [ Anopheles gambiae str. PEST]72XP_32032058393809ENSANGP00000016486 [ Anopheles gambiae str. PEST]73XP_32032158393811ENSANGP00000016512 [ Anopheles gambiae str. PEST]74BAE6530283775179unnamed protein product [ Aspergillus oryzae ]75NP_72401724584734midway CG31991-PC, isoform C [ Drosophila melanogaster ]76NP_99572445552403midway CG31991-PD, isoform D [ Drosophila melanogaster ]77EAL3359354644853GA16599-PA [ Drosophila pseudoobscura ]78NP_58614519074639STEROL O-ACYLTRANSFERASE [ Encephalitozoon cuniculiGB-M1]79XP_50255750550169hypothetical protein [ Yarrowia lipolytica ]80XP_88591476617939PREDICTED: similar to Sterol O-acyltransferase 2 (Cholesterolacyltransferase 2) (Acyl coenzyme A:cholesterol acyltransferase2) (ACAT-2) isoform 2 [ Bos taurus ]81XP_59125176617937PREDICTED: similar to Sterol O-acyltransferase 2 (Cholesterolacyltransferase 2) (Acyl coenzyme A:cholesterol acyltransferase2) (ACAT-2) isoform 1 [ Bos taurus ]82XP_62469166564061PREDICTED: similar to CG8112-PA [ Apis mellifera ]83O7590818202149Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acylcoenzyme A:cholesterol acyltransferase 2) (ACAT-2)84XP_001 . . .109096888PREDICTED: sterol O-acyltransferase 2 [ Macaca mulatta ]85AAK4882913898623acyl coenzyme A: cholesterol acyltransferase-2 [ Homo sapiens ]86AAH7791650416229Soat1-prov protein [ Xenopus laevis ]87AAH9609164654094Sterol O-acyltransferase 2 [ Homo sapiens ]88EAT38531108874306sterol o-acyltransferase [ Aedes aegypti ]89AAH9609064652990Sterol O-acyltransferase 2 [ Homo sapiens ]90NP_001 . . .50539976hypothetical protein LOC436731 [ Danio rerio ]91NP_71495040254723sterol O-acyltransferase 2 [ Rattus norvegicus ]92XP_42226750751122PREDICTED: similar to Sterol O-acyltransferase 1 (Cholesterolacyltransferase 1) (Acyl coenzyme A:cholesterol acyltransferase1) (ACAT-1) [ Gallus gallus ]93O8890818202245Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acylcoenzyme A:cholesterol acyltransferase 2) (ACAT-2)94O7775918202176Sterol O-acyltransferase 2 (Cholesterol acyltransferase 2) (Acylcoenzyme A:cholesterol acyltransferase 2) (ACAT-2)95NP_66617622122547sterol O-acyltransferase 2 [ Mus musculus ]96BAC0084621392392AcylCoA:Cholesterol Acyltransferase 2 [ Rattus norvegicus ]97XP_69285568364838PREDICTED: similar to Soatl-prov protein [ Danio rerio ]98XP_54363773996435PREDICTED: similar to sterol O-acyltransferase 2 [ Canisfamiliaris ]99CAG1194447225461unnamed protein product [ Tetraodon nigroviridis ]100CAF9651447222847unnamed protein product [ Tetraodon nigroviridis ]101CAG1081547219451unnamed protein product [ Tetraodon nigroviridis ]102EAR9464789296659MBOAT family protein [ Tetrahymena thermophila SB210]103AAP6832231711932At2g19450 [ Arabidopsis thaliana ]104EAR9444189296453MBOAT family protein [ Tetrahymena thermophila SB210]105CAG0799047225647unnamed protein product [ Tetraodon nigroviridis ]106XP_78820972085563PREDICTED: similar to sterol O-acyltransferase 1[ Strongylocentrotus purpuratus ]107AAO3247528564193ARE2 [ Saccharomyces castellii ]108XP_67312868062248hypothetical protein PB300300.00.0 [ Plasmodium berghei strainANKA] TABLE 43Examples of phospholipid-diacylglycerol polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50403850553256hypothetical protein [ Yarrowia lipolytica ].2XP_45889750420721hypothetical protein DEHA0D10868g [ Debaryomyces hanseniiCBS767]3XP_71887868473963hypothetical protein CaO19_13439 [ Candida albicans SC5314]4XP_44750150290139hypothetical protein CAGL0I05786g [ Candida glabrataCBS138]5XP_45536950310695unnamed protein product [ Kluyveromyces lactis ]6NP_0144056324335Acyltransferase that catalyzes diacylglycerol esterification; oneof several acyltransferases that contribute to triglyceridesynthesis; putative homolog of human lecithin cholesterolacyltransferase; Lro1p [ Saccharomyces cerevisiae ]7NP_98537145198342AFL179Cp [ Eremothecium gossypii ]8BAE5768483767545unnamed protein product [ Aspergillus oryzae ]9EAS3292890303297hypothetical protein CIMG_03952 [ Coccidioides immitis RS]10EAT89812111068692hypothetical protein SNOG_03081 [ Phaeosphaeria nodorumSN15]11XP_66259667537644hypothetical protein AN4992.2 [ Aspergillus nidulans FGSC A4]12XP_36101739942960hypothetical protein MG03560.4 [ Magnaporthe grisea 70-15]13CAD6071427803011unnamed protein product [ Podospora anserina ]14XP_71898068473754hypothetical protein CaO19_6018 [ Candida albicans SC5314]15XP_38655146123995hypothetical protein FG06375.1 [ Gibberella zeae PH-1]16XP_95959885092964hypothetical protein [ Neurospora crassa OR74A]17XP_75462470999814phospholipid:diacylglycerol acyltransferase [ Aspergillusfumigatus Af293]18O9468021362753Phospholipid:diacylglycerol acyltransferase (PDAT) ( PombeLRO1 homolog 1)19EAQ9221388184745hypothetical protein CHGG_00448 [ Chaetomium globosumCBS 148.51]20XP_75646971003606hypothetical protein UM00322.1 [ Ustilago maydis 521]21EAL1895350256226hypothetical protein CNBI2140 [ Cryptococcus neoformans var.neoformans B-3501A]22XP_56801458261208phospholipid:diacylglycerol acyltransferase [ Cryptococcusneoformans var. neoformans JEC21]23AAP4763537785695lecithine cholesterol acyltransferase-like protein [ Medicagotruncatula ]24AAS7959045935132putative phosphatidylcholine-sterol acyltransferase [ Ipomoeatrifida ]25BAF25212113631531Os09g0444200 [ Oryza sativa ( japonica cultivar-group)]26AAK9661915450695AT5g13640/MSH12_10 [ Arabidopsis thaliana ]27XP_82937974025626phospholipid:diacylglycerol acyltransferase-like protein[ Trypanosoma brucei TREU927]28XP_81655271655997phospholipid:diacylglycerol acyltransferase [ Trypanosoma cruzistrain CL Brener]29AAO1778737724553lecithine cholesterol acyltransferase-like protein [ Arabidopsisthaliana ]30XP_82175671660075phospholipid:diacylglycerol acyltransferase [ Trypanosoma cruzistrain CL Brener]31CAD3815327552462putative phosphatidylcholine-sterol acetyltransferase[ Physcomitrella patens ]32NP_19006915230521phosphatidylcholine-sterol O-acyltransferase [ Arabidopsisthaliana ]33CAD3815527552466putative acetyltransferase [ Physcomitrella patens ]34CAJ0284368124573phospholipid:diacylglycerol acyltransferase, putative[ Leishmania major ] TABLE 44Examples of malate dehydrogenase polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_503933.150553046hypothetical protein [ Yarrowia lipolytica ].2EAT83219111062099predicted protein [ Phaeosphaeria nodorum SN15]3XP_74755670984070malate dehydrogenase, NAD-dependent [ Aspergillusfumigatus Af293]4BAE6177683771646unnamed protein product [ Aspergillus oryzae ]5EAQ8901088181542malate dehydrogenase, mitochondrial precursor [ Chaetomiumglobosum CBS 148.51]6EAS3722690307595hypothetical protein CIMG_02580 [ Coccidioides immitis RS]7XP_57201358269714L-malate dehydrogenase [ Cryptococcus neoformans var.neoformans JEC21]8XP_74893670986899malate dehydrogenase, NAD-dependent [ Aspergillusfumigatus Af293]9BAE5550283765359unnamed protein product [ Aspergillus oryzae ]10EAQ8855388181085malate dehydrogenase, mitochondrial precursor [ Chaetomiumglobosum CBS 148.51]11ABH10641111606553malate dehydrogenase [ Coccidioides posadasii ]12XP_32116358395331ENSANGP00000020184 [ Anopheles gambiae str. PEST]13XP_71704768477790putative peroxisomal malate dehydrogenase [ Candida albicansSC5314]14AAY6397867043759mitochondrial malate dehydrogenase [ Lysiphlebus testaceipes ]15AAX1949660393102mitochondrial malate dehydrogenase 2b [ Xenopus laevis ]16EAT40089108875864malate dehydrogenase [ Aedes aegypti ]17AAI0669676780392Mdh2a protein [ Xenopus laevis ]18XP_57203858269764malate dehydrogenase [ Cryptococcus neoformans var.neoformans JEC21]19XP_39247866513092PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor isoform 1 [ Apis mellifera ]20XP_97353391085015PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor [ Tribolium castaneum ]21CAG1289447224065unnamed protein product [ Tetraodon nigroviridis ]22NP_001 . . .58332672mitochondrial malate dehydrogenase 2 [ Xenopus tropicalis ]23XP_81910471664243malate dehydrogenase [ Trypanosoma cruzi strain CL Brener]24CAJ0771568129178malate dehydrogenase [ Leishmania major ]25EAL2912454639722GA20754-PA [ Drosophila pseudoobscura ]26XP_70878268367713PREDICTED: similar to malate dehydrogenase, mitochondrialisoform 6 [ Danio rerio ]27XP_70877968367700PREDICTED: similar to malate dehydrogenase, mitochondrialisoform 3 [ Danio rerio ]28AAW7931958613465malate dehydrogenase [ Isochrysis galbana ]29CAI2960156403598hypothetical protein [ Pongo pygmaeus ]30XP_46075450424335hypothetical protein DEHA0F09911g [ Debaryomyceshansenii CBS767]31XP_001 . . .109066259PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor [ Macaca mulatta ]32AAK6976714583133malate dehydrogenase [ Sphyraena idiastes ]33XP_70877868367696PREDICTED: similar to malate dehydrogenase, mitochondrialisoform 2 [ Danio rerio ]34NP_001 . . .79327392PMDH2 [ Arabidopsis thaliana ]35ABE8479992877831Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Medicago truncatula ]36AAU2920052139820glyoxisomal malate dehydrogenase [ Lycopersiconesculentum ]37AAW2742556758570SJCHGC06124 protein [ Schistosoma japonicum ]38XP_70878168367709PREDICTED: similar to malate dehydrogenase, mitochondrialisoform 5 [ Danio rerio ]391SMKH60593494Chain H, Mature And Translocatable Forms Of GlyoxysomalMalate Dehydrogenase Have Different Activities AndStabilities But Similar Crystal Structures40XP_82250971746908mitochondrial malate dehydrogenase [ Trypanosoma bruceiTREU927]411SEVB60593476Chain B, Mature And Translocatable Forms Of GlyoxysomalMalate Dehydrogenase Have Different Activities AndStabilities But Similar Crystal Structures42XP_70878068367705PREDICTED: similar to malate dehydrogenase, mitochondrialisoform 4 [ Danio rerio ]43ABD7729089574129mitochondrial malate dehydrogenase 2, NAD [ Homo sapiens ]44ABD7728489574117mitochondrial malate dehydrogenase 2, NAD [ Rattusnorvegicus ]45ABD7728389574115mitochondrial malate dehydrogenase 2, NAD [ Mus musculus ]46ABD7728789574123mitochondrial malate dehydrogenase 2, NAD [ Oryctolaguscuniculus ]47ABD7728089574109mitochondrial malate dehydrogenase 2, NAD [ Loxodontaafricana ]48ABD7728889574125mitochondrial malate dehydrogenase 2, NAD [ Lepuseuropaeus ]49XP_79200472025672PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor [ Strongylocentrotus purpuratus ]50ABD7729389574135mitochondrial malate dehydrogenase 2, NAD [ Canisfamiliaris ]51ABD7729489574137mitochondrial malate dehydrogenase 2, NAD [ Felis catus ]52ABD7727889574105mitochondrial malate dehydrogenase 2, NAD [ Didelphisvirginiana ]53XP_80921071414199mitochondrial malate dehydrogenase [ Trypanosoma cruzistrain CL Brener]54ABD7730189574151mitochondrial malate dehydrogenase 2, NAD [ Sus scrofa ]55ABD7728689574121mitochondrial malate dehydrogenase 2, NAD [ Mesocricetusauratus ]56ABD7729889574145mitochondrial malate dehydrogenase 2, NAD [ Bos taurus ]57AAT3523047531133mitochondrial malate dehydrogenase [ Clonorchis sinensis ]58ABD7728189574111mitochondrial malate dehydrogenase 2, NAD [ Dasypusnovemcinctus ]59ABD7729689574141mitochondrial malate dehydrogenase 2, NAD [ Ceratotheriumsimum ]60ABA99939108863014Malate dehydrogenase, glyoxysomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]61AAU2919852139816mitochondrial malate dehydrogenase [ Lycopersiconesculentum ]62ABD7727989574107mitochondrial malate dehydrogenase 2, NAD [ Sminthopsisdouglasi ]63CAJ0771768129180malate dehydrogenase, putative [ Leishmania major ]64XP_51916055628772PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor [ Pan troglodytes ]65ABD7270289473780putative mitochondrial malate dehydrogenase [ Acyrthosiphonpisum ]66ABD7729989574147mitochondrial malate dehydrogenase 2, NAD [ Balaenopteraphysalus ]67BAF23792113623847Os08g0434300 [ Oryza sativa ( japonica cultivar-group)]68CAI1136157337458putative malate dehydrogenase [ Orpinomyces sp. OUS1]69ABD7728989574127mitochondrial malate dehydrogenase 2, NAD [ Tadaridabrasiliensis ]70BAF06605113534222Os01g0829800 [ Oryza sativa ( japonica cultivar-group)]71ABD7729289574133mitochondrial malate dehydrogenase 2, NAD [ Tupaia glis ]72ABD7728589574119mitochondrial malate dehydrogenase 2, NAD [ Caviaporcellus ]73BAF18303113579940Os05g0574400 [ Oryza sativa ( japonica cultivar-group)]74ZP_010 . . .85712491malate dehydrogenase [ Idiomarina baltica OS145]75XP_53971857097207PREDICTED: similar to malate dehydrogenase 2, NAD(mitochondrial) [ Canis familiaris ]76ABD7727789574103mitochondrial malate dehydrogenase 2, NAD [ Monodelphisdomestica ]77Q5R03062286970Malate dehydrogenase78YP_660122109896867malate dehydrogenase, NAD-dependent [ Pseudoalteromonasatlantica T6c]79Q87SU748428249Malate dehydrogenase80ABD7729189574131mitochondrial malate dehydrogenase 2, NAD [ Aotustrivirgatus ]81ZP_007 . . .75854582COG0039: Malate/lactate dehydrogenases [ Vibrio sp. Ex25]82ZP_011 . . .88795318malate dehydrogenase [ Alteromonas macleodii ‘Deepecotype’]83ZP_012 . . .91228842malate dehydrogenase [ Vibrio alginolyticus 12G01]84ZP_011 . . .89075547malate dehydrogenase [ Photobacterium sp. SKA34]85ZP_012 . . .90580811malate dehydrogenase [ Vibrio angustum S14]86YP_671200110643470malate dehydrogenase [ Escherichia coli 536]87ABD7729589574139mitochondrial malate dehydrogenase 2, NAD [ Equus caballus ]88Q5E87566774139Malate dehydrogenase89ZP_007 . . .75209673COG0039: Malate/lactate dehydrogenases [ Escherichia coliB171]90ZP_009 . . .84394039malate dehydrogenase [ Vibrio splendidus 12B01]91ZP_007 . . .75228638COG0039: Malate/lactate dehydrogenases [ Escherichia coliB7A]92ZP_010 . . .86147822malate dehydrogenase [ Vibrio sp. MED222]93BAD3006450508045malate dehydrogenase [ Moritella sp. 36B1]94Q4QL8973621201Malate dehydrogenase95YP_40489382778544malate dehydrogenase [ Shigella dysenteriae Sd197]96BAD3005950508035malate dehydrogenase [ Moritella sp. 47A1]97BAD3006650508049malate dehydrogenase [ Moritella sp. 36G1]98ZP_008 . . .77958772COG0039: Malate/lactate dehydrogenases [ Yersiniabercovieri ATCC 43970]99BAD3007150508059malate dehydrogenase [ Moritella sp. 38F1]100ZP_008 . . .77973999COG0039: Malate/lactate dehydrogenases [ Yersiniafrederiksenii ATCC 33641]101ZP_008 . . .77977600COG0039: Malate/lactate dehydrogenases [ Yersiniaintermedia ATCC 29909]102P483641346511Malate dehydrogenase103BAD3006250508041malate dehydrogenase [ Moritella sp. 16H2]104BAD3006950508055malate dehydrogenase [ Moritella ]sp. 56A1]105ZP_008 . . .77961850COG0039: Malate/lactate dehydrogenases [ Yersinia mollaretiiATCC 43969]106ZP_012 . . .90411956putative malate dehydrogenase [ Photobacterium profundum3TCK]107Q6AW2157012891Malate dehydrogenase108Q57JA968052390Malate dehydrogenase109ZP_012 . . .90407531malate dehydrogenase [ Psychromonas sp. CNPT3]110BAD3674651172588malate dehydrogenase [ Moritella yayanosii ]111Q6AW2357012892Malate dehydrogenase112ABG22106108863015Malate dehydrogenase, glyoxysomal precursor, putative,expressed [ Oryza sativa ( japonica cultivar-group)]113ZP_005 . . .68546610Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Shewanella amazonensis SB2B]114BAD3006050508037malate dehydrogenase [ Moritella sp. 47B1]115EAL3100854642259GA10540-PA [ Drosophila pseudoobscura ]116YP_736674114046124malate dehydrogenase, NAD-dependent [ Shewanella sp. MR-7]117CAJ0771668129179malate dehydrogenase, putative [ Leishmania major ]118ZP_009 . . .82743617Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Shewanella sp. W3-18-1]119Q47VL083288301Malate dehydrogenase120ZP_011 . . .88859032malate dehydrogenase [ Pseudoalteromonas tunicata D2]121YP_56183891792187malate dehydrogenase, NAD-dependent [ Shewanelladenitrificans OS217]122ZP_005 . . .68544347Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Shewanella baltica OS155]123ZP_007 . . .75429373malate dehydrogenase [ Actinobacillus succinogenes 130Z]124AAW2994056788316malate dehydrogenase [ Pasteurella trehalosi ]125BAD3006350508043malate dehydrogenase [ Shewanella sp. T4609]126EAL3100954642260GA10541-PA [ Drosophila pseudoobscura ]127ZP_006 . . .69950735Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Shewanella frigidimarina NCIMB400]128YP_34114877361573malate dehydrogenase [ Pseudoalteromonas haloplanktisTAC125]129ZP_013 . . .106882260malate dehydrogenase, NAD-dependent [ Psychromonasingrahamii 37]130BAD3006850508053malate dehydrogenase [ Shewanella sp. 33H2]131ZP_008 . . .78368581Malate dehydrogenase, NAD-dependent, eukaryotes andgamma proteobacteria [ Shewanella sp. PV-4]132XP_85110574004024PREDICTED: similar to malate dehydrogenase, mitochondrial[ Canis familiaris ]133ABD7730089574149mitochondrial malate dehydrogenase 2, NAD [ Hippopotamusamphibius ]134XP_81694871656813glycosomal malate dehydrogenase [ Trypanosoma cruzi strainCL Brener]135CAJ1959682655060malate dehydrogenase [ Klebsiella pneumoniae ]136AAW2993956788314malate dehydrogenase [ Mannheimia glucosida ]137CAJ1958382655034malate dehydrogenase [ Klebsiella pneumoniae ]138CAJ1958982655046malate dehydrogenase [ Klebsiella pneumoniae ]139CAJ1958082655028malate dehydrogenase [ Klebsiella pneumoniae ]140CAJ1959182655050malate dehydrogenase [ Klebsiella pneumoniae ]141CAJ1959582655058malate dehydrogenase [ Klebsiella pneumoniae ]142CAJ1959382655054malate dehydrogenase [ Klebsiella pneumoniae ]143AAW2993756788310malate dehydrogenase [ Mannheimia haemolytica ]144XP_81246771423452glycosomal malate dehydrogenase [ Trypanosoma cruzi strainCL Brener]145AAW2993856788312malate dehydrogenase [ Mannheimia haemolytica ]146AAW2993656788308malate dehydrogenase [ Mannheimia haemolytica ]147XP_84985873993436PREDICTED: similar to malate dehydrogenase, mitochondrial[ Canis familiaris ]148AAW2804856718658malate dehydrogenase [ Vibrio cholerae ]149AAU8899852856248malate dehydrogenase [ Shigella flexneri ]150AAW2804156718644malate dehydrogenase [ Vibrio cholerae ]151AAW2804756718656malate dehydrogenase [ Vibrio mimicus ]152AAW2804556718652malate dehydrogenase [ Vibrio mimicus ]153ABD7728289574113mitochondrial malate dehydrogenase 2, NAD [ Tamanduatetradactyla ]154AAU8901852856288malate dehydrogenase [ Shigella boydii ]155AAU8900352856258malate dehydrogenase [ Escherichia coli ]156AAU8896052856172malate dehydrogenase [ Escherichia coli ]157AAU8896252856176malate dehydrogenase [ Shigella flexneri ]158AAU8899652856244malate dehydrogenase [ Escherichia coli ]159AAU8897252856196malate dehydrogenase [ Shigella boydii ]160AAU8896952856190malate dehydrogenase [ Shigella boydii ]161ZP_007 . . .75822170COG0039: Malate/lactate dehydrogenases [ Vibrio choleraeRC385]162AAU8906252856376malate dehydrogenase [ Shigella boydii ]163AAU8898252856216malate dehydrogenase [ Shigella dysenteriae ]164AAU8899552856242malate dehydrogenase [ Escherichia coli ]165AAU8899352856238malate dehydrogenase [ Escherichia coli ]166AAU8904452856340malate dehydrogenase [ Shigella flexneri ]167AAU8901552856282malate dehydrogenase [ Shigella boydii ]168AAU8897152856194malate dehydrogenase [ Shigella sonnei ]169AAW2803456718629malate dehydrogenase [ Vibrio cholerae ]170AAU8901152856274malate dehydrogenase [ Shigella flexneri ]171AAU8895852856168malate dehydrogenase [ Escherichia coli ]172AAU8897652856204malate dehydrogenase [ Shigella dysenteriae ]173AAU8899152856234malate dehydrogenase [ Escherichia coli ]174XP_85081873988067PREDICTED: similar to mitochondrial malate dehydrogenaseprecursor [ Canis familiaris ]175AAU8655052697626malate dehydrogenase [ Shigella boydii ]176AAU8897952856210malate dehydrogenase [ Shigella dysenteriae ]177AAU8900552856262malate dehydrogenase [ Escherichia coli ]178AAU8901952856290malate dehydrogenase [ Shigella dysenteriae ]179AAU8898352856218malate dehydrogenase [ Shigella dysenteriae ]180AAU8654952697624malate dehydrogenase [ Escherichia albertii ]181AAX8584262532910Mdh [ Escherichia coli ]182AAU8900752856266malate dehydrogenase [ Shigella flexneri ]183AAU8898052856212malate dehydrogenase [ Shigella flexneri ]184AAU8900052856252malate dehydrogenase [ Shigella flexneri ]185AAU8896852856188malate dehydrogenase [ Shigella boydii ]186AAU8898852856228malate dehydrogenase [ Escherichia coli ]187AAX8585662532938Mdh [ Escherichia coli ]188AAU8656652697658malate dehydrogenase [ Shigella boydii ]189AAU8657152697668malate dehydrogenase [ Escherichia albertii ]190ABF2015094468239Mdh [ Escherichia coli ]191AAU8905152856354malate dehydrogenase [ Shigella boydii ]192AAU8905952856370malate dehydrogenase [ Shigella boydii ]193AAU8905752856366malate dehydrogenase [ Shigella boydii ]194AAU8903652856324malate dehydrogenase [ Shigella flexneri ]195AAU8655952697644malate dehydrogenase [ Shigella boydii ]196ABF2015194468241Mdh [ Escherichia coli ]197ABF2014294468223Mdh [ Escherichia coli ]198AAU8899052856232malate dehydrogenase [ Escherichia coli ]199AAU8656752697660malate dehydrogenase [ Shigella boydii ]200AAU8903252856316malate dehydrogenase [ Shigella dysenteriae ]201AAU8901252856276malate dehydrogenase [ Shigella flexneri ] TABLE 45Examples of glucose-6-phosphate dehydrogenase polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50427550553728hypothetical protein [ Yarrowia lipolytica ]2XP_36508139965237hypothetical protein MG09926.4 [ Magnaporthe grisea 70-15]3XP_38145546108794G6PD_ASPNG Glucose-6-phosphate 1-dehydrogenase(G6PD) [ Gibberella zeae PH-1]4XP_66058567525047glucose-6-phosphate 1-dehydrogenase [ Aspergillus nidulansFGSC A4]5P488261346070Glucose-6-phosphate 1-dehydrogenase (G6PD)6CAA548401523782glucose-6-phosphate 1-dehydrogenase [ Aspergillus niger ]7EAU38380114196680glucose-6-phosphate 1-dehydrogenase [ Aspergillus terreusNIH2624]8EAT83608111062488predicted protein [ Phaeosphaeria nodorum SN15]9EAS2891590299284glucose-6-phosphate 1-dehydrogenase [ Coccidioides immitisRS]10XP_75476771000100glucose-6-phosphate 1-dehydrogenase [ Aspergillus fumigatusAf293]11XP_95832085090234GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE (G6PD)[ Neurospora crassa OR74A]12EAQ9337088185902glucose-6-phosphate 1-dehydrogenase [ Chaetomiumglobosum CBS 148.51]13CAA58825642160unnamed protein product [ Emericella nidulans ]14XP_45812950419213hypothetical protein DEHA0C11286g [ Debaryomyceshansenii CBS767]15AAB25541299248glucose-6-phosphate dehydrogenase [ Pichia jadinii = yeast,Peptide, 495 aa]16XP_72325168465104putative glucose-6-phosphate dehydrogenase [ Candidaalbicans SC5314]17XP_72344068464725putative glucose-6-phosphate dehydrogenase [ Candidaalbicans SC5314]18XP_45394450307901G6PD_KLULA [ Kluyveromyces lactis ]19NP_98274145185024ABL206Cp [ Eremothecium gossypii ]20XP_44803850291211unnamed protein product [ Candida glabrata ]21XP_57204558269778glucose-6-phosphate 1-dehydrogenase [ Cryptococcusneoformans var. neoformans JEC21]22NP_0141586324088Glucose-6-phosphate dehydrogenase (G6PD), catalyzes thefirst step of the pentose phosphate pathway; involved inadapting to oxidatve stress; homolog of the human G6PDwhich is deficient in patients with hemolytic anemia; Zwf1p[ Saccharomyces cerevisiae ]23AAT9301751013447YNL241C [ Saccharomyces cerevisiae ]24AAA34619171545glucose-6-phosphate dehydrogenase (ZWF1) (EC 1.1.1.49)25XP_76107771021693hypothetical protein UM04930.1 [ Ustilago maydis 521]26NP_59334463054535glucose-6-phosphate 1-dehydrogenase [ Schizosaccharomycespombe 972h-]27XP_64481466822919glucose 6-phosphate-1-dehydrogenase [ Dictyosteliumdiscoideum AX4]28ABD7251989357348glucose 6-phosphate dehydrogenase [ Trypanosoma cruzi ]29BAE99888110735823glucose-6-phosphate dehydrogenase [ Arabidopsis thaliana ]30CAB526755732197glucose-6-phosphate 1-dehydrogenase [ Arabidopsis thaliana ]31CAB087462104434SPAC3A12.18 [ Schizosaccharomyces pombe ]32ABD7251789357344glucose 6-phosphate dehydrogenase [ Trypanosoma cruzi ]33ABD7251889357346glucose 6-phosphate dehydrogenase [ Trypanosoma cruzi ]34BAB9675721262179glucose-6-phosphate dehydrogenase 1 [ Chlorella vulgaris ]35XP_82250271746894glucose-6-phosphate 1-dehydrogenase [ Trypanosoma bruceiTREU927]36CAJ0770868129171glucose-6-phosphate dehydrogenase [ Leishmania major ]37CAC0781610045209glucose-6-phosphate 1-dehydrogenase [ Trypanosoma brucei ]38BAF15046113564703Os04g0485300 [ Oryza sativa ( japonica cultivar-group)]39AAO3782528261397glucose-6-phosphate dehydrogenase [ Leishmania mexicana ]40AAM6422827434608glucose-6-phosphate dehydrogenase [ Leishmania mexicanaamazonensis ]41XP_001 . . .110750934PREDICTED: similar to Zwischenferment CG12529-PA,isoform A [ Apis mellifera ]42XP_97409691082561PREDICTED: similar to CG12529-PA, isoform A [ Triboliumcastaneum ]43ABE8395992876243Glucose-6-phosphate dehydrogenase [ Medicago truncatula ]44BAE3807774138546unnamed protein product [ Mus musculus ]45NP_001 . . .79313844G6PD5; glucose-6-phosphate 1-dehydrogenase [ Arabidopsisthaliana ]46CAB526745732195glucose-6-phosphate 1-dehydrogenase [ Arabidopsis thaliana ]47AAD114264206114cytoplasmic glucose-6-phosphate 1-dehydrogenase[ Mesembryanthemum crystallinum ]48Q429193023815Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform(G6PD)49AAL7995919071787glucose-6-phosphate dehydrogenase [ Oryza sativa ( japonicacultivar-group)]50CAE6205439593761Hypothetical protein CBG06072 [ Caenorhabditis briggsae ]51EAL3161954642875GA11679-PA [ Drosophila pseudoobscura ]52Q0061254037161Glucose-6-phosphate 1-dehydrogenase X (G6PD)53AAH7566349523350Glucose-6-phosphate dehydrogenase X-linked [ Musmusculus ]54AAB693192352923cytosolic glucose-6-phosphate dehydrogenase 2 [ Petroselinumcrispum ]55AAM6423027434612glucose-6-phosphate dehydrogenase [ Leishmania guyanensis ]56ABB2956478183137putative Zwischenferment [ Drosophila yakuba ]57AAL5768818086470AT3g27300/K17E12_12 [ Arabidopsis thaliana ]58NP_72828724643352Zwischenferment CG12529-PB, isoform B [ Drosophilamelanogaster ]59EAT38627108874402glucose-6-phosphate 1-dehydrogenase [ Aedes aegypti ]60AAR2630389214190glucose-6-phosphate dehydrogenase [ Populus suaveolens ]61AAA990731304700glucose-6-phosphate 1-dehydrogenase [ Drosophilamelanogaster ]62AAK9350315292469SD03244p [ Drosophila melanogaster ]63AAB028091304686glucose-6-phosphate 1-dehydrogenase [ Drosophilamelanogaster ]64NP_52341124643350Zwischenferment CG12529-PA, isoform A [ Drosophilamelanogaster ]65AAA991071305086glucose-6-phosphate 1-dehydrogenase [ Drosophilamelanogaster ]66ABB2956278183133putative Zwischenferment [ Drosophila simulans ]67NP_50212917538218B0035.5 [ Caenorhabditis elegans ]68AAZ2385071089991glucose-6-phosphate dehydrogenase [ Boophilus microplus ]69P37830585165Glucose-6-phosphate 1-dehydrogenase, cytoplasmic isoform(G6PD)70AAB028121304692glucose-6-phosphate 1-dehydrogenase [ Drosophilamelanogaster ]71ABB5538681075965glucose-6-phosphate 1-dehydrogenase cytoplasmic isoform-like [ Solanum tuberosum ]72CAJ8368389273424glucose-6-phosphate dehydrogenase [ Xenopus tropicalis ]73NP_001 . . .62859893glucose-6-phosphate dehydrogenase 2 [ Xenopus tropicalis ]74ABB2956378183135putative Zwischenferment [ Drosophila teissieri ]75AAX4578561394184glucose-6-phosphate dehydrogenase isoform B [ Ipstypographus ]76AAX4578461394183glucose-6-phosphate dehydrogenase isoform A [ Ipstypographus ]77AAH8182051980296Glucose-6-phosphate dehydrogenase X-linked [ Rattusnorvegicus ]78XP_31145258381765ENSANGP00000018551 [ Anopheles gambiae str. PEST]79XP_53820974009187PREDICTED: similar to Glucose-6-phosphate 1-dehydrogenase (G6PD) [ Canis familiaris ]80AAH59324111185531Unknown (protein for MGC: 69058) [ Xenopus laevis ]81ABB2956078183129putative Zwischenferment [ Drosophila erecta ]82Q276383023810Glucose-6-phosphate 1-dehydrogenase (G6PD)83Q294922494652Glucose-6-phosphate 1-dehydrogenase (G6PD)84BAF09259113536876Os02g0600400 [ Oryza sativa ( japonica cultivar-group)]85O5504462510568Glucose-6-phosphate 1-dehydrogenase (G6PD)86CAA049933021510glucose-6-phosphate dehydrogenase [ Nicotiana tabacum ]87ABB2956178183131putative Zwischenferment [ Drosophila orena ]88BAA976628918502glucose-6-phosphate dehydrogenase [ Triticum aestivum ]89BAD1792046849421glucose-6-phosphate 1-dehydrogenase [ Acipenser baerii ]90XP_69916868440567PREDICTED: similar to glucose-6-phosphate dehydrogenase[ Danio rerio ]91AAB963632734869glucose-6-phosphate dehydrogenase [ Takifugu rubripes ]92NP_000393109389365glucose-6-phosphate dehydrogenase isoform a [ Homo sapiens ]93NP_001 . . .108773793glucose-6-phosphate dehydrogenase isoform b [ Homosapiens ]94AAA52500182871glucose-6-phosphate dehydrogenase variant A-(EC 1.1.1.49)95P11413120731Glucose-6-phosphate 1-dehydrogenase (G6PD)96AAA926531203978G6PD [ Homo sapiens ]97AAX4333561369430glucose-6-phosphate dehydrogenase [synthetic construct]98P415711169799Glucose-6-phosphate 1-dehydrogenase (G6PD)(Zwischenferment)992BHLB66361518Chain B, X-Ray Structure Of Human Glucose-6-PhosphateDehydrogenase (Deletion Variant) Complexed With Glucose-6-Phosphate100ABC7452785700174glucose-6-phosphate dehydrogenase [ Populus trichocarpa ]101ABC7452885700176glucose-6-phosphate dehydrogenase [ Populus trichocarpa ]102AAA51463157470glucose-6-phosphate dehydrogenase103XP_001 . . .109132852PREDICTED: glucose-6-phosphate dehydrogenase isoform 1[ Macaca mulatta ]1041QKIH7546530Chain H, X-Ray Structure Of Human Glucose 6-PhosphateDehydrogenase (Variant Canton R4591) Complexed WithStructural Nadp+105XP_001 . . .109132850PREDICTED: glucose-6-phosphate dehydrogenase isoform 2[ Macaca mulatta ]106BAA976638918504glucose-6-phosphate dehydrogenase [ Triticum aestivum ]107CAA049923021508glucose-6-phosphate dehydrogenase [ Nicotiana tabacum ]108AAB693182352921cytosolic glucose-6-phosphate dehydrogenase 1 [ Petroselinumcrispum ]109XP_30709558375370ENSANGP00000012074 [ Anopheles gambiae str. PEST]110AAA41179204197glucose-6-phosphate dehydrogenase111AAA63175182890glucose-6-phosphate dehydrogenase [ Homo sapiens ]112BAA976648918506glucose-6-phosphate dehydrogenase [ Triticum aestivum ]113AAW2482356753227SJCHGC02527 protein [ Schistosoma japonicum ]114CAA585905459313glucose-6-phosphate 1-dehydrogenase [ Takifugu rubripes ]115CAG0745147228719unnamed protein product [ Tetraodon nigroviridis ]116CAJ28912113207852glucose-6-phosphate 1-dehydrogenase [ Crassostrea gigas ]117ABC2588183628088glucose-6-phosphate 1-dehydrogenase [ Homo sapiens ]118ABC2598183628208glucose-6-phosphate 1-dehydrogenase [ Homo sapiens ]119ABC2582683628022glucose-6-phosphate 1-dehydrogenase [ Homo sapiens ]120BAD1791246849405glucose-6-phosphate 1-dehydrogenase [ Amia calva ]121BAD1787746849335glucose-6-phosphate 1-dehydrogenase [ Protopterus annectens ]122BAD1794746849475glucose-6-phosphate 1-dehydrogenase [ Callorhinchuscallorynchus ]123AAI20828111306848Glucose-6-phosphate dehydrogenase 2 [ Mus musculus ]124BAD1792746849435glucose-6-phosphate 1-dehydrogenase [ Polypterusornatipinnis ]125BAD1789846849377glucose-6-phosphate 1-dehydrogenase [ Oryzias latipes ]126BAD1789146849363glucose-6-phosphate 1-dehydrogenase [ Ambystomamexicanum ]127BAD1795146849483glucose-6-phosphate 1-dehydrogenase [ Lethenteron reissneri ]128AAF190307629275glucose-6-phosphate-1-dehydrogenase; G6PD [ Pimephalespromelas ]129BAD1794146849463glucose-6-phosphate 1-dehydrogenase [ Potamotrygon motoro ]130BAD1795446849489glucose-6-phosphate 1-dehydrogenase [ Branchiostomabelcheri ]131BAD1790546849391glucose-6-phosphate 1-dehydrogenase [ Lepisosteus osseus ]132BAD1788446849349glucose-6-phosphate 1-dehydrogenase [ Lepidosiren paradoxa ]133BAD1793446849449glucose-6-phosphate 1-dehydrogenase [ Cephaloscylliumumbratile ]134ABC7452985700178glucose-6-phosphate dehydrogenase [ Populus trichocarpa ]135CAB526855734379plastidic glucose-6-phosphate dehydrogenase [ Dunaliellabioculata ]136Q437933023817Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor(G6PD)137AAF872169392607plastidic glucose 6-phosphate dehydrogenase [ Nicotianatabacum ]138BAC2304124745908glucose 6-phosphate dehydrogenase [ Solanum tuberosum ]139CAB527085734502glucose-6-phosphate 1-dehydrogenase [ Solanum tuberosum ]140BAF21344113610966Os07g0406300 [ Oryza sativa ( japonica cultivar-group)]141AAQ0267133304517putative plastidic glucose-6-phosphate dehydrogenase [ Oryzasativa ( japonica cultivar-group)]142AAW8264358803037hepatic glucose-6-phosphate dehydrogenase [ Rhabdosargussarba ]143BAF12270113548827Os03g0412800 [ Oryza sativa ( japonica cultivar-group)]144AAN7214425083966glucose-6-phosphate dehydrogenase [ Arabidopsis thaliana ]145AAB693172352919plastidic glucose-6-phosphate dehydrogenase [ Petroselinumcrispum ]146O243573334193Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor(G6PD)147AAO2359727764952At1g24280/F3I6_22 [ Arabidopsis thaliana ]148Q8L74325452975Glucose-6-phosphate 1-dehydrogenase 3, chloroplastprecursor (G6PD3) (G6PDH3)149CAA590111166405glucose-6-phosphate 1-dehydrogenase [ Arabidopsis thaliana ]150CAA590121174336glucose-6-phosphate 1-dehydrogenase [ Arabidopsis thaliana ]151CAC054399955555glucose-6-phosphate 1-dehydrogenase [ Arabidopsis thaliana ]152Q9FY9925452980Glucose-6-phosphate 1-dehydrogenase 2, chloroplastprecursor (G6PD2) (G6PDH2)153AAL5767818086448AT5g13110/T19L5_70 [ Arabidopsis thaliana ]154Q438393023818Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor(G6PD)155CAA046963021305plastidic glucose-6-phosphate dehydrogenase [ Arabidopsisthaliana ]156CAB526815734372glucose-6-phosphate 1-dehydrogenase [ Cyanidium caldarium ]157CAA049943021532glucose-6-phosphate dehydrogenase [ Nicotiana tabacum ]158Q7YS3762510624Glucose-6-phosphate 1-dehydrogenase (G6PD)159CAG0405947229307unnamed protein product [ Tetraodon nigroviridis ]160CAD2886229149997glucose 6 phosphate dehydrogenase [ Acraea encedana ]161CAD2886329149999glucose 6 phosphate dehydrogenase [ Acraea encedana ]162AAM6423127434614glucose-6-phosphate dehydrogenase [ Leishmania braziliensis ]163AAG2872811066848glucose-6-phosphate-dehydrogenase [ Drosophila mauritiana ]164AAG2873011066852glucose-6-phosphate-dehydrogenase [ Drosophila sechellia ]165ABF96583108708788Glucose-6-phosphate 1-dehydrogenase, chloroplast precursor,putative, expressed [ Oryza sativa ( japonica cultivar-group)]166CAA039412276348Glucose-6-phosphate dehydrogenase [ Spinacia oleracea ]167XP_58362876658972PREDICTED: similar to Glucose-6-phosphate 1-dehydrogenase (G6PD) [ Bos taurus ]168AAA52499182869glucose-6-phosphate dehydrogenase169AAM6422927434610glucose-6-phosphate dehydrogenase [ Leishmania mexicana ]170NP_58774919075249hypothetical protein SPCC794.01c [ Schizosaccharomycespombe 972h-]171AAR1294538156652glucose-6-phosphate dehydrogenase [ Drosophila mojavensis ]172AAR1295338156668glucose-6-phosphate dehydrogenase [ Drosophila mojavensis ]173AAR1294638156654glucose-6-phosphate dehydrogenase [ Drosophila mojavensis ]174AAR1294338156648glucose-6-phosphate dehydrogenase [ Drosophila mojavensis ]175AAR1295238156666glucose-6-phosphate dehydrogenase [ Drosophila mojavensis ]176BAF11858113548415Os03g0318500 [ Oryza sativa ( japonica cultivar-group)]177XP_55925257942974ENSANGP00000028421 [ Anopheles gambiae str. PEST]178NP_59361419114526hypothetical protein SPAC3C7.13c [ Schizosaccharomycespombe 972h-]179BAD9474362321397glucose-6-phosphate dehydrogenase [ Arabidopsis thaliana ]180CAJ2038195007160glucose-6-phosphate-1-dehydrogenase [ Toxoplasma gondii ]181YP_60543794986073glucose-6-phosphate 1-dehydrogenase [ Deinococcusgeothermalis DSM 11300]182CAE5122837651949glucose 6 phosphate dehydrogenase [ Adalia bipunctata ]183YP_00782046446455putative glucose-6-phosphate [ Candidatus Protochlamydiaamoebophila UWE25]184NP_29531915806604glucose-6-phosphate 1-dehydrogenase [ Deinococcusradiodurans R1]185CAE5122237651937glucose 6 phosphate dehydrogenase [ Adalia bipunctata ]186CAE5122937651951glucose 6 phosphate dehydrogenase [ Adalia decempunctata ]187ZP_007 . . .76260057Glucose-6-phosphate dehydrogenase [ Chloroflexusaurantiacus J-10-fl]188ZP_002 . . .47096622glucose-6-phosphate 1-dehydrogenase [ Listeriamonocytogenes str. ½a F6854]189ZP_004 . . .66965919Glucose-6-phosphate dehydrogenase [ Arthrobacter sp. FB24 ]190ZP_002 . . .47093301glucose-6-phosphate 1-dehydrogenase [ Listeriamonocytogenes str. 4b H7858]191NP_47141916801151hypothetical protein lin2085 [ Listeria innocua Clip11262]192NP_69386023100393glucose-6-phosphate 1-dehydrogenase [ Oceanobacillusiheyensis HTE831]193NP_82940529840299glucose-6-phosphate 1-dehydrogenase [ Chlamydophila caviaeGPIC]194CAJ7104191203388strongly similar to glucose-6-phosphate dehydrogenase[ Candidatus Kuenenia stuttgartiensis ]195YP_629214108761123glucose-6-phosphate 1-dehydrogenase [ Myxococcus xanthusDK 1622]196ZP_009 . . .84387050glucose-6-phosphate 1-dehydrogenase [ Vibrio splendidus12B01]197ZP_011 . . .88856188glucose-6-phosphate 1-dehydrogenase [marineactinobacterium PHSC20C1]198NP_82748929832855glucose-6-phosphate 1-dehydrogenase [ Streptomycesavermitilis MA-4680]199CAH1010488319768putative glucose-6-phosphate-1-dehydrogenase [ Streptomycessp. SCC 2136]200YP_14818756420869glucose-6-phosphate 1-dehydrogenase [ Geobacilluskaustophilus HTA426]201ZP_006 . . .71368421Glucose-6-phosphate dehydrogenase [ Nocardioides sp. JS614] TABLE 46Examples of 6-phosphogluconate dehydrogenase polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50093850546937hypothetical protein [ Yarrowia lipolytica ].2XP_45872650420381hypothetical protein DEHA0D06820g [ Debaryomyceshansenii CBS767]3XP_45140850302941unnamed protein product [ Kluyveromyces lactis ]4O1328733341106-phosphogluconate dehydrogenase, decarboxylating5XP_72222768467588hypothetical protein CaO19_5024 [ Candida albicans SC5314]6NP_01205363219776-phosphogluconate dehydrogenase (decarboxylating),catalyzes an NADPH regenerating reaction in the pentosephosphate pathway; required for growth on D-glucono-delta-lactone and adaptation to oxidative stress; Gnd1p[ Saccharomyces cerevisiae ]7AAO3239628564035GND1 [ Saccharomyces bayanus ]8XP_750696709916956-phosphogluconate dehydrogenase, decarboxylating[ Aspergillus fumigatus Af293]9CAD80254294099636-phosphogluconate dehydrogenase [ Aspergillus niger ]10XP_66155867526993hypothetical protein AN3954.2 [ Aspergillus nidulans FGSCA4]11AAO3245628564155GND1 [ Saccharomyces servazzii ]12AAO3249728564385GND1 [ Saccharomyces castellii ]13BAE5734983767210unnamed protein product [ Aspergillus oryzae ]14AAT9283051013073YGR256W [ Saccharomyces cerevisiae ]15XP_44992350295024hypothetical protein CAGL0M13343g [ Candida glabrataCBS138]16NP_98567645198647AFR129Wp [ Eremothecium gossypii ]17EAS35799903061686-phosphogluconate dehydrogenase, decarboxylating[ Coccidioides immitis RS]18XP_75872471014537hypothetical protein UM02577.1 [ Ustilago maydis 521]19O60037122296356-phosphogluconate dehydrogenase, decarboxylating20XP_96495985115938hypothetical protein [ Neurospora crassa OR74A]21XP_38128746108458hypothetical protein FG01111.1 [ Gibberella zeae PH-1]22EAT76717111055597predicted protein [ Phaeosphaeria nodorum SN15]23XP_36906939975357hypothetical protein MG00175.4 [ Magnaporthe grisea 70-15]24XP_56779358260766phosphogluconate dehydrogenase (decarboxylating)[ Cryptococcus neoformans var. neoformans JEC21]25NP_595095191118876-phosphogluconate dehydrogenase [ Schizosaccharomycespombe 972h-]26EAQ9260888185140hypothetical protein CHGG_00843 [ Chaetomium globosumCBS 148.51]27T4252311251352probable phosphogluconate dehydrogenase (decarboxylating)(EC 1.1.1.44) - fission yeast ( Schizosaccharomyces pombe )(fragment)28XP_78139472005545PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating [ Strongylocentrotus purpuratus ]29BAD98151630037206-phosphogluconate dehydrogenase [ Ascidia sydneiensissamea ]30XP_62509066547531PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating, partial [ Apis mellifera ]31CAG3230353134115hypothetical protein [ Gallus gallus ]322PGD999886Chain, 6-Phosphogluconate Dehydrogenase (6-Pgdh)(E.C.1.1.1.44)33NP_001 . . .571641796-phosphogluconate dehydrogenase (decarboxylating) [ Ovisaries ]34XP_91164082896232PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating isoform 6 [ Mus musculus ]35BAE3157774225286unnamed protein product [ Mus musculus ]36AAX4335961369608phosphogluconate dehydrogenase [synthetic construct]37CAI9575166347393phosphogluconate dehydrogenase [ Homo sapiens ]38XP_99347894374014PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating isoform 4 [ Mus musculus ]39AAH1132915030150Phosphogluconate dehydrogenase [ Mus musculus ]40AAI0217973586529LOC514939 protein [ Bos taurus ]41AAA75302984325phosphogluconate dehydrogenase [ Homo sapiens ]42AAH5995837747616MGC68486 protein [ Xenopus laevis ]43ZP_005 . . .679311086-phosphogluconate dehydrogenase, decarboxylating[ Solibacter usitatus Ellin6076]44EAT425571088783326-phosphogluconate dehydrogenase [ Aedes aegypti ]45XP_53541173950940PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating isoform 1 [ Canis familiaris ]46XP_31309158384192ENSANGP00000012857 [ Anopheles gambiae str. PEST]47CAG0754647228814unnamed protein product [ Tetraodon nigroviridis ]48YP_007316464459516-phosphogluconate dehydrogenase [ CandidatusProtochlamydia amoebophila UWE25]49NP_99871747087205phosphogluconate hydrogenase isoform 2 [ Danio rerio ]50XP_97205191094851PREDICTED: similar to phosphogluconate hydrogenaseisoform 2 [ Tribolium castaneum ]51CAE7084839594980Hypothetical protein CBG17632 [ Caenorhabditis briggsae ]52XP_001 . . .94372948PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating isoform 9 [ Mus musculus ]53NP_99861847087439phosphogluconate hydrogenase isoform 1 [ Danio rerio ]54AAH9557163102189Pgd protein [ Danio rerio ]55XP_99344694374016PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating isoform 3 [ Mus musculus ]56EAL3150054642755GA17642-PA [ Drosophila pseudoobscura ]57Q17761749624146-phosphogluconate dehydrogenase, decarboxylating58P4157311682336-phosphogluconate dehydrogenase, decarboxylating59AAL9018519528141AT26455p [ Drosophila melanogaster ]60NP_47686024639279Phosphogluconate dehydrogenase CG3724-PA [ Drosophilamelanogaster ]61NP_001 . . .1140532536-phosphogluconate dehydrogenase [ Bombyx mori ]62P4157011682286-phosphogluconate dehydrogenase, decarboxylating63CAJ43391951402476-phosphogluconate dehydrogenase [ Bactrocera oleae ]64CAJ43390951402456-phosphogluconate dehydrogenase [ Ceratitis capitata ]65AAP9264833086672Cc2-27 [ Rattus norvegicus ]66YP_6616821098984276-phosphogluconate dehydrogenase, decarboxylating[ Pseudoalteromonas atlantica T6c]67XP_59285976637462PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating [ Bos taurus ]68YP_526109900202826-phosphogluconate dehydrogenase, decarboxylating[ Saccharophagus degradans 2-40]69ZP_001 . . .53733078COG0362: 6-phosphogluconate dehydrogenase [ Haemophilusinfluenzae R2846]70NP_761502273659746-phosphogluconate dehydrogenase [ Vibrio vulnificusCMCP6]71YP_391484784855596-phosphogluconate dehydrogenase, decarboxylating[ Thiomicrospira crunogena XCL-2]72YP_248262682491506-phosphogluconate dehydrogenase [ Haemophilus influenzae86-028NP]73NP_934400376797916-phosphogluconate dehydrogenase [ Vibrio vulnificus YJ016]74ZP_007 . . .75857693COG0362: 6-phosphogluconate dehydrogenase [ Vibrio sp.Ex25]75NP_798087288984826-phosphogluconate dehydrogenase [ Vibrio parahaemolyticusRIMD 2210633]76YP_206428597136536-phosphogluconate dehydrogenase [ Vibrio fischeri ES114]77ZP_001 . . .53733322COG0362: 6-phosphogluconate dehydrogenase [ Haemophilusinfluenzae R2866]78ZP_012 . . .912244366-phosphogluconate dehydrogenase [ Vibrio alginolyticus12G01]79AAB203772393836-phosphogluconate dehydrogenase [sheep, Peptide, 466 aa]80ZP_010 . . .861458836-phosphogluconate dehydrogenase [ Vibrio sp. MED222]81ZP_007 . . .75432781Phosphogluconate dehydrogenase (decarboxylating)[ Actinobacillus succinogenes 130Z]82ZP_001 . . .46143450COG0362: 6-phosphogluconate dehydrogenase[ Actinobacillus pleuropneumoniae serovar 1 str. 4074]83ZP_012 . . .905789576-phosphogluconate dehydrogenase [ Vibrio angustum S14]84YP_087205524240686-phosphogluconate dehydrogenase [ Mannheimiasucciniciproducens MBEL55E]85ZP_011 . . .890730096-phosphogluconate dehydrogenase [ Photobacterium sp .SKA34]86NP_273081156759636-phosphogluconate dehydrogenase [ Neisseria meningitidisMC58]87ZP_007 . . .75825242COG0362: 6-phosphogluconate dehydrogenase [ Vibriocholerae O395]88ZP_007 . . .75822319COG0362: 6-phosphogluconate dehydrogenase [ Vibriocholerae RC385]89ZP_007 . . .75831146COG0362: 6-phosphogluconate dehydrogenase [ Vibriocholerae MO10]90YP_7198591134617906-phosphogluconate dehydrogenase [ Haemophilus somnus129PT]91ZP_012 . . .904118286-phosphogluconate dehydrogenase [ Photobacteriumprofundum 3TCK]92YP_129657543086376-phosphogluconate dehydrogenase [ Photobacteriumprofundum SS9]93ZP_001 . . .53728695COG0362: 6-phosphogluconate dehydrogenase [ Haemophilussomnus 2336]94BAD36766512417576-phosphogluconate dehydrogenase [ Cyanidioschyzonmerolae ]95P7071824924946-phosphogluconate dehydrogenase, decarboxylating96XP_642122668162256-phosphogluconate dehydrogenase (decarboxylating)[ Dictyostelium discoideum AX4]97Q7VMX4711522056-phosphogluconate dehydrogenase, decarboxylating98NP_283102157932806-phosphogluconate dehydrogenase [ Neisseria meningitidisZ2491]99NP_246493156034196-phosphogluconate dehydrogenase [ Pasteurella multocidasubsp. multocida str. Pm70]100AAO19943275730876-phosphogluconate dehydrogenase, decarboxylating[ Neisseria gonorrhoeae ]101AAO19944275730896-phosphogluconate dehydrogenase, decarboxylating[ Neisseria gonorrhoeae ]102YP_208939598022276-phosphogluconate dehydrogenase [ Neisseria gonorrhoeaeFA 1090]103AAO19934275730696-phosphogluconate dehydrogenase, decarboxylating[ Neisseria gonorrhoeae ]104AAO19942275730856-phosphogluconate dehydrogenase, decarboxylating[ Neisseria gonorrhoeae ]105ZP_013 . . .1068816746-phosphogluconate dehydrogenase, decarboxylating[ Psychromonas ingrahamii 37]106XP_51567055599346PREDICTED: similar to 6-phosphogluconate dehydrogenase,decarboxylating [ Pan troglodytes ]107ZP_010 . . .873094976-phosphogluconate dehydrogenase [ Blastopirellula marinaDSM 3645]108NP_865160324721666-phosphogluconate dehydrogenase [ Rhodopirellula balticaSH 1]109AAW29923567882826-phosphogluconate dehydrogenase [ Mannheimiahaemolytica ]110AAW29924567882846-phosphogluconate dehydrogenase [ Mannheimia glucosida ]111AAW29925567882866-phosphogluconate dehydrogenase [ Pasteurella trehalosi ]112NP_218771156393226-phosphogluconate dehydrogenase [ Treponema pallidumsubsp. pallidum str. Nichols]113YP_148197564208796-phosphogluconate dehydrogenase [ Geobacillus kaustophilusHTA426]114YP_35634877918533probable phosphogluconate dehydrogenase (decarboxylating)[ Pelobacter carbinolicus DSM 2380]115NP_390267508122646-phosphogluconate dehydrogenase [ Bacillus subtilis subsp.subtilis str. 168]116YP_092134527863056-phosphogluconate dehydrogenase [ Bacillus licheniformisATCC 14580]117ZP_011 . . .890990106-phosphogluconate dehydrogenase [ Bacillus sp. NRRL B-14911]118NP_691106230976406-phosphogluconate dehydrogenase [ Oceanobacillus iheyensisHTE831]119YP_219832621850476-phosphogluconate dehydrogenase [ Chlamydophila abortusS26/3]120ZP_002 . . .475653656-phosphogluconate dehydrogenase, decarboxylating [ Bacilluscereus G9241]121YP_026451491831996-phosphogluconate dehydrogenase [ Bacillus anthracis str.Sterne]122YP_034514494767316-phosphogluconate dehydrogenase [ Bacillus thuringiensisserovar konkukian str. 97-27]123YP_081773521450566-phosphogluconate dehydrogenase [ Bacillus cereus E33L]124YP_515493898983836-phosphogluconate dehydrogenase [ Chlamydophila felisFe/C-56]125NP_814782293756286-phosphogluconate dehydrogenase [ Enterococcus faecalisV583]126ZP_003 . . .65317607COG0362: 6-phosphogluconate dehydrogenase [ Bacillusanthracis str. A2012]127YP_175422569636916-phosphogluconate dehydrogenase [ Bacillus clausii KSM-K16]128ZP_006 . . .692473516-phosphogluconate dehydrogenase, decarboxylating[ Enterococcus faecium DO]129NP_810135293466326-phosphogluconate dehydrogenase [ Bacteroidesthetaiotaomicron VPI-5482]130NP_829300298401946-phosphogluconate dehydrogenase [ Chlamydophila caviaeGPIC]131AAL76325186446786-phosphogluconate dehydrogenase [ Porphyra yezoensis ]132YP_546705917769496-phosphogluconate dehydrogenase, decarboxylating[ Methylobacillus flagellatus KT]133ZP_004 . . .675461186-phosphogluconate dehydrogenase, decarboxylating[ Burkholderia vietnamiensis G4]134Q9CHU6182028026-phosphogluconate dehydrogenase, decarboxylating135ZP_006 . . .740149556-phosphogluconate dehydrogenase, decarboxylating[ Burkholderia ambifaria AMMD]136YP_372936780630286-phosphogluconate dehydrogenase [ Burkholderia sp. 383 ]137YP_6243141070268036-phosphogluconate dehydrogenase, decarboxylating[ Burkholderia cenocepacia AU 1054]138NP_928851375255076-phosphogluconate dehydrogenase [ Photorhabdusluminescens subsp. laumondii TTO1]139ZP_002 . . .470959606-phosphogluconate dehydrogenase, decarboxylating [ Listeriamonocytogenes str. ½a F6854]140YP_438830837176306-phosphogluconate dehydrogenase, decarboxylating[ Burkholderia thailandensis E264]141P9678981342946-phosphogluconate dehydrogenase, decarboxylating142NP_924063375206866-phosphogluconate dehydrogenase [ Gloeobacter violaceusPCC 7421]143AAA242071469386-phosphogluconate dehydrogenase144ZP_009 . . .84360352COG0362: 6-phosphogluconate dehydrogenase [ Burkholderiadolosa AUO158]145YP_335987768178866-phosphogluconate dehydrogenase [ Burkholderiapseudomallei 1710b]146AAA244951475016-phosphogluconate dehydrogenase147NP_310857158320846-phosphogluconate dehydrogenase [ Escherichia coliO157:H7 str. Sakai]148ZP_009 . . .83571257COG0362: 6-phosphogluconate dehydrogenase [ Shigelladysenteriae 1012]149ZP_007 . . .75229110COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli B7A]150ZP_013 . . .100915196hypothetical protein Bmal10_03003493 [ Burkholderia mallei10399]151AAG35219114645186-phosphogluconate dehydrogenase [ Escherichia coli ]152ZP_013 . . .100236192hypothetical protein Bpse4_03000697 [ Burkholderiapseudomallei 406e]153YP_6699721106422426-phosphogluconate dehydrogenase, decarboxylating[ Escherichia coli 536]154ZP_013 . . .100062231hypothetical protein BpseP_03002198 [ Burkholderiapseudomallei Pasteur]155YP_114383538039946-phosphogluconate dehydrogenase [ Methylococcuscapsulatus str. Bath]156AAA242081469406-phosphogluconate dehydrogenase157YP_31099174312572gluconate-6-phosphate dehydrogenase, decarboxylating[ Shigella sonnei Ss046]158ZP_003 . . .48870455COG0362: 6-phosphogluconate dehydrogenase [ Pediococcuspentosaceus ATCC 25745]159ZP_007 . . .75514070COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli 53638]160YP_049550501203836-phosphogluconate dehydrogenase [ Erwinia carotovorasubsp. atroseptica SCRI1043]161AP_00263089108850gluconate-6-phosphate dehydrogenase, decarboxylating[ Escherichia coli W3110]162ZP_007 . . .75259178COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli E22]163YP_541301912113156-phosphogluconate dehydrogenase, decarboxylating[ Escherichia coli UTI89]164YP_013993469076046-phosphogluconate dehydrogenase [ Listeria monocytogenesstr. 4b F2365]165YP_40378882777439gluconate-6-phosphate dehydrogenase [ Shigella dysenteriaeSd197]166ZP_009 . . .83588030COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli 101-1]167AAD5049257394706-phosphogluconate dehydrogenase Gnd [ Escherichia coli ]168ZP_006 . . .75177157COG0362: 6-phosphogluconate dehydrogenase [ Shigellaboydii BS512]169AAA242091469426-phosphogluconate dehydrogenase170AAG35221114645226-phosphogluconate dehydrogenase [ Escherichia coli ]171ZP_007 . . .75186836COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli E24377A]172YP_689521110806001gluconate-6-phosphate dehydrogenase [ Shigella flexneri 5 str.8401]173ZP_008 . . .77959279COG0362: 6-phosphogluconate dehydrogenase [ Yersiniabercovieri ATCC 43970]174AAG35224114645286-phosphogluconate dehydrogenase [ Escherichia coli ]175ZP_007 . . .77636293COG0362: 6-phosphogluconate dehydrogenase [ Yersiniapestis Angola]176ZP_008 . . .77962467COG0362: 6-phosphogluconate dehydrogenase [ Yersiniamollaretii ATCC 43969]177ZP_008 . . .77978861COG0362: 6-phosphogluconate dehydrogenase [ Yersiniaintermedia ATCC 29909]178AAG35218114645166-phosphogluconate dehydrogenase [ Escherichia coli ]179BAA7773648679276-phosphogluconate dehydrogenase [ Escherichia coli ]180AAA244901474916-phosphogluconate dehydrogenase181YP_6483671088126006-phosphogluconate dehydrogenase, decarboxylating[ Yersinia pestis Nepal516]182NP_669932221265096-phosphogluconate dehydrogenase [ Yersinia pestis KIM]183AAA239181462326-phosphogluconate dehydrogenase (EC 1.1.1.44)184CAJ7104291203389strongly similar to 6-phosphogluconate dehydrogenase(decarboxylating) [ Candidatus Kuenenia stuttgartiensis ]185AAA242061469366-phosphogluconate dehydrogenase186AAA244941474996-phosphogluconate dehydrogenase187AAA244921474956-phosphogluconate dehydrogenase188YP_099135537131436-phosphogluconate dehydrogenase [ Bacteroides fragilisYCH46]189AAA239251462466-phosphogluconate dehydrogenase190YP_211552606814086-phosphogluconate dehydrogenase [ Bacteroides fragilisNCTC 9343]191AAV7438156122509Gnd [ Escherichia coli ]192NP_992794454412556-phosphogluconate dehydrogenase [ Yersinia pestis biovarMicrotus str. 91001]193YP_6507491088068336-phosphogluconate dehydrogenase, decarboxylating[ Yersinia pestis Antiqua]194NP_876643332417026-phosphogluconate dehydrogenase [ Chlamydophilapneumoniae TW-183]195NP_357929159023796-phosphogluconate dehydrogenase [ Streptococcuspneumoniae R6]196ZP_014 . . .111658214hypothetical protein SpneT_02000606 [ Streptococcuspneumoniae TIGR4]197NP_782446282115026-phosphogluconate dehydrogenase [ Clostridium tetani E88]198AAG35223114645266-phosphogluconate dehydrogenase [ Escherichia coli ]199AAA244931474976-phosphogluconate dehydrogenase200ZP_007 . . .75214880COG0362: 6-phosphogluconate dehydrogenase [ Escherichiacoli E110019] TABLE 47Examples of Fructose 1,6 bisphosphatase polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1XP_50011150545147hypothetical protein [ Yarrowia lipolytica ].2AAP8529432492043fructose-1,6-bisphosphatase [ Yarrowia lipolytica ]3XP_46041050423651hypothetical protein DEHA0F01309g [ Debaryomyceshansenii CBS767]4CAC6913915528447putative fructose-1,6-bisphosphatase [ Pichia anomala ]5XP_44742550289987hypothetical protein CAGL0I04048g [ Candida glabrataCBS138]6NP_98614045199111AFR593Cp [ Eremothecium gossypii ]7XP_45400350308005F16P_KLULA [ Kluyveromyces lactis ]8EAT78213111057093predicted protein [ Phaeosphaeria nodorum SN15]9XP_71093468490480fructose-1,6-bisphosphatase [ Candida albicans SC5314]10AAT9283551013083YLR377C [ Saccharomyces cerevisiae ]11XP_36405039954137hypothetical protein MG08895.4 [ Magnaporthe grisea 70-15]12NP_001. . .68006542fructose-1,6-bisphosphatase [ Schizosaccharomyces pombe972h-]13NP_59508319111875hypothetical protein SPBC1198.14c [ Schizosaccharomycespombe 972h-]14XP_75169870993702fructose-1,6-bisphosphatase [ Aspergillus fumigatus Af293]15XP_44701050289161unnamed protein product [ Candida glabrata ]16BAE5818583768046unnamed protein product [ Aspergillus oryzae ]17EAQ8492488177456conserved hypothetical protein [ Chaetomium globosum CBS148.51]18AAF346936980006fructose 1,6-bisphosphatase [ Candida albicans ]19BAB122089955389fructose-1,6-bisphosphatase [ Aspergillus oryzae ]20XP_66320867538868hypothetical protein AN5604.2 [ Aspergillus nidulans FGSCA4]21XP_38945646134281conserved hypothetical protein [ Gibberella zeae PH-1]22XP_96042385097320hypothetical protein [ Neurospora crassa OR74A]23EAS3619290306561fructose-1,6-bisphosphatase [ Coccidioides immitis RS]24XP_56647558258125fructose-bisphosphatase [ Cryptococcus neoformans var.neoformans JEC21]25XP_75885071015920hypothetical protein UM02703.1 [ Ustilago maydis 521]26P14766119748Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)27AAZ8653873811203fructose 1,6-bisphosphatase [ Brassica rapa subsp. pekinensis ]28Q9MA7975312318Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)29Q9SDL875313310Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)30BAD8191656785198fructose-1,6-bisphosphatase [ Oryza sativa ( japonica cultivar-group)]31P462671169585Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)32P462761169586Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase) (CY-F1)33Q8RW9975303233Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)34Q4313976363515Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)35CAB460845305145fructose-1,6-bisphosphatase [ Pisum sativum ]36BAF06820113534437Os01g0866400 [ Oryza sativa ( japonica cultivar-group)]37Q4264976789650Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)38Q9XF4775315047Fructose-1,6-bisphosphatase, cytosolic (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)39CAA61409895909fructose-1,6-bisphosphatase [ Saccharum hybrid cultivar H65-7052]401906373A444324cytosolic fructose bisphosphatase41EAR8734789289359fructose-1,6-bisphosphatase family protein [ Tetrahymenathermophila SB210]42NP_91564134908588fructose-1,6-bisphosphatase [ Oryza sativa ( japonica cultivar-group)]43XP_47531450931573putative fructose-1,6-bisphosphatase [ Oryza sativa ( japonicacultivar-group)]44NP_49100417508131K07A3.1 [ Caenorhabditis elegans ]45XP_78241172013871PREDICTED: similar to fructose-1,6-bisphosphatase 1, like[ Strongylocentrotus purpuratus ]46CAE6053839595500Hypothetical protein CBG04165 [ Caenorhabditis briggsae ]47NP_61000119921562fructose-1,6-bisphosphatase CG31692-PA, isoform A[ Drosophila melanogaster ]48NP_72422345550998fructose-1,6-bisphosphatase CG31692-PB, isoform B[ Drosophila melanogaster ]49XP_31993758393257ENSANGP00000016841 [ Anopheles gambiae str. PEST]50AAN3147123394363fructose-1 6-biphosphatase [ Phytophthora infestans]51XP_42504050762393PREDICTED: similar to fructose 1,6-bisphosphatase [ Gallusgallus ]52EAT47721108883496fructose-1,6-bisphosphatase [ Aedes aegypti ]53EAT47722108883497fructose-1,6-bisphosphatase [ Aedes aegypti ]54AAH5378432450356Fbp-prov protein [ Xenopus laevis ]55YP_00165945657573fructose-1,6-bisphosphatase [ Leptospira interrogans serovarCopenhageni str. Fiocruz L1-130]56NP_98914545361017Fructose-1,6-bisphosphatase [ Xenopus tropicalis ]571YZ0B62738852Chain B, R-State Amp Complex Reveals Initial Steps Of TheQuaternary Transition Of Fructose-1,6-Bisphosphatase581Q9DB39654661Chain B, Fructose-1,6-Bisphosphatase Complexed With ANew Allosteric Site Inhibitor (I-State)59NP_99914447522784fructose 1,6-bisphosphatase [ Sus scrofa ]60EAL3280754644065GA16400-PA [ Drosophila pseudoobscura ]61XP_84830673946392PREDICTED: similar to fructose-1,6-bisphosphatase 1isoform 3 [ Canis familiaris ]621FJ9B11514534Chain B, Fructose-1,6-Bisphosphatase (Mutant Y57w)ProductsZNAMP Complex (T-State)631LEVF24987566Chain F, Porcine Kidney Fructose-1,6-BisphosphataseComplexed With An Amp-Site Inhibitor641BK4A6729708Chain A, Crystal Structure Of Rabbit Liver Fructose-1,6-Bisphosphatase At 2.3 Angstrom Resolution65Q3SZB7110808224Fructose-1,6-bisphosphatase 1 (D-fructose-1,6-bisphosphate1-phosphohydrolase 1) (FBPase 1)66AAA41131310111fructose-biphosphatase67P462752506391Fructose-1,6-bisphosphatase, chloroplast precursor (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)682F3HB99032142Chain B, Mechanism Of Displacement Of A CatalyticallyEssential Loop From The Active Site Of Fructose-1,6-Bisphosphatase69NP_03669051036635fructose-1,6-biphosphatase 1 [ Rattus norvegicus ]70AAC255973288991fructose-1,6-bisphosphatase [ Sus scrofa ]71XP_96780291077758PREDICTED: similar to CG31692-PA, isoform A [ Triboliumcastaneum ]72AAK5992914318171fructose-1,6-bisphosphatase [ Pisum sativum ]731DCUD6730314Chain D, Redox Signaling In The Chloroplast: Structure OfOxidized Pea Fructose-1,6-Bisphosphate Phosphatase741DBZD6730306Chain D, C153s Mutant Of Pea Fructose-1,6-Bisphosphatase75CAB397594539148fructose-1,6-bisphosphatase [ Pisum sativum ]76P0919920141075Fructose-1,6-bisphosphatase 1 (D-fructose-1,6-bisphosphate1-phosphohydrolase 1) (FBPase 1)77CAA4871920717fructose-bisphosphatase [ Pisum sativum ]781FPIB1633402Chain B, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) Complexed With Amp,2,5-Anhydro-D-Glucitol-1,6-Bisphosphate And PotassiumIons (100 Mm)79AAB30523546354fructose-1,6-biphosphatase, FBPase {EC 3.1.3.11} [ Pisumsativum = peas, Lincoln, Peptide Chloroplast, 357 aa]801KZ8F24987484Chain F, Crystal Structure Of Porcine Fructose-1,6-Bisphosphatase Complexed With A Novel Allosteric-SiteInhibitor81AAW2541656754457SJCHGC06706 protein [ Schistosoma japonicum ]821FRPB809402Chain B, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11) ComplexedWith Fructose-2,6-Bisphosphate, Adenosine Monophosphate(Amp), And Zinc83XP_42503950762391PREDICTED: similar to fructose-1,6-bisphosphatase [ Gallusgallus ]84NP_99829747085885fructose-1,6-bisphosphatase 1 [ Danio rerio ]851RDZB1942591Chain B, T-State Structure Of The Arg 243 To Ala Mutant OfPig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli861FSAB2554913Chain B, The T-State Structure Of Lys 42 To Ala Mutant OfThe Pig Kidney Fructose 1,6-Bisphosphatase Expressed In E. Coli87BAE2894074146344unnamed protein product [ Mus musculus ]88CAG0521647228396unnamed protein product [ Tetraodon nigroviridis ]89NP_95623641053949fructose-1,6-bisphosphatase 1, like [ Danio rerio ]90Q07204585118Fructose-1,6-bisphosphatase, chloroplast precursor (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)91BAF11578113548135Os03g0267300 [ Oryza sativa ( japonica cultivar-group)]922FIXL90109451Chain L, Structure Of Human Liver Fbpase Complexed WithPotent Benzoxazole Allosteric Inhibitiors932FHYL90109424Chain L, Structure Of Human Liver Fpbase Complexed WithA Novel Benzoxazole As Allosteric Inhibitor94XP_001 . . .109112377PREDICTED: fructose-1,6-bisphosphatase 1 isoform 2[ Macaca mulatta ]951FTAD1311149Chain D, Fructose-1,6-Bisphosphatase(D-Fructose-1,6-Bisphosphate, 1-Phosphohydrolase) (E.C.3.1.3.11) ComplexedWith The Allosteric Inhibitor Amp96CAH7269255662224fructose-1,6-bisphosphatase 1 [ Homo sapiens ]97CAG0819047221528unnamed protein product [ Tetraodon nigroviridis ]98XP_53350473946534PREDICTED: similar to Fructose-1,6-bisphosphatase isozyme2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)[ Canis familiaris ]99AAC257743293553fructose-1,6-bisphosphatase [ Homo sapiens ]100AAA35817182311fructose-1,6-bisphosphatase101AAD122434218951fructose-1,6-bisphosphatase precursor [ Brassica napus ]102NP_001 . . .114051459hypothetical protein LOC514066 [ Bos taurus ]103P09195119745Fructose-1,6-bisphosphatase, chloroplast precursor (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)104NP_001 . . .57524507hypothetical protein LOC445505 [ Danio rerio ]105NP_001. . .114051287fructose-1,6-bisphosphatase [ Bombyx mori ]106NP_001. . .73853862hypothetical protein LOC613108 [ Xenopus tropicalis ]107AAD255414585576fructose-1,6-bisphosphatase precursor [ Solanum tuberosum ]108Q9N0J675067927Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (FBPase 2)109AAN3188423397203putative fructose-bisphosphatase precursor [ Arabidopsisthaliana ]110AAH8122951703601Unknown (protein for MGC: 85456) [ Xenopus laevis ]111P224183915687Fructose-1,6-bisphosphatase, chloroplast precursor (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)112CAA4115411242fructose-bisphosphatase [ Arabidopsis thaliana ]113XP_001. . .109112375PREDICTED: fructose-1,6-bisphosphatase 1 isoform 1[ Macaca mulatta ]114P7069576363514Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (FBPase 2) (RAE-30)115CAG0818947221527unnamed protein product [ Tetraodon nigroviridis ]116AAI13633109731177Fructose-1,6-bisphosphatase 2 [ Homo sapiens ]1171SPID999624Chain D, Fructose-1,6-Bisphosphatase (D-Fructose-1,6-Bisphosphate 1-Phosphohydrolase) (E.C.3.1.3.11)118AAF729738118281fructose-1,6-bisphosphatase [ Zaocys dhumnades ]119AAH1272015215255Fbp2 protein [ Mus musculus ]120O0075776789651Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (FBPase 2)121XP_82719671745132fructose-1,6-bisphosphate cytosolic [ Trypanosoma bruceiTREU927]122Q9Z1N176364186Fructose-1,6-bisphosphatase isozyme 2 (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (FBPase 2)123BAE4030674212301unnamed protein product [ Mus musculus ]124CAC7074715718373fructose-1,6-bisphosphatase [ Trypanosoma brucei ]125NP_0320206679761fructose bisphosphatase 2 [ Mus musculus ]126AAP7919232307574fructose-1,6 bisphosphatase [ Bigelowiella natans ]127ZP_010. . .86130901fructose-1,6-bisphosphatase [ Cellulophaga sp. MED134]128YP_42202483311760Fructose-1,6-bisphosphatase [ Magnetospirillum magneticumAMB-1]129YP_679484110639275fructose-1,6-bisphosphatase [ Cytophaga hutchinsonii ATCC33406]130ZP_000. . .23014308COG0158: Fructose-1,6-bisphosphatase [ Magnetospirillummagnetotacticum MS-1]131XP_88862776363832Leishmania major strain Friedlin cytosolic fructose-1,6-bisphosphatase [ Leishmania major strain Friedlin]132ZP_009. . .83855881fructose-1,6-bisphosphatase [ Croceibacter atlanticusHTCC2559]133YP_43751683649081Fructose-1,6-bisphosphatase [ Hahella chejuensis KCTC 2396]134ZP_011. . .88711300fructose-1,6-bisphosphatase [ Flavobacteriales bacteriumHTCC2170]135CAC8280016519317fructose 1,6-bisphosphatase [ Galdieria sulphuraria ]136ZP_012. . .91215105fructose-1,6-bisphosphatase [ Psychroflexus torquis ATCC700755]137ZP_012. . .90591576Inositol phosphatase/fructose-1,6-bisphosphatase[ Flavobacterium johnsoniae UW101]138XP_79345272046390PREDICTED: similar to fructose-1,6-bisphosphatase 1, like[ Strongylocentrotus purpuratus ]139CAJ7222391202584strongly similar to fructose-1,6-bisphosphatase [ CandidatusKuenenia stuttgartiensis ]140ZP_011. . .88804197fructose-1,6-bisphosphatase [ Robiginitalea biformataHTCC2501]141YP_44559883815956fructose-1,6-bisphosphatase [ Salinibacter ruber DSM 13855]142ZP_007. . .75815977COG0158: Fructose-1,6-bisphosphatase [ Vibrio cholerae V52]143ZP_011. . .88802508fructose-1,6-bisphosphatase [ Polaribacter irgensii 23-P]144ZP_007. . .75827798COG0158: Fructose-1,6-bisphosphatase [ Vibrio choleraeO395]145ZP_011. . .88797163Fructose-1,6-bisphosphatase [ Reinekea sp. MED297]146ZP_005. . .68553442Inositol phosphatase/fructose-1,6-bisphosphatase[ Prosthecochloris aestuarii DSM 271]147ZP_007. . .75830525COG0158: Fructose-1,6-bisphosphatase [ Vibrio choleraeMO10]148Q427962494415Fructose-1,6-bisphosphatase, chloroplast precursor (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (FBPase)149ZP_007. . .75822783COG0158: Fructose-1,6-bisphosphatase [ Vibrio choleraeRC385]150NP_93322737678618fructose-1,6-bisphosphatase [ Vibrio vulnificus YJ016]151XP_81263671423971fructose-1,6-bisphosphatase, cytosolic [ Trypanosoma cruzistrain CL Brener]152ZP_006. . .71480926Inositol phosphatase/fructose-1,6-bisphosphatase[ Prosthecochloris vibrioformis DSM 265]153ZP_007. . .75854570COG0158: Fructose-1,6-bisphosphatase [ Vibrio sp. Ex25]154NP_93171437528369fructose-1,6-bisphosphatase [ Photorhabdus luminescenssubsp. laumondii TTO1]155XP_80583971406635fructose-1,6-bisphosphatase, cytosolic [ Trypanosoma cruzistrain CL Brener]156YP_37439278186349fructose-1,6-bisphosphatase [ Pelodictyon luteolum DSM 273]157NP_90209734497882fructose-1,6-bisphosphatase [ Chromobacterium violaceumATCC 12472]158XP_64632366825937D-fructose-1,6-bisphosphate 1-phosphohydrolase[ Dictyostelium discoideum AX4]159ZP_010. . .86147594fructose-1,6-bisphosphatase [ Vibrio sp. MED222]160NP_79669128897086fructose-1,6-bisphosphatase [ Vibrio parahaemolyticus RIMD2210633]161YP_05201450122847fructose-1,6-bisphosphatase [ Erwinia carotovora subsp.atroseptica SCRI1043]162ZP_007. . .77634762COG0158: Fructose-1,6-bisphosphatase [ Yersinia pestisAngola]163ZP_012. . .90406722fructose-1,6-bisphosphatase [ Psychromonas sp. CNPT3]164ZP_006. . .71549000Inositol phosphatase/fructose-1,6-bisphosphatase[ Nitrosomonas eutropha C71]165ZP_013. . .106882698Inositol phosphatase/fructose-1,6-bisphosphatase[ Psychromonas ingrahamii 37]166ZP_008. . .77973994COG0158: Fructose-1,6-bisphosphatase [ Yersiniafrederiksenii ATCC 33641]167ZP_012. . .90411963fructose-1,6-bisphosphatase [ Photobacterium profundum3TCK]168ZP_005. . .67938188Inositol phosphatase/fructose-1,6-bisphosphatase [ Chlorobiumphaeobacteroides BS1]169NP_99195645440417fructose-1,6-bisphosphatase [ Yersinia pestis biovar Microtusstr. 91001]170NP_84060630248536fructose-1,6-bisphosphatase [ Nitrosomonas europaea ATCC19718]171YP_649191108813424fructose-1,6-bisphosphatase [ Yersinia pestis Nepal516]172ZP_010. . .86134593fructose-1,6-bisphosphatase [ Tenacibaculum sp. MED152]173ZP_012. . .94268582Inositol phosphatase/fructose-1,6-bisphosphatase [deltaproteobacterium MLMS-1]174ZP_012. . .94264279Inositol phosphatase/fructose-1,6-bisphosphatase [deltaproteobacterium MLMS-1]175ZP_005. . .67919158Inositol phosphatase/fructose-1,6-bisphosphatase [ Chlorobiumlimicola DSM 245]176NP_66126221673197fructose-1,6-bisphosphatase [ Chlorobium tepidum TLS]177YP_12861854307598fructose-1,6-bisphosphatase [ Photobacterium profundum SS9]178YP_37891878188580fructose-1,6-bisphosphatase [ Chlorobium chlorochromatiiCaD3]179ZP_005. . .68551142Inositol phosphatase/fructose-1,6-bisphosphatase [ Pelodictyonphaeoclathratiforme BU-1]180YP_44596883814754fructose-1,6-bisphosphatase [ Salinibacter ruber DSM 13855]181ZP_012. . .90580816fructose-1,6-bisphosphatase [ Vibrio angustum S14]182ZP_011. . .89075542fructose-1,6-bisphosphatase [ Photobacterium sp. SKA34]183YP_34209377163568fructose-1,6-bisphosphatase [ Nitrosococcus oceani ATCC19707]184ZP_009. . .84387793fructose-1,6-bisphosphatase [ Vibrio splendidus 12B01]185ZP_010. . .86141292fructose-1,6-bisphosphatase [ Flavobacterium sp. MED217]186ZP_005. . .67937321Inositol phosphatase/fructose-1,6-bisphosphatase [ Chlorobiumphaeobacteroides DSM 266]187ZP_012. . .91228829fructose-1,6-bisphosphatase [ Vibrio alginolyticus 12G01]188ZP_008. . .77961846COG0158: Fructose-1,6-bisphosphatase [ Yersinia mollaretiiATCC 43969]189ZP_008. . .77977605COG0158: Fructose-1,6-bisphosphatase [ Yersinia intermediaATCC 29909]190YP_20364759710871fructose-1,6-bisphosphatase [ Vibrio fischeri ES114]191ZP_013. . .110596824Inositol phosphatase/fructose-1,6-bisphosphatase [ Chlorobiumferrooxidans DSM 13031]192YP_45403685058334fructose-1,6-bisphosphatase [ Sodalis glossinidius str.‘morsitans’]193ZP_001. . .32035025COG0158: Fructose-1,6-bisphosphatase [ Actinobacilluspleuropneumoniae serovar 1 str. 4074]194YP_01105846580250fructose-1,6-bisphosphatase [ Desulfovibrio vulgaris subsp.vulgaris str. Hildenborough]195YP_21927662182859fructose-1,6-bisphosphatase [ Salmonella enterica subsp.enterica serovar Choleraesuis str. SC-B67]196YP_56007791784871Inositolphosphatase/fructose-1,6-bisphosphatase[ Burkholderia xenovorans LB400]197YP_31633574318595fructose-1,6-bisphosphatase [ Thiobacillus denitrificans ATCC25259]198YP_38856178357112fructose-1,6-bisphosphatase [ Desulfovibrio desulfuricansG20]199NP_31323615834463fructose-1,6-bisphosphatase [ Escherichia coli O157:H7 str.Sakai]200YP_31312874314709fructose-bisphosphatase [ Shigella sonnei Ss046]201ZP_011. . .88801533fructose-1,6-bisphosphatase [ Polaribacter irgensii 23-P] TABLE 53Examples of squalene epoxidase polypeptidesRowACCESSIONGIPROTEIN DESCRIPTION1XP_50399450553168hypothetical protein [ Yarrowia lipolytica ].2EAS3067090301039hypothetical protein CIMG_06149 [ Coccidioides immitis RS]3XP_75385870998268squalene monooxygenase Erg1 [ Aspergillus fumigatus Af293]4XP_71189468488538squalene epoxidase [ Candida albicans SC5314]5ABD4870688697124squalene epoxidase [ Emericella nidulans ]6XP_68102067901528hypothetical protein AN7751.2 [ Aspergillus nidulans FGSC A4]7AAQ1821533415411squalene epoxidase [ Trichophyton rubrum ]8BAE6235983772229unnamed protein product [ Aspergillus oryzae ]9AAQ1821661807216squalene epoxidase [ Trichophyton rubrum ]10AAZ0856370797544squalene epoxidase [ Trichophyton rubrum ]11CAJ1828190185988squalene epoxidase [ Hypocrea lixii ]12XP_46216050427105hypothetical protein DEHA0G15202g [ Debaryomyces hanseniiCBS767]13NP_0116916321614Squalene epoxidase, catalyzes the epoxidation of squalene to 2,3-oxidosqualene; plays an essential role in the ergosterol-biosynthesispathway and is the specific target of the antifungal drug terbinafine;Erg1p [ Saccharomyces cerevisiae ]14AAA34592171471squalene epoxidase15O1330651704232Squalene monooxygenase (Squalene epoxidase) (SE)16XP_45576350311477unnamed protein product [ Kluyveromyces lactis ]17XP_38639146123675hypothetical protein FG06215.1 [ Gibberella zeae PH-1]18EAQ8813988180671hypothetical protein CHGG_04758 [ Chaetomium globosum CBS148.51]19XP_96180685104779hypothetical protein [ Neurospora crassa OR74A]20XP_75854571012984hypothetical protein UM02398.1 [ Ustilago maydis 521]21XP_36932539975869hypothetical protein MG06139.4 [ Magnaporthe grisea 70-15]22XP_57009258265872squalene monooxygenase [ Cryptococcus neoformans var.neoformans JEC21]23Q9C1W351701448Probable squalene monooxygenase (Squalene epoxidase) (SE)24EAT79729111058609hypothetical protein SNOG_12929 [ Phaeosphaeria nodorum SN15]25CAG38355108743007squalene epoxidase [ Aspergillus niger ]26BAE7309484579321hypothetical protein [ Macaca fascicularis ]27EAU31524114189824hypothetical protein ATEG_08351 [ Aspergillus terreus NIH2624]28NP_00312062865635squalene monooxygenase [ Homo sapiens ]29CAI4607657997512hypothetical protein [ Homo sapiens ]30BAE3737474200967unnamed protein product [ Mus musculus ]31XP_85064073974448PREDICTED: similar to squalene monooxygenase isoform 1 [ Canisfamiliaris ]32Q75F6951701415Squalene monooxygenase (Squalene epoxidase) (SE)33AAS6023445388098squalene epoxidase 1 [ Aspergillus fumigatus ]34Q1453412644414Squalene monooxygenase (Squalene epoxidase) (SE)35XP_001. . .109087424PREDICTED: similar to squalene monooxygenase [ Macaca mulatta ]36AAH9733066911977Sqle protein [ Rattus norvegicus ]37EAU30782114189082hypothetical protein ATEG_08650 [ Aspergillus terreus NIH2624]38CAF9805747218525unnamed protein product [ Tetraodon nigroviridis ]39XP_86194473974450PREDICTED: similar to squalene monooxygenase isoform 2 [ Canisfamiliaris ]40ABF94794108706999Squalene monooxygenase, putative, expressed [ Oryza sativa( japonica cultivar-group)]41BAF11377113547934Os03g0231800 [ Oryza sativa ( japonica cultivar-group)]42XP_47061450920507Putative Squalene monooxygenase [ Oryza sativa ( japonica cultivar-group)]43ABF94791108706996Squalene monooxygenase, putative, expressed [ Oryza sativa( japonica cultivar-group)]44AAM6138421537043squalene epoxidase-like protein [ Arabidopsis thaliana ]45BAE98940110742002hypothetical protein [ Arabidopsis thaliana ]46ABE8480192877833Helix-turn-helix, AraC type; NAD-binding site; Fumarate lyase[ Medicago truncatula ]47BAE3659874183459unnamed protein product [ Mus musculus ]48XP_69369868403773PREDICTED: similar to squalene monooxygenase [ Danio rerio ]49CAB804417270759squalene epoxidase-like protein [ Arabidopsis thaliana ]50O486516685403Squalene monooxygenase (Squalene epoxidase) (SE)51AAY2220062945915squalene monooxygenase [ Datura innoxia ]52BAD1533046359651squalene epoxidase [ Panax ginseng ]53CAD2324827475610squalene monooxygenase 2 [ Medicago truncatula ]54ABC9494386371770squalene epoxidase [ Medicago sativa ]55CAD2324927475612squalene monooxygenase 1 [ Medicago truncatula ]56AAN1555823198062squalene monooxygenase, putative [ Arabidopsis thaliana ]57NP_17986815227757oxidoreductase [ Arabidopsis thaliana ]58AAG5064512321049squalene monooxygenase, putative [ Arabidopsis thaliana ]59XP_62902266800193hypothetical protein DDBDRAFT_0192021 [ Dictyosteliumdiscoideum AX4]60CAK1146694733753novel protein similar to vertebrate squalene epoxidase (SQLE)[ Danio rerio ]61AAQ1359533337947putative squalene epoxidase [ Lycopersicon esculentum ]62ABF94792108706997Squalene monooxygenase, putative, expressed [ Oryza sativa( japonica cultivar-group)]63XP_60490876660360PREDICTED: similar to squalene monooxygenase [ Bos taurus ]64BAA112091483186squalene epoxidase [ Homo sapiens ]65NP_19780315237902SQP1 [ Arabidopsis thaliana ]66NP_001. . .79328611SQP1 [ Arabidopsis thaliana ]67CAA067723123331squalene epoxidase homologue [ Arabidopsis thaliana ]68O657266685410Squalene monooxygenase 1,2 (Squalene epoxidase 1,2) (SE 1,2)69O657276685411Squalene monooxygenase 1,1 (Squalene epoxidase 1,1) (SE 1,1)70NP_19780415237903oxidoreductase [ Arabidopsis thaliana ]71CAJ0318268125205squalene monooxygenase-like protein [ Leishmania major ]72NP_19780215237900SQP2; oxidoreductase [ Arabidopsis thaliana ]73XP_82840971754989squalene monooxygenase [ Trypanosoma brucei TREU927]74XP_80834371412304squalene monooxygenase [ Trypanosoma cruzi strain CL Brener]75XP_78905972038634PREDICTED: similar to squalene monooxygenase[ Strongylocentrotus purpuratus ]76XP_79629772133073PREDICTED: similar to squalene monooxygenase[ Strongylocentrotus purpuratus ]77AAB691892352528squalene epoxidase [ Candida glabrata ]78XP_81343471649420squalene monooxygenase [ Trypanosoma cruzi strain CL Brener]79XP_79626172133071PREDICTED: similar to squalene monooxygenase[ Strongylocentrotus purpuratus ]80XP_79378372114550PREDICTED: similar to squalene monooxygenase, partial[ Strongylocentrotus purpuratus ]81XP_78902872038632PREDICTED: similar to squalene xygenase [ Strongylocentrotuspurpuratus ]82AAT9708751105054squalene epoxidase-like protein [ Lymnaea stagnalis ]83XP_80434371402993squalene monooxygenase [ Trypanosoma cruzi strain CL Brener]84YP_11526553803024monooxygenase family protein [ Methylococcus capsulatus str. Bath]85AAM9117722136198unknown protein [ Arabidopsis thaliana ]86XP_79913472026766PREDICTED: similar to Squalene monooxygenase (Squaleneepoxidase) (SE), partial [ Strongylocentrotus purpuratus ] TABLE 54Examples of ERG1 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAA34592171471squalene epoxidase2O1330651704232Squalene monooxygenase (Squalene epoxidase) (SE)3XP_45576350311477unnamed protein product [ Kluyveromyces lactis ]4Q75F6951701415Squalene monooxygenase (Squalene epoxidase) (SE)5XP_46216050427105hypothetical protein DEHA0G15202g [ Debaryomyces hansenii CBS767]6XP_71189468488538squalene epoxidase [ Candida albicans SC5314]7XP_50399450553168hypothetical protein [ Yarrowia lipolytica ]8AAB691892352528squalene epoxidase [ Candida glabrata ]9AAQ1821533415411squalene epoxidase [ Trichophyton rubrum ]10AAQ1821661807216squalene epoxidase [ Trichophyton rubrum ]11AAZ0856370797544squalene epoxidase [ Trichophyton rubrum ]12EAS3067090301039hypothetical protein CIMG_06149 [ Coccidioides immitis RS]13Q9C1W351701448Probable squalene monooxygenase (Squalene epoxidase) (SE)14XP_75854571012984hypothetical protein UM02398.1 [ Ustilago maydis 521]15XP_68102067901528hypothetical protein AN7751.2 [ Aspergillus nidulans FGSC A4]16ABD4870688697124squalene epoxidase [ Emericella nidulans ]17BAE6235983772229unnamed protein product [ Aspergillus oryzae ]18XP_75385870998268squalene monooxygenase Erg1 [ Aspergillus fumigatus Af293]19XP_96180685104779hypothetical protein [ Neurospora crassa OR74A]20XP_38639146123675hypothetical protein FG06215.1 [ Gibberella zeae PH-1]21CAJ1828190185988squalene epoxidase [ Hypocrea lixii ]22BAE7309484579321hypothetical protein [ Macaca fascicularis ]23BAE3737474200967unnamed protein product [ Mus musculus ]24XP_57009258265872squalene monooxygenase [ Cryptococcus neoformans var. neoformansJEC21]25NP_00312062865635squalene monooxygenase [ Homo sapiens ]26EAT79729111058609hypothetical protein SNOG_12929 [ Phaeosphaeria nodorum SN15]27AAH9733066911977Sqle protein [ Rattus norvegicus ]28CAI4607657997512hypothetical protein [ Homo sapiens ]29CAF9805747218525unnamed protein product [ Tetraodon nigroviridis ]30XP_85064073974448PREDICTED: similar to squalene monooxygenase isoform 1 [ Canisfamiliaris ]31XP_36932539975869hypothetical protein MG06139.4 [ Magnaporthe grisea 70-15]32Q1453412644414Squalene monooxygenase (Squalene epoxidase) (SE)33XP_001. . .109087424PREDICTED: similar to squalene monooxygenase [ Macaca mulatta ]34EAQ8813988180671hypothetical protein CHGG_04758 [ Chaetomium globosum CBS 148.51]35XP_69369868403773PREDICTED: similar to squalene monooxygenase [ Danio rerio ]36CAG38355108743007squalene epoxidase [ Aspergillus niger ]37XP_86194473974450PREDICTED: similar to squalene monooxygenase isoform 2 [ Canisfamiliaris ]38XP_51995055631226PREDICTED: similar to squalene epoxidase [ Pan troglodytes ]39AAS6023445388098squalene epoxidase 1 [ Aspergillus fumigatus ]40XP_62902266800193hypothetical protein DDBDRAFT_0192021 [ Dictyostelium discoideumAX4]41CAK1146694733753novel protein similar to vertebrate squalene epoxidase (SQLE) [ Daniorerio ]42BAE98940110742002hypothetical protein [ Arabidopsis thaliana ]43AAM6138421537043squalene epoxidase-like protein [ Arabidopsis thaliana ]44ABC9494386371770squalene epoxidase [ Medicago sativa ]45CAB804417270759squalene epoxidase-like protein [ Arabidopsis thaliana ]46CAD2324827475610squalene monooxygenase 2 [ Medicago truncatula ]47BAE3659874183459unnamed protein product [ Mus musculus ]48AAQ1359533337947putative squalene epoxidase [ Lycopersicon esculentum ]49AAY2220062945915squalene monooxygenase [ Datura innoxia ]50ABF94791108706996Squalene monooxygenase, putative, expressed [ Oryza sativa ( japonicacultivar-group)]51AAN1555823198062squalene monooxygenase, putative [ Arabidopsis thaliana ]52ABF94794108706999Squalene monooxygenase, putative, expressed [ Oryza sativa ( japonicacultivar-group)]53XP_47061450920507Putative Squalene monooxygenase [ Oryza sativa ( japonica cultivar-group)]54BAF11377113547934Os03g0231800 [ Oryza sativa ( japonica cultivar-group)]55CAD2324927475612squalene monooxygenase 1 [ Medicago truncatula ]56AAG5064512321049squalene monooxygenase, putative [ Arabidopsis thaliana ]57NP_17986815227757oxidoreductase [ Arabidopsis thaliana ]58ABE8480192877833Helix-turn-helix, AraC type; NAD-binding site; Fumarate lyase [ Medicagotruncatula ]59ABF94792108706997Squalene monooxygenase, putative, expressed [ Oryza sativa ( japonicacultivar-group)]60BAA112091483186squalene epoxidase [ Homo sapiens ]61XP_60490876660360PREDICTED: similar to squalene monooxygenase [ Bos taurus ]62XP_82840971754989squalene monooxygenase [ Trypanosoma brucei TREU927]63XP_80834371412304squalene monooxygenase [ Trypanosoma cruzi strain CL Brener]64CAJ0318268125205squalene monooxygenase-like protein [ Leishmania major ]65O657266685410Squalene monooxygenase 1,2 (Squalene epoxidase 1,2) (SE 1,2)66NP_19780415237903oxidoreductase [ Arabidopsis thaliana ]67O657276685411Squalene monooxygenase 1,1 (Squalene epoxidase 1,1) (SE 1,1)68CAA067723123331squalene epoxidase homologue [ Arabidopsis thaliana ]69NP_001. . .79328611SQP1 [ Arabidopsis thaliana ]70NP_19780315237902SQP1 [ Arabidopsis thaliana ]71NP_19780215237900SQP2; oxidoreductase [ Arabidopsis thaliana ] TABLE 55Examples of ERG7 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAT9306251013537YHR072W [ Saccharomyces cerevisiae ]2AAA16975465105lanosterol synthase3XP_44818250291499unnamed protein product [ Candida glabrata ]4XP_45198250304065unnamed protein product [ Kluyveromyces lactis ]5NP_98701745201447AGR351Wp [ Eremothecium gossypii ]6XP_45793750418833hypothetical protein DEHA0C06501g [ Debaryomyces hansenii CBS767]7XP_722471684671122,3-oxidosqualene-lanosterol cyclase [ Candida albicans SC5314]8XP_722612684668332,3-oxidosqualene-lanosterol cyclase [ Candida albicans SC5314]91903190A383419oxidosqualene cyclase10XP_50499050555163hypothetical protein [ Yarrowia lipolytica ]11AAB084721549343inactive oxidosqualene-lansoterol cyclase [ Saccharomyces cerevisiae ]12Q96WJ030913110Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-epoxysqualene--lanosterol cyclase) (OSC)13XP_74793670984860oxidosqualene:lanosterol cyclase [ Aspergillus fumigatus Af293]14BAE6162683771494unnamed protein product [ Aspergillus oryzae ]15NP_59370263054562lanosterol synthase activity [ Schizosaccharomyces pombe 972h-]16XP_75838771010409hypothetical protein UM02240.1 [ Ustilago maydis 521]17XP_68152967902546hypothetical protein AN8260.2 [ Aspergillus nidulans FGSC A4]18EAS3743890307807hypothetical protein CIMG_02792 [ Coccidioides immitis RS]19XP_96102685100788lanosterol synthase related protein [MIPS] [ Neurospora crassa OR74A]20XP_75162770993560oxidosqualene:lanosterol cyclase [ Aspergillus fumigatus Af293]21EAQ8643988178971hypothetical protein CHGG_07692 [ Chaetomium globosum CBS 148.51]22XP_38612646123145hypothetical protein FG05950.1 [ Gibberella zeae PH-1]23BAE6341583773288unnamed protein product [ Aspergillus oryzae ]24EAS3116790301536hypothetical protein CIMG_06646 [ Coccidioides immitis RS]25EAT81661111060541hypothetical protein SNOG_11162 [ Phaeosphaeria nodorum SN15]26XP_57045058266588lanosterol synthase [ Cryptococcus neoformans var. neoformans JEC21]27AAL5602018028346oxidosqualene:lanosterol cyclase [ Cephalosporium caerulens ]28BAC3710226346907unnamed protein product [ Mus musculus ]29Q8BLN562286881Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-epoxysqualene--lanosterol cyclase) (OSC)30XP_001. . .109065021PREDICTED: lanosterol synthase isoform 2 [ Macaca mulatta ]311W6KA56966682Chain A, Structure Of Human Osc In Complex With Lanosterol32BAC3173926336108unnamed protein product [ Mus musculus ]33XP_64624666825783hypothetical protein DDB_0191311 [ Dictyostelium discoideum AX4]34AAF803848886139cycloartenol synthase [ Dictyostelium discoideum ]35CAB428284808278lanosterol synthase [ Homo sapiens ]361W6JA56966681Chain A, Structure Of Human Osc In Complex With Ro 48-807137BAA082086398652,3-oxidosqualene:lanosterol cyclase [ Rattus norvegicus ]38NP_11231113591981lanosterol synthase [ Rattus norvegicus ]39NP_001. . .114053041lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) [ Bos taurus ]40P4845062296496Lanosterol synthase (Oxidosqualene--lanosterol cyclase) (2,3-epoxysqualene--lanosterol cyclase) (OSC)41NP_001. . .57529773lanosterol synthase (2,3-oxidosqualene-lanosterol cyclase) [ Gallus gallus ]42XP_75135670993016oxidosqualene cyclase [ Aspergillus fumigatus Af293]43CAG0828447222029unnamed protein product [ Tetraodon nigroviridis ]44BAB8308518147590cycloartenol synthase [ Betula platyphylla ]45BAA769024589852cycloartenol synthase [ Glycyrrhiza glabra ]46BAE6171983771588unnamed protein product [ Aspergillus oryzae ]47BAA334603688598Cycloartenol Synthase [ Panax ginseng ]48XP_001. . .109065023PREDICTED: lanosterol synthase isoform 1 [ Macaca mulatta ]49BAD3464450896401cycloartenol synthase [ Cucurbita pepo ]50BAA852666045133cycloartenol synthase [ Luffa aegyptiaca ]51BAB8325318147771cycloartenol synthase [ Costus speciosus ]52ABB7676782468805cycloartenol synthase [ Ricinus communis ]53BAA235332627181cycloartenol synthase [ Pisum sativum ]54BAD3464550896403cucurbitadienol synthase [ Cucurbita pepo ]55BAE5343183016479cycloartenol synthase [ Lotus japonicus ]56AAS8346946242746cycloartenol synthase [ Bupleurum kaoi ]57A49398541855cycloartenol synthase (EC 5.4.99.8) - Arabidopsis thaliana58AAN6450924796994At2g07050/T4E14.16 [ Arabidopsis thaliana ]59BAD3464650896405putative oxidosqualene cyclase [ Cucurbita pepo ]60AAC04931452446cycloartenol synthase; (S)-2,3-epoxysqualene mutase [ Arabidopsisthaliana ]61BAE95408108743265lanosterol synthase [ Arabidopsis thaliana ]62AAG4409612004573cycloartenol synthase [ Abies magnifica ]63AAS0152441387168cycloartenol synthase [ Centella asiatica ]64BAB8308618147592cycloartenol synthase [ Betula platyphylla ]65AAF033756090879putative cycloartenol synthase [ Oryza sativa ]66BAF07762113535379Os02g0139700 [ Oryza sativa ( japonica cultivar-group)]67BAE95410108743269lanosterol synthase [ Lotus japonicus ]68AAK8299515076959lanosterol synthase [ Trypanosoma cruzi ]69XP_82096771668047lanosterol synthase [ Trypanosoma cruzi strain CL Brener]70BAA852676045135oxidosqualene cyclase [ Luffa aegyptiaca ]71NP_19009942565553catalytic/lyase [ Arabidopsis thaliana ]72AAT3888947834383cycloartenol synthase [ Avena longiglumis ]73BAA869336456469oxidosqualene cyclase [ Taraxacum officinale ]74AAT3889147834387cycloartenol synthase [ Avena strigosa ]75CAC8455915866702cycloartenol synthase [ Avena strigosa ]76AAT3889047834385cycloartenol synthase [ Avena prostrata ]77AAT3888847834381cycloartenol synthase [ Avena longiglumis ]78AAT3888747834379cycloartenol synthase [ Avena clauda ]79AAT3889247834389cycloartenol synthase [ Avena ventricosa ]80XP_81975871665580lanosterol synthase [ Trypanosoma cruzi strain CL Brener]81BAA869306456434lupeol synthase [ Olea europaea ]82CAA61078984145lanosterol synthase [ Homo sapiens ]83BAA334623688602Oxidosqualene Cyclase [ Panax ginseng ]84AAG2632811023151lanosterol synthase [ Trypanosoma brucei brucei ]85XP_82567371752517lanosterol synthase [ Trypanosoma brucei TREU927]86BAA869326456467lupeol synthase [ Taraxacum officinale ]87CAD2324727475608beta-amyrin synthase [ Medicago truncatula ]88BAA975588918271beta-amyrin synthase [ Pisum sativum ]89BAA869316456465cycloartenol synthase [ Olea europaea ]90BAD0858741687978lupeol synthase [ Glycyrrhiza glabra ]91BAA846035922599oxidosqualene cyclase [ Allium macrostemon ]92AAO3357828194504beta-amyrin synthase [ Medicago truncatula ]93BAB8308718147594lupeol synthase [ Betula platyphylla ]94BAB8325418147773multifunctional triterpene synthase [ Costus speciosus ]95BAA898156730969beta-amyrin synthase [ Glycyrrhiza glabra ]96BAE5342983016474beta-amyrin synthase [ Lotus japonicus ]97AAO3357928194506putative beta-amyrin synthase [ Lotus japonicus ]98BAA334613688600beta-Amyrin Synthase [ Panax ginseng ]99CAB721516911851oxidosqualene cyclase-like protein [ Arabidopsis thaliana ]100CAJ0211068124127lanosterol synthase, putative [ Leishmania major ]101BAA337223721856beta-Amyrin Synthase [ Panax ginseng ]102AAX1471660203059beta-amyrin synthase [ Aster sedifolius ]103BAE5343083016477lupeol synthase [ Lotus japonicus ]104ABE9109092892072Prenyltransferase/squalene oxidase [ Medicago truncatula ]105XP_68151867902524hypothetical protein AN8249.2 [ Aspergillus nidulans FGSC A4]106AAC170803152599Strong similarity to lupeol synthase gb|U49919 and cycloartenol synthasegb|U02555 from A. thaliana (the third gene with similar homology).[ Arabidopsis thaliana ]107BAF28067113644926Os11g0286800 [ Oryza sativa ( japonica cultivar-group)]108NP_68350822330736beta-amyrin synthase [ Arabidopsis thaliana ]109AAS8346846242744beta-armyrin synthase [ Bupleurum kaoi ]110AAO3358028194508multifunctional beta-amyrin synthase [ Lotus japonicus ]111BAE4364273991374beta-amyrin synthase [ Euphorbia tirucalli ]112BAB8308818147596beta-amyrin synthase [ Betula platyphylla ]113ABB7676682468803lupeol synthase [ Ricinus communis ]114ABG22399108864084Cycloartenol synthase, putative, expressed [ Oryza sativa ( japonica cultivar-group)]115BAF28063113644922Os11g0285000 [ Oryza sativa ( japonica cultivar-group)]116ABG22398108864083Cycloartenol synthase, putative, expressed [ Oryza sativa ( japonica cultivar-group)]117NP_84990330699380LUP1 (LUPEOL SYNTHASE 1); lupeol synthase [ Arabidopsis thaliana ]118AAB9434127380272,3-oxidosqualene-triterpenoid cyclase [ Arabidopsis thaliana ]119AAN77001259919992,3-oxidosqualene-triterpene cyclase [ Arabidopsis thaliana ]120AAT3889347834391beta-amyrin synthase [ Avena clauda ]121AAD050321762150lupeol synthase [ Arabidopsis thaliana ]122NP_17801730699377ATLUP2; lupeol synthase [ Arabidopsis thaliana ]123ABE8859992887080squalene/oxidosqualene cyclases [ Medicago truncatula ]124ABG22449108864253Cycloartenol synthase, putative, expressed [ Oryza sativa ( japonica cultivar-group)]125BAB6852915787841isomultiflorenol synthase [ Luffa aegyptiaca ]126AAT3889847834401beta-amyrin synthase [ Avena ventricosa ]127AAT3889447834393beta-amyrin synthase [ Avena longiglumis ]128AAT3889747834399beta-amyrin synthase [ Avena strigosa ]129NP_17801622330734catalytic/lyase [ Arabidopsis thaliana ]130AAT3889547834395beta-amyrin synthase [ Avena longiglumis ]131AAT3889647834397beta-amyrin synthase [ Avena prostrata ]132BAA975598918273mixed-amyrin synthase [ Pisum sativum ]133AAC988644090722pentacyclic triterpene synthase [ Arabidopsis thaliana ]134BAF28466113645325Os11g0562100 [ Oryza sativa ( japonica cultivar-group)]135AAG4176211934652pentacyclic triterpene synthase [synthetic construct]136XP_48075950942463putative Cycloartenol Synthase [ Oryza sativa ( japonica cultivar-group)]137BAE4364373991380putative oxidosqulene cyclase [ Euphorbia tirucalli ]138AAC170703152589Strong similarity to lupeol synthase gb|U49919 from A. thaliana (secondgene in a series of three with similar homologies). [ Arabidopsis thaliana ]139BAD1533246359655beta-amyrin synthase [ Panax ginseng ]140AAM2326423428800beta-amyrin synthase [ Glycine max ]141ABC3392283638481beta-amyrin synthase [ Gypsophila paniculata ]142AAS0152341387158putative beta-amyrin synthase [ Centella asiatica ]143BAE99758110743847cycloartenol synthase [ Arabidopsis thaliana ]144BAB1106510177752cycloartenol synthase [ Arabidopsis thaliana ]145NP_17797115218390catalytic [ Arabidopsis thaliana ]146CAD3919632526539cycloartenol synthase [ Stigmatella aurantiaca ]147ABG22450108864254Cycloartenol synthase, putative, expressed [ Oryza sativa ( japonica cultivar-group)]148CAA935711204221erg7 [ Schizosaccharomyces pombe ]149NP_56746218414430ATPEN1; catalytic/lyase [ Arabidopsis thaliana ]150NP_19961242568386catalytic [ Arabidopsis thaliana ]151NP_19327215233798catalytic/lyase [ Arabidopsis thaliana ]152ABE8861092887091squalene/oxidosqualene cyclases [ Medicago truncatula ]153AAW3003456790234At5g42600 [ Arabidopsis thaliana ]154BAF01935110740066putative lupeol synthase [ Arabidopsis thaliana ]155NP_19846415239312ATPEN3; catalytic [ Arabidopsis thaliana ]156BAB8308918147598putative oxidosqualene cyclase [ Betula platyphylla ]157YP_11526653803023squalene cyclase family protein [ Methylococcus capsulatus str. Bath]158CAB785797268284lupeol synthase like protein [ Arabidopsis thaliana ]159CAB785767268281lupeol synthase like protein [ Arabidopsis thaliana ] TABLE 56Examples of ERG6 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1CAA89944854482Erg6p [ Saccharomyces cerevisiae ]2P25087462024Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)3CAA52308396515S-adenosyl-methionine:delta-24-sterol-C-methyltransferase[ Saccharomyces cerevisiae ]4AAB31378619251putative S-adenosylmethionine-dependent methyltransferase[ Saccharomyces cerevisiae ]5Q6FRZ762900214Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)6AAX7320062178560C24 sterol methyltransferase [ Candida glabrata ]7P_44699750289135unnamed protein product [ Candida glabrata ]8CAG5993049526306unnamed protein product [ Candida glabrata CBS138]9AAX7319962178558C24 sterol methyltransferase [ Candida glabrata ]10Q6CYB362900210Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)11P_45107650302283unnamed protein product [ Kluyveromyces lactis ]12CAH0266449640207unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]13Q759S762900245Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)14P_98429245188069ADR196Wp [ Eremothecium gossypii ]15AAS5211644982886ADR196Wp [ Ashbya gossypii ATCC 10895]16CAA378264122unnamed protein product [ Saccharomyces cerevisiae ]17Q875K162900279Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)18AAO2193627803704S-adenosylmethionine:D24-methyltransferase [ Clavisporalusitaniae ]19Q6BRB762900203Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)20P_45925350421405hypothetical protein DEHA0D19151g [ Debaryomyces hanseniiCBS767]21CAG8742749654920unnamed protein product [ Debaryomyces hansenii CBS767]22P_72158868468538SAM:delta 24-methyltransferase [ Candida albicans SC5314]23P_72170868468297SAM:delta 24-methyltransferase [ Candida albicans SC5314]24EAL0292046443640hypothetical protein CaO19.1631 [ Candida albicans SC5314]25EAL0279246443511hypothetical protein CaO19.9199 [ Candida albicans SC5314]26O741986015114Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)27AAC266263323500sterol transmethylase [ Candida albicans ]28Q6C2D962900205Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)29P_50517350555530hypothetical protein [ Yarrowia lipolytica ]30CAG7798049651043unnamed protein product [ Yarrowia lipolytica CLIB122]31P_59578719112579hypothetical protein SPBC16E9.05 [ Schizosaccharomyces pombe972h-]32O143216166151Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)33CAB168972467267SPBC16E9.05 [ Schizosaccharomyces pombe ]34EAT84719111063599hypothetical protein SNOG_08443 [ Phaeosphaeria nodorum SN15]35EAS2969890300067hypothetical protein CIMG_08444 [ Coccidioides immitis RS]36EAQ7070986196071hypothetical protein MGG_ch7g116 [ Magnaporthe grisea 70-15]37P_36635039969919hypothetical protein MG10568.4 [ Magnaporthe grisea 70-15]38P_74655070982043sterol 24-c-methyltransferase [ Aspergillus fumigatus Af293]39EAL8451266844173sterol 24-c-methyltransferase, putative [ Aspergillus fumigatusAf293]40BAE6480983774686unnamed protein product [ Aspergillus oryzae ]41P_96539285118140probable DELTA(24)-STEROL C-METHYLTRANSFERASE[MIPS] [ Neurospora crassa OR74A]42Q9P3R162900336Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)43EAA3615628927200probable DELTA(24)-STEROL C-METHYLTRANSFERASE[MIPS] [ Neurospora crassa ]44CAB972899367272probable DELTA(24)-STEROL C-METHYLTRANSFERASE(ERG6) [ Neurospora crassa ]45P_66475067541965hypothetical protein AN7146.2 [ Aspergillus nidulans FGSC A4]46EAA6139840742208hypothetical protein AN7146.2 [ Aspergillus nidulans FGSC A4]47P_38295946111803hypothetical protein FG02783.1 [ Gibberella zeae PH-1]48EAA7077842547935hypothetical protein FG02783.1 [ Gibberella zeae PH-1]49Q96WX462900323Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)50AAK5443914192727S-adenosyl methionine:sterol methyl transferase [ Pneumocystiscarinii ]51EAQ8952288182054conserved hypothetical protein [ Chaetomium globosum CBS148.51]52BAA1379341688402unnamed protein product [ Schizosaccharomyces pombe ]53P_38591646122725hypothetical protein FG05740.1 [ Gibberella zeae PH-1]54EAA7581542552972hypothetical protein FG05740.1 [ Gibberella zeae PH-1]55P_36187239944670hypothetical protein MG04346.4 [ Magnaporthe grisea 70-15]56Q5EN2262900141Sterol 24-C-methyltransferase (Delta(24)-sterol C-methyltransferase)57AAX0763159802827sterol 24-C-methyltransferase-like protein [ Magnaporthe grisea ]58BAE6103383770900unnamed protein product [ Aspergillus oryzae ]59P_75932971018197hypothetical protein UM03182.1 [ Ustilago maydis 521]60EAK8441246099179hypothetical protein UM03182.1 [ Ustilago maydis 521]61AAK0029412642580sterol methyl transferase [ Pneumocystis carinii f. sp. carinii ]62P_36054839942022hypothetical protein MG10860.4 [ Magnaporthe grisea 70-15]63P_56888758262954sterol 24-C-methyltransferase [ Cryptococcus neoformans var.neoformans JEC21]64AAW4158057223537sterol 24-C-methyltransferase, putative [ Cryptococcus neoformansvar. neoformans JEC21]65EAL2262850259962hypothetical protein CNBB2600 [ Cryptococcus neoformans var.neoformans B-3501A]66AAC349513560474S-adenosyl-methionine-sterol-C-methyltransferase [ Nicotianatabacum ]67AAC042652909846(S)-adenosyl-L-methionine:delta 24-sterol methyltransferase [ Zeamays ]68AAB493381872473delta-24-sterol methyltransferase [ Triticum aestivum ]69Q9LM0262901053Cycloartenol-C-24-methyltransferase (24-sterol C-methyltransferase1) (Sterol C-methyltransferase 1) (Protein STEROLMETHYLTRANSFERASE 1) (Protein CEPHALOPOD)70AAN153772319770024-sterol C-methyltransferase [ Arabidopsis thaliana ]71AAM532742153944324-sterol C-methyltransferase [ Arabidopsis thaliana ]72P_19687515240691SMT1 (STEROL METHYLTRANSFERASE 1) [ Arabidopsisthaliana ]73AAG2846211066105sterol methyltransferase SMT1 [ Arabidopsis thaliana ]74BAB08698975803724-sterol C-methyltransferase [ Arabidopsis thaliana ]75AAF788478745241SAM:cycloartenol-C24-methyltransferase [ Arabidopsis thaliana ]76AAM5355321434843cephalopod [ Arabidopsis thaliana ]77AAB708861899060endosperm C-24 sterol methyltransferase [ Zea mays ]78AAB377691706965delta-24-sterol methyltransferase [ Triticum aestivum ]79BAF21068113610690Os07g0206700 [ Oryza sativa ( japonica cultivar-group)]80Q6ZIX268566037Cycloartenol-C-24-methyltransferase 1 (24-sterol C-methyltransferase 1) (Sterol C-methyltransferase 1)81P_47707850935101cycloartenol-C24-methyltransferase [ Oryza sativa ( japonicacultivar-group)]82BAC8323834393309cycloartenol-C24-methyltransferase [ Oryza sativa ( japonicacultivar-group)]83AAB040571399380S-adenosyl-L-methionine:delta24-sterol-C-methyltransferase84AAB628122246458S-adenosyl-methionine-sterol-C-methyltransferase [ Ricinuscommunis ]85AAC357873603295S-adenosyl-methionine cycloartenol-C24-methyltransferase[ Nicotiana tabacum ]86AAC349883560531cycloartenol-C24-methyltransferase [ Oryza sativa subsp. japonica ]87AAZ833457376169124-sterol C-methyltransferase [ Gossypium hirsutum ]88EAS3066090301029hypothetical protein CIMG_06139 [ Coccidioides immitis RS]89P_47003550919277putative endosperm C-24 sterol methyltransferase [ Oryza sativa( japonica cultivar-group)]90AAP2141930103006putative endosperm C-24 sterol methyltransferase [ Oryza sativa( japonica cultivar-group)]91AAR9209940806291S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase B[ Leishmania donovani ]92AAR9209840806289S-adenosyl-L-methionine-C-24-delta-sterol-methyltransferase A[ Leishmania donovani ]93CAJ0919768129891sterol 24-c-methyltransferase, putative [ Leishmania major ]94CAJ0919668129890sterol 24-c-methyltransferase, putative [ Leishmania major ]95P_80286471399753sterol 24-c-methyltransferase [ Trypanosoma cruzi strain CL Brener]96EAN8141870865128sterol 24-c-methyltransferase, putative [ Trypanosoma cruzi ]97P_80271671399140sterol 24-c-methyltransferase [ Trypanosoma cruzi strain CL Brener]98EAN8127070864663sterol 24-c-methyltransferase, putative [ Trypanosoma cruzi ]99P_82293071747750sterol 24-c-methyltransferase [ Trypanosoma brucei TREU927]100AAZ4021471738257sterol methyltransferase [ Trypanosoma brucei brucei ]101CAJ1695870908212s-adenosyl-L-methionine-c-24-delta-sterol-methyltransferase a,putative [ Trypanosoma brucei ]102EAN7810270832598sterol 24-c-methyltransferase, putative [ Trypanosoma brucei ]103P_63648166805519hypothetical protein DDBDRAFT_0188166 [ Dictyosteliumdiscoideum AX4]104EAL6297760464861hypothetical protein DDBDRAFT_0188166 [ Dictyosteliumdiscoideum AX4]105ABF99454108711659Cyclopropane-fatty-acyl-phospholipid synthase family protein,expressed [ Oryza sativa ( japonica cultivar-group)]106P_80281171399535sterol 24-c-methyltransferase [ Trypanosoma cruzi strain CL Brener]107EAN8136570864963sterol 24-c-methyltransferase, putative [ Trypanosoma cruzi ]108ABB9054182780739c24-sterol methyltransferase [ Paracoccidioides brasiliensis ]109AAB628072246452S-adenosyl-methionine-sterol-C-methyltransferase homolog[ Nicotiana tabacum ]110Q392276290089324-methylenesterol C-methyltransferase 2 (24-sterol C-methyltransferase 2) (Sterol-C-methyltransferase 2)111AAM4500921281107putative sterol-C-methyltransferase [ Arabidopsis thaliana ]112P_17345815217917SMT2 (STEROL METHYLTRANSFERASE 2) [ Arabidopsisthaliana ]113AAK7671615028255putative sterol-C-methyltransferase [ Arabidopsis thaliana ]114AAG4878012083242putative sterol-C-methyltransferase [ Arabidopsis thaliana ]115AAF881569558593Identical to 24-sterol C-methyltransferase from Arabidopsis thalianagi|2129517 and is a member of the ubiE/COQ5 methyltransferasefamily PF|01209. ESTs gb|T42228, gb|T46520, gb|T41746,gb|N38458, gb|AI993515, gb|AA389843, gb|AI099890,gb|AI099653 come f1162207220A1587694sterol C-methyltransferase117CAA619661061040sterol-C-methyltransferase [ Arabidopsis thaliana ]118AAN721042508368224-sterol C-methyltransferase [ Arabidopsis thaliana ]119AAM915922213602024-sterol C-methyltransferase [ Arabidopsis thaliana ]120Q94JS46747270624-methylenesterol C-methyltransferase 3 (24-sterol C-methyltransferase 3) (Sterol-C-methyltransferase 3)121AAM4733921360447At1g76090/T23E18_40 [ Arabidopsis thaliana ]122P_17773615222955SMT3; S-adenosylmethionine-dependent methyltransferase[ Arabidopsis thaliana ]123AAK5298114030613At1g76090/T23E18_40 [ Arabidopsis thaliana ]124AAN3189023397216putative sterol-C-methyltransferase [ Arabidopsis thaliana ]125AAB628092246456S-adenosyl-methionine-sterol-C-methyltransferase [ Arabidopsisthaliana ]126AAB628082246454S-adenosyl-methionine-sterol-C-methyltransferase [ Nicotianatabacum ]127AAM6375321555010sterol-C-methyltransferase [ Arabidopsis thaliana ]128BAF10805113547362Os03g0136200 [ Oryza sativa ( japonica cultivar-group)]129ABF9385410870605924-methylenesterol C-methyltransferase 2, putative, expressed[ Oryza sativa ( japonica cultivar-group)]130O824276856601324-methylenesterol C-methyltransferase 2 (24-sterol C-methyltransferase 2) (Sterol-C-methyltransferase 2) TABLE 57Examples of ERG5 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1P547811706693Cytochrome P450 61 (C-22 sterol desaturase)2AAB062171235991cytochrome P4503CAA89116798924unknown [ Saccharomyces cerevisiae ]4AAU0976951830482YMR015C [ Saccharomyces cerevisiae ]5AAX7319862178556C22 sterol desaturase [ Candida glabrata ]6AAX7319762178554C22 sterol desaturase [ Candida glabrata ]7P_44968150294540hypothetical protein CAGL0M07656g [ Candida glabrata CBS138]8CAG6265749528995unnamed protein product [ Candida glabrata CBS138]9P_45356250307167unnamed protein product [ Kluyveromyces lactis ]10CAH0065849642696unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]11P_98299945185282ABR053Cp [ Eremothecium gossypii ]12AAS5082344980940ABR053Cp [ Ashbya gossypii ATCC 10895]13P_45872750420383hypothetical protein DEHA0D06842g [ Debaryomyces hanseniiCBS767]14CAG8687149654394unnamed protein product [ Debaryomyces hansenii CBS767]15P_88889377022898hypothetical protein CaJ7.0323 [ Candida albicans SC5314]16BAE4479076573706hypothetical protein [ Candida albicans ]17P_71693368478128cytochrome P450 [ Candida albicans SC5314]18P_71700068477993hypothetical protein CaO19.5178 [ Candida albicans SC5314]19EAK9802046438693hypothetical protein CaO19.5178 [ Candida albicans SC5314]20EAK9795046438622hypothetical protein CaO19.12645 [ Candida albicans SC5314]21CAA219533850153cytochrome P450 [ Candida albicans ]22P_50018850545301hypothetical protein [ Yarrowia lipolytica ]23CAG8412049646053unnamed protein product [ Yarrowia lipolytica CLIB122]24BAC0114221624361sterol C-22 desaturase [ Symbiotaphrina buchneri ]25BAC0114021624354sterol C-22 desaturase [ Symbiotaphrina buchneri ]26BAC0114121624359sterol C-22 desaturase [ Symbiotaphrina kochii ]27BAC0113921624352sterol C22 desaturase [ Symbiotaphrina kochii ]28EAQ8820688180738conserved hypothetical protein [ Chaetomium globosum CBS148.51]29P_96191585105220hypothetical protein [ Neurospora crassa OR74A]30EAA3267928923500hypothetical protein [ Neurospora crassa ]31EAS3398590304354hypothetical protein CIMG_05009 [ Coccidioides immitis RS]32P_75014570990592cytochrome P450 sterol C-22 desaturase [ Aspergillus fumigatusAf293]33EAL8810766847777cytochrome P450 sterol C-22 desaturase, putative [ Aspergillusfumigatus Af293]34EAT87119111065999hypothetical protein SNOG_06055 [ Phaeosphaeria nodorum SN15]35BAE5806883767929unnamed protein product [ Aspergillus oryzae ]36P_38213546110154hypothetical protein FG01959.1 [ Gibberella zeae PH-1]37EAA6885542546012hypothetical protein FG01959.1 [ Gibberella zeae PH-1]38P_66164667527317hypothetical protein AN4042.2 [ Aspergillus nidulans FGSC A4]39EAA5951340740323hypothetical protein AN4042.2 [ Aspergillus nidulans FGSC A4]40P_38386246115688hypothetical protein FG03686.1 [ Gibberella zeae PH-1]41EAA7149942548656hypothetical protein FG03686.1 [ Gibberella zeae PH-1]42P_36941739976053hypothetical protein MG06047.4 [ Magnaporthe grisea 70-15]43BAE5746183767322unnamed protein product [ Aspergillus oryzae ]44P_59378819114700hypothetical protein SPAC19A8.04 [ Schizosaccharomyces pombe972h-]45CAB116407007345SPAC19A8.04 [ Schizosaccharomyces pombe ]46P_75649771003662hypothetical protein UM00350.1 [ Ustilago maydis 521]47EAK8116846095935hypothetical protein UM00350.1 [ Ustilago maydis 521]48P_57144558268578C-22 sterol desaturase [ Cryptococcus neoformans var. neoformansJEC21]49AAW4413857227680C-22 sterol desaturase, putative [ Cryptococcus neoformans var.neoformans JEC21]50EAL2029850257593hypothetical protein CNBF1100 [ Cryptococcus neoformans var.neoformans B-3501A]51EAQ8614088178672hypothetical protein CHGG_07393 [ Chaetomium globosum CBS148.51]52AAO4860128864257ERG5 [ Clavispora lusitaniae ]53P_64701866827327cytochrome P450 family protein [ Dictyostelium discoideum AX4]54EAL7309760475161cytochrome P450 family protein [ Dictyostelium discoideum AX4]55BAF04287113531904Os01g0211200 [ Oryza sativa ( japonica cultivar-group)]56P_91328734903880unnamed protein product [ Oryza sativa ( japonica cultivar-group)]57BAA961968096624putative sterol C-22 desaturase [ Oryza sativa ( japonica cultivar-group)]58BAA961548096581putative sterol C-22 desaturase [ Oryza sativa ( japonica cultivar-group)]59ABC5909784514177cytochrome P450 monooxygenase CYP710A15 [ Medicagotruncatula ]60P_18045215226976CYP710A4; heme binding/iron ion binding/monooxygenase/oxygen binding [ Arabidopsis thaliana ]61AAC795903927833putative cytochrome P450 [ Arabidopsis thaliana ]62P_91328534903876unnamed protein product [ Oryza sativa ( japonica cultivar-group)]63BAA961948096622sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]64BAA961528096579sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]65P_91329134903888unnamed protein product [ Oryza sativa ( japonica cultivar-group)]66BAA962008096628sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]67BAA961588096585sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]68BAF04286113531903Os01g0210900 [ Oryza sativa ( japonica cultivar-group)]69P_91328434903874unnamed protein product [ Oryza sativa ( japonica cultivar-group)]70BAA961938096621sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]71BAA961518096578sterol C-22 desaturase-like [ Oryza sativa ( japonica cultivar-group)]72BAE7135184468537CYP710 [ Arabidopsis thaliana ]73AAQ6517734365731At2g34500 [ Arabidopsis thaliana ]74AAN7208025083451putative cytochrome P450 [ Arabidopsis thaliana ]75AAM1494420197156putative cytochrome P450 [ Arabidopsis thaliana ]76P_18099715226758CYP710A1; heme binding/iron ion binding/monooxygenase/oxygen binding [ Arabidopsis thaliana ]77AAC266903128210putative cytochrome P450 [ Arabidopsis thaliana ]78P_18045115226974CYP710A3; heme binding/iron ion binding/monooxygenase/oxygen binding [ Arabidopsis thaliana ]79AAC795893927832putative cytochrome P450 [ Arabidopsis thaliana ]80BAE8031689111285CYP710 protein [ Arabidopsis thaliana ]81AAM2666420856398At2g34490/T31E10.17 [ Arabidopsis thaliana ]82AAM1494520197157putative cytochrome P450 [ Arabidopsis thaliana ]83AAL7588818650637At2g34490/T31E10.17 [ Arabidopsis thaliana ]84P_18099615226756CYP710A2; heme binding/iron ion binding/monooxygenase/oxygen binding [ Arabidopsis thaliana ]85AAC266913128211putative cytochrome P450 [ Arabidopsis thaliana ]86AAM6279921553706putative cytochrome P450 [ Arabidopsis thaliana ]87BAE9315691204699sterol 22-desaturase [ Lycopersicon esculentum ] TABLE 58Examples of ERG3 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAT9301551013443YLR056W [ Saccharomyces cerevisiae ]2NP_0131576323085C-5 sterol desaturase, catalyzes the introduction of a C-5(6)3BAA202922143190C-5 sterol desaturase [ Saccharomyces cerevisiae ]4CAA643031181277C-5 sterol desaturase [ Saccharomyces cerevisiae ]5P32353416963C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta6AAB39844233331C-5 sterol desaturase [ Saccharomyces cerevisiae ]7AAA34595171477C-5 sterol desaturase8AAA34594171475C-5 sterol desaturase9XP_44605050287241unnamed protein product [ Candida glabrata ]10CAG5897449525357unnamed protein product [ Candida glabrata CBS138]11P508601706691C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta12AAB02330755695ERG313Q754B951701406C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta14NP_98569845198669AFR151Cp [ Eremothecium gossypii ]15AAS5352244984679AFR151Cp [ Ashbya gossypii ATCC 10895A]16XP_45548250310919unnamed protein product [ Kluyveromyces lactis ]17CAG9819049644618unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]18Q8NJ5751701432C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta19CAD1313122022945ergosterol delta 5,6 desaturase [ Candida dubliniensis ]20XP_71357768485022hypothetical protein CaO19.767 [ Candida albicans SC5314]21XP_71361268484947hypothetical protein CaO19.8387 [ Candida albicans SC5314]22EAK9450746435118hypothetical protein CaO19.8387 [ Candida albicans SC5314]23EAK9447246435082hypothetical protein CaO19.767 [ Candida albicans SC5314]24O9387551701379C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta25AAC993434091929C5,6 desaturase [ Candida albicans ]26XP_46074750424321hypothetical protein DEHA0F09757g [ Debaryomyces hanseniiCBS7627CAG8908849656416unnamed protein product [ Debaryomyces hansenii CBS767]28XP_50309050551233hypothetical protein [ Yarrowia lipolytica ]29CAG8128249648958unnamed protein product [ Yarrowia lipolytica CLIB122]30XP_66411067540672hypothetical protein AN6506.2 [ Aspergillus nidulans FGSC A4]31EAA5784640738656hypothetical protein AN6506.2 [ Aspergillus nidulans FGSC A4]32BAE6178483771654unnamed protein product [ Aspergillus oryzae ]33XP_74756370984086sterol delta 5,6-desaturase ERG3 [ Aspergillus fumigatus Af293]34EAL8552566845190sterol delta 5,6-desaturase ERG3 [ Aspergillus fumigatus Af293]35AAU8209852548218C-5 sterol desaturase B-like [ Aspergillus fumigatus ]36BAE5607683765933unnamed protein product [ Aspergillus oryzae ]37XP_96292385109451hypothetical protein [ Neurospora crassa OR74A]38Q7SBB651701418Probable C-5 sterol desaturase (Sterol-C5-desaturase) (Ergoste39EAA3368728924567hypothetical protein [ Neurospora crassa ]40EAS3725690307625C-5 sterol desaturase [ Coccidioides immitis RS]41Q8J20751701428C-5 sterol desaturase (Sterol-C5-desaturase) (Ergosterol delta42AAN2799823476431sterol delta 5,6-desaturase ERG3 [ Leptosphaeria maculans ]43XP_36398739953467hypothetical protein MG08832.4 [ Magnaporthe grisea 70-15]44EAT83541111062421hypothetical protein SNOG_09349 [ Phaeosphaeria nodorum SN15]45O9445751701380Probable C-5 sterol desaturase 1 (Sterol-C5-desaturase 1) (Erg46NP_59313519114047hypothetical protein SPAC1687.16c [ Schizosaccharomyces pombe 947CAA226104106670SPAC1687.16c [ Schizosaccharomyces pombe ]48XP_38267846111241hypothetical protein FG02502.1 [ Gibberella zeae PH-1]49EAA6723642544393hypothetical protein FG02502.1 [ Gibberella zeae PH-1]50BAE6560783775487unnamed protein product [ Aspergillus oryzae ]51O136666015113Probable C-5 sterol desaturase 2 (Sterol-C5-desaturase 2) (Erg52CAA168982853109SPBC27B12.03c [ Schizosaccharomyces pombe ]53BAA214572257565C-5 STEROL DESATURASE [ Schizosaccharomyces pombe ] TABLE 59Examples of ERG2 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAS5644845270134YMR202W [ Saccharomyces cerevisiae ]2CAA88643736299Erg2p [ Saccharomyces cerevisiae ]3P32352416962C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)4AAA34593171473C-8 sterol isomerase5P_98536945198340AFL181Cp [ Eremothecium gossypii ]6AAS5319344984227AFL181Cp [ Ashbya gossypii ATCC 10895]7P_44923350293643unnamed protein product [ Candida glabrata ]8CAG6220749528546unnamed protein product [ Candida glabrata CBS138]9P_45536750310691unnamed protein product [ Kluyveromyces lactis ]10CAG9807549644503unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]11P_45889150420709hypothetical protein DEHA0D10714g [ Debaryomyces hanseniiCBS767]12CAG8704349654558unnamed protein product [ Debaryomyces hansenii CBS767]13P_71888668473979sterol C8-C7 isomerase [ Candida albicans SC5314 ]14P_71898868473770sterol C8-C7 isomerase [ Candida albicans SC5314]15EAL0008746440785hypothetical protein CaO19.6026 [ Candida albicans SC5314]16EAK9998246440679hypothetical protein CaO19.13447 [ Candida albicans SC5314]17P_50466850554519hypothetical protein [ Yarrowia lipolytica ]18CAG8027249650537unnamed protein product [ Yarrowia lipolytica CLIB122]19P_50100650547073hypothetical protein [ Yarrowia lipolytica ]20CAG8325949646872unnamed protein product [ Yarrowia lipolytica CLIB122]21Q9225467476925C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)22CAC2874912718205C-8 sterol isomerase erg-1 [ Neurospora crassa ]23AAB094701575320C-8 sterol isomerase24P_65805567516339hypothetical protein AN0451.2 [ Aspergillus nidulans FGSC A4]25EAA6655040747394hypothetical protein AN0451.2 [ Aspergillus nidulans FGSC A4]26P_59332419114236hypothetical protein SPAC20G8.07c [ Schizosaccharomyces pombe972h-]27P871133219796Probable C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)28CAB086012094862SPAC20G8.07c [ Schizosaccharomyces pombe ]29P_36304039947737hypothetical protein MG08624.4 [ Magnaporthe grisea 70-15]30P33281462023C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)31CAA80454311322C-8 sterol isomerase [ Magnaporthe grisea ]32EAQ8588888178420hypothetical protein CHGG_07141 [ Chaetomium globosum CBS148.51]33P_96131285102300C-8 STEROL ISOMERASE (DELTA-8--DELTA-7 STEROLISOMERASE) [ Neurospora crassa OR74A]34EAA3207628922855C-8 STEROL ISOMERASE (DELTA-8--DELTA-7 STEROLISOMERASE) [ Neurospora crassa ]35P_84405772387265C-8 sterol isomerase, putative [ Trypanosoma brucei ]36P_82654071905267C-8 sterol isomerase, putative [ Trypanosoma brucei ]37AAZ1049870800589C-8 sterol isomerase, putative [ Trypanosoma brucei ]38AAX8063462360216C-8 sterol isomerase, putative [ Trypanosoma brucei ]39P_75808171006989C-8 sterol isomerase [ Ustilago maydis 521]40EAK8238846097155ERG2_USTMA C-8 sterol isomerase (Delta-8--delta-7 sterolisomerase) [ Ustilago maydis 521]41P32360416961C-8 sterol isomerase (Delta-8--delta-7 sterol isomerase)42CAA789592967C-8 sterol isomerase [ Ustilago maydis ]43P_56707058259315C-8 sterol isomerase [ Cryptococcus neoformans var. neoformansJEC21]44AAW4125157223207C-8 sterol isomerase, putative [ Cryptococcus neoformans var.neoformans JEC21]45EAL2304550260386hypothetical protein CNBA8120 [ Cryptococcus neoformans var.neoformans B-3501A]46P_82118671658920C-8 sterol isomerase [ Trypanosoma cruzi strain CL Brener]47EAN9933570886558C-8 sterol isomerase, putative [ Trypanosoma cruzi ]48AAQ1879633439494C-8 sterol isomerase [ Trypanosoma cruzi ]49P_84787973536920C-8 sterol isomerase-like protein [ Leishmania major strain Friedlin]50AAZ0967170799755C-8 sterol isomerase-like protein [ Leishmania major strain Friedlin] TABLE 60Examples of ERG3-like polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1BAA337303721884sterol-C5-desaturase [ Mus musculus ]2BAE3250674178504unnamed protein product [ Mus musculus ]3AAH2413218848246Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog ( S. cerevisae )[ Mus musculus ]4NP_76635727777693sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog[ Mus musculus ]5BAC3694426346591unnamed protein product [ Mus musculus ]6BAC3166626335931unnamed protein product [ Mus musculus ]7AAH8170451859106Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog ( S. cerevisae )[ Rattus norvegicus]8NP_44609425742651sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog[ Rattus norvegicus ]9BAB1979811990472sterol C5-desaturase [ Rattus norvegicus ]10XP_85300473955000PREDICTED: similar to sterol-C5-desaturase-like [ Canis familiaris ]11XP_50882555637121PREDICTED: similar to delta7-sterol-C5-desaturase [ Pantroglodytes ]12NP_001 . . .68160945sterol-C5-desaturase-like [ Homo sapiens ]13NP_00884968160941sterol-C5-desaturase-like [ Homo sapiens ]14BAD9686162897843sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-like variant [ Homo sapiens ]15BAD9640662896931sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-like variant [ Homo sapiens ]16AAH5042730046554Sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-like [ Homo sapiens ]17AAH1233315147389Sterol-C5-desaturase (ERG3 delta-5-desaturase homolog, fungal)-like [ Homo sapiens ]18AAF005446003685delta7-sterol-C5-desaturase [ Homo sapiens ]19BAB6821815637108sterol C5 desaturase [ Homo sapiens ]20O758456174975Lathosterol oxidase (Lathosterol 5-desaturase) (Delta-7-sterol 5-desaturase) (C-5 sterol desatur21BAA337293721882sterol-C5-desaturase [ Homo sapiens ]22XP_001 . . .1.09E+08PREDICTED: sterol-C5-desaturase (ERG3 delta-5-desaturasehomolog, fungal)-like isoform 2 [ Macaca23AAH7805550416254Sc5d-prov protein [ Xenopus laevis ]24NP_001 . . .52219112sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog[ Danio rerio ]25AAH8139551859008Sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog ( S. cerevisae )[ Danio rerio ]26BAA189701906796fungal sterol-C5-desaturase homolog [ Homo sapiens ]27XP_001 . . .1.09E+08PREDICTED: sterol-C5-desaturase (ERG3 delta-5-desaturasehomolog, fungal)-like isoform 1 [ Macaca28XP_79333172159211PREDICTED: similar to sterol-C5-desaturase (fungal ERG3, delta-5-desaturase) homolog [ Strongyloc29NP_001 . . .78369462hypothetical protein LOC525154 [ Bos taurus ]30AAI0333974353920Similar to sterol-C5-desaturase-like [ Bos taurus ]31CAF9049847207599unnamed protein product [ Tetraodon nigroviridis ] TABLE 61Examples of ERG27 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1Q12452603922633-keto-steroid reductase2CAA976641360483unnamed protein product [ Saccharomyces cerevisiae ]3AAB675441256850Ylr100wp [ Saccharomyces cerevisiae ]4Q6FIV3622869203-keto-steroid reductase5P_44984150294860hypothetical protein CAGL0M11506g [ Candida glabrata CBS138]6CAG6282149529155unnamed protein product [ Candida glabrata CBS138]7Q6CJC2622869193-keto-steroid reductase8P_45596750311871unnamed protein product [ Kluyveromyces lactis ]9CAG9867549645103unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]10Q74ZZ0622869263-keto-steroid reductase11P_98673345201163AGR068Wp [ Eremothecium gossypii ]12AAS5455744985946AGR068Wp [ Ashbya gossypii ATCC 10895]13Q6BNP0622869173-keto-steroid reductase14P_46018050423199hypothetical protein DEHA0E21263g [ Debaryomyces hansenii CBS15CAG8845349655848unnamed protein product [ Debaryomyces hansenii CBS767]16Q874K0622869353-keto-steroid reductase17AAN28009294658583-keto reductase [ Candida albicans ]18P_717865684761123-keto sterol reductase [ Candida albicans SC5314]19P_717931684759813-keto sterol reductase [ Candida albicans SC5314]20EAK9898246439667hypothetical protein CaO19.3240 [ Candida albicans SC5314]21EAK9891546439599hypothetical protein CaO19.10750 [ Candida albicans SC5314]22Q6CE88622869183-keto-steroid reductase23P_50102450547109hypothetical protein [ Yarrowia lipolytica ]24CAG8327749646890unnamed protein product [ Yarrowia lipolytica CLIB122]25P_595440191122323-keto sterol reductase [ Schizosaccharomyces pombe 972h-]26CAA212463738145SPBC1709.07 [ Schizosaccharomyces pombe ]27BAA138781749642unnamed protein product [ Schizosaccharomyces pombe ]28P_751680709936663-ketosteroid reductase [ Aspergillus fumigatus Af293]29EAL89642668493143-ketosteroid reductase [ Aspergillus fumigatus Af293]30P_95879985091228hypothetical protein [ Neurospora crassa OR74A]31EAA2956328920185hypothetical protein [ Neurospora crassa ]32BAE5817183768032unnamed protein product [ Aspergillus oryzae ]33EAQ8508688177618hypothetical protein CHGG_09100 [ Chaetomium globosum CBS14834EAT86025111064905hypothetical protein SNOG_06194 [ Phaeosphaeria nodorum SN15]35P_66318967538830hypothetical protein AN5585.2 [ Aspergillus nidulans FGSC A4]36EAA6222840743038hypothetical protein AN5585.2 [ Aspergillus nidulans FGSC A4]37EAS3622190306590hypothetical protein CIMG_01575 [ Coccidioides immitis RS]38AAO64345291506863-ketosteroid reductase [ Botryotinia fuckeliana ]39P_79677072131681PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase40P_79314572086766PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase41P_570518582667243-keto sterol reductase [ Cryptococcus neoformans var. neofor42AAW43211572267513-keto sterol reductase, putative [ Cryptococcus neoformans v43EAL2127950258592hypothetical protein CNBD3330 [ Cryptococcus neoformans var.44AAI0022071681260Unknown (protein for MGC: 114978) [ Xenopus laevis ]45BAE0684370720928hypothetical protein [ Epichloe festucae ]46P_001 . . .62859081hydroxysteroid (17-beta) dehydrogenase 7 [ Xenopus tropicalis47P_85169874006237PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase48CAC881191807784517beta-hydroxysteroid dehydrogenase type 7 [ Mus musculus ]49AAH1146415079256Hsd17b7 protein [ Mus musculus ]50P_03460687162470hydroxysteroid (17-beta) dehydrogenase 7 [ Mus musculus ]51BAC2591826390565unnamed protein product [ Mus musculus ]52BAC3412426340924unnamed protein product [ Mus musculus ]53O8873681344033-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)54CAA75742331997117-beta-hydroxysteroid dehydrogenase type 7 [ Mus musculus ]55P_69582068440091PREDICTED: similar to Hydroxysteroid (17-beta) dehydrogenase56P_0589318393576hydroxysteroid (17-beta) dehydrogenase 7 [ Rattus norvegicus ]57Q6290481344053-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)58AAC526231397235ovarian-specific protein59BAC3706126346825unnamed protein product [ Mus musculus ]60AAM212112038519617-beta-hydroxysteroid dehydrogenase type 7 [ Mus musculus ]61P_36337739951321hypothetical protein MG01303.4 [ Magnaporthe grisea 70-15]62P_58146776611932PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase63CAC881111807784317beta hydroxysteroid dehydrogenase [ Homo sapiens ]64AAX4203261361334hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc65AAX4203161361326hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc66CAI1345755959848hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]67CAI1594755959770hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]68AAH6524640807207Hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]69AAQ8932137183042HSD17B7 [ Homo sapiens ]70AAP3573830582989hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]71AAH0706813937918Hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]72CAC204181205369117beta-hydroxysteroid dehydrogenase type 7 [ Homo sapiens ]73P5693781344043-keto-steroid reductase (Estradiol 17-beta-dehydrogenase 7)74P_0574557705421hydroxysteroid (17-beta) dehydrogenase 7 [ Homo sapiens ]75AAF09266672109517 beta-hydroxysteroid dehydrogenase type VII [ Homo sapiens ]76ABB728538240027117-beta hydroxysteroid dehydrogenase 7 [ Macaca fascicularis ]77AAX2948760653587hydroxysteroid (17-beta) dehydrogenase 7 [synthetic construc78AAP3618030583863Homo sapiens hydroxysteroid (17-beta) dehydrogenase 7 [synth79AAF14537650298817beta-hydroxysteroid dehydrogenase type 7 [ Homo sapiens ]80AAK209501338337417-beta-hydroxysteroid dehydrogenase type 7 [ Oryctolagus cun81AAP9727533150794ovarian-specific protein; OSP [ Homo sapiens ]82P_42221050750970PREDICTED: similar to Estradiol 17 beta-dehydrogenase 7 (17- TABLE 62Examples of ERG26 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAT9304551013503YGL001C [ Saccharomyces cerevisiae ]2P531991723793Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating3CAA967011322447unnamed protein product [ Saccharomyces cerevisiae ]4P_44639050287923unnamed protein product [ Candida glabrata ]5CAG5931749525698unnamed protein product [ Candida glabrata CBS138]6P_45302550306127unnamed protein product [ Kluyveromyces lactis ]7CAH0187649642158unnamed protein product [ Kluyveromyces lactis NRRL Y-1140]8CAC3801613940379putative C-3 sterol dehydrogenase [ Zygosaccharomyces rouxii ]9P_98554845198519AFR001Wp [ Eremothecium gossypii ]10AAS5337244984470AFR001Wp [ Ashbya gossypii ATCC 10895]11P_45817850419307hypothetical protein DEHA0C12463g [ Debaryomyces hanseniiCBS767]12CAG8625249653844unnamed protein product [ Debaryomyces hansenii CBS767]13P_71556468481045C-3 sterol dehydrogenase/C-4 decarboxylase [ Candida albicansSC5314P_71562068480934C-3 sterol dehydrogenase/C-4 decarboxylase [ Candida albicansSC5315EAK9660146437251hypothetical protein CaO19.10427 [ Candida albicans SC5314]16EAK9654246437191hypothetical protein CaO19.2909 [ Candida albicans SC5314]17AAK6961714582743C-3 sterol dehydrogenase/C-4 decarboxylase [ Candida albicans ]18P_50212450549307hypothetical protein [ Yarrowia lipolytica ]19CAG8244449647991unnamed protein product [ Yarrowia lipolytica CLIB122]20P_59674119113533hypothetical protein SPBC3F6.02c [ Schizosaccharomyces pombe972h-21CAA176912924499SPBC3F6.02c [ Schizosaccharomyces pombe ]22AAQ8812937039511C-3 sterol dehydrogenase [ Cryptococcus neoformans var. grubii H9923P_38137946108642hypothetical protein FG01203.1 [ Gibberella zeae PH-1]24EAA6766742544824hypothetical protein FG01203.1 [ Gibberella zeae PH-1]25EAQ9088488183416conserved hypothetical protein [ Chaetomium globosum CBS 148.51]26P_640712668130663beta-hydroxysteroid dehydrogenase [ Dictyostelium discoideumAX4]27EAL66725604687233beta-hydroxysteroid dehydrogenase [ Dictyostelium discoideumAX4]28EAT77489111056369hypothetical protein SNOG_15264 [ Phaeosphaeria nodorum SN15]29P_96546685118539hypothetical protein [ Neurospora crassa OR74A]30CAE7651838567226related to C-3 sterol dehydrogenase (C-4 decarboxylase) [Neurospo31EAA3623028927275hypothetical protein [ Neurospora crassa ]32P_42027950745878PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like33P_001 . . .78369400hypothetical protein LOC616694 [ Bos taurus ]34AAI0339073586574Similar to NAD(P) dependent steroid dehydrogenase-like [ Bos tauru35P_001 . . .62859757hypothetical protein LOC550044 [ Xenopus tropicalis ]36AAH8869956788986LOC496236 protein [ Xenopus laevis ]37P_53819974008671PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like38P_85307374008673PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like39AAH5283431127258NAD(P) dependent steroid dehydrogenase-like [ Mus musculus ]40P_001 . . .109132673PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like41P_001 . . .109132671PREDICTED: similar to NAD(P) dependent steroid dehydrogenase-like42P_001 . . .57164113NAD(P) dependent steroid dehydrogenase-like [ Rattus norvegicus ]43AAH8762656388600NAD(P) dependent steroid dehydrogenase-like [ Rattus norvegicus ]44BAE2452274187675unnamed protein product [ Mus musculus ]45P_03507131982437NAD(P) dependent steroid dehydrogenase-like [ Mus musculus ]46Q9R1J08473695Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating47CAA159487619723NAD(P)H steroid dehydrogenase [ Mus musculus ]48AAD384485052206putative NAD(P)H steroid dehydrogenase [ Mus musculus ]49AAH1994518043286NAD(P) dependent steroid dehydrogenase-like [ Mus musculus ]50AAH0781614043700NAD(P) dependent steroid dehydrogenase-like [ Homo sapiens ]51AAH0024512652969NAD(P) dependent steroid dehydrogenase-like [ Homo sapiens ]52Q157388488997Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating (H10553P_0570068393516NAD(P) dependent steroid dehydrogenase-like [ Homo sapiens ]54AAC505584457237H105e3 [ Homo sapiens ]55CAF9910747222951unnamed protein product [ Tetraodon nigroviridis ]56P_75607571002788C-3 sterol dehydrogenase/C-4 decarboxylase [ Aspergillus fumigatus57EAL9403766853713C-3 sterol dehydrogenase/C-4 decarboxylase [ Aspergillus fumigatus58P_56729958259773C-3 sterol dehydrogenase (C-4 sterol decarboxylase) [ Cryptococcus59AAW4578257229349C-3 sterol dehydrogenase (C-4 sterol decarboxylase), putative [Cr60EAL1838350255650hypothetical protein CNBJ3060 [ Cryptococcus neoformans var.neofo61P_001 . . .62955325hypothetical protein LOC550369 [ Danio rerio ]62AAH9333262204675Zgc: 112474 [ Danio rerio ]63EAS3701190307380hypothetical protein CIMG_02365 [ Coccidioides immitis RS]64P_75583671002310C-3 sterol dehydrogenase/C-4 decarboxylase [ Aspergillus fumigatus65EAL9379866853474C-3 sterol dehydrogenase/C-4 decarboxylase [ Aspergillus fumigatus66CAH9081555728130hypothetical protein [ Pongo pygmaeus ]67P_76027471020087hypothetical protein UM04127.1 [ Ustilago maydis 521]68EAK8515546099922hypothetical protein UM04127.1 [ Ustilago maydis 521]69P_68084467901176hypothetical protein AN7575.2 [ Aspergillus nidulans FGSC A4]70EAA6215540742965hypothetical protein AN7575.2 [ Aspergillus nidulans FGSC A4]71AAZ1493670906332putative sterol dehydrogenase [ Coprinellus disseminatus ] TABLE 63Examples of ERG25 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAS5615345269545YGR060W [ Saccharomyces cerevisiae ]2XP_44842050291975unnamed protein product [ Candida glabrata ]3XP_45189050303885unnamed protein product [ Kluyveromyces lactis ]4NP_98611945199090AFR572Wp [ Eremothecium gossypii ]5XP_45686150409318hypothetical protein DEHA0A12661g [ Debaryomyces hanseniiCBS767]6XP_71342068485318C-4 sterol methyl oxidase [ Candida albicans SC5314]7XP_46165850426123hypothetical protein DEHA0G03124g [ Debaryomyces hanseniiCBS767]8XP_50528150555746hypothetical protein [ Yarrowia lipolytica ]9XP_72270368466442putative C-4 sterol methyl oxidase [ Candida albicans SC5314]10XP_72284968466149putative C-4 sterol methyl oxidase [ Candida albicans SC5314]11ABF84061107785180C-4 sterol methyl oxidase [ Chaetomium globosum ]12Q9UUH428558117C-4 methylsterol oxidase (Methylsterol monooxygenase)13XP_96224085106720hypothetical protein [ Neurospora crassa OR74A]14EAT84680111063560hypothetical protein SNOG_08404 [ Phaeosphaeria nodorum SN15]15XP_74666870982279hypothetical protein Afu4g04820 [ Aspergillus fumigatus Af293]16XP_39000646136629hypothetical protein FG09830.1 [ Gibberella zeae PH-1]17BAE6538183775259unnamed protein product [ Aspergillus oryzae ]18XP_36082739942580hypothetical protein MG03370.4 [ Magnaporthe grisea 70-15]19ABA7059077377695hypothetical protein [ Penicillium chrysogenum ]20XP_36933139975881hypothetical protein MG06133.4 [ Magnaporthe grisea 70-15]21EAS2976290300131hypothetical protein CIMG_08508 [ Coccidioides immitis RS]22XP_76202771023595hypothetical protein UM05880.1 [ Ustilago maydis 521]23XP_56952658264740C-4 methyl sterol oxidase [ Cryptococcus neoformans var.neoformans JEC21]24EAQ8812588180657hypothetical protein CHGG_04744 [ Chaetomium globosum CBS148.51]25BAE6649183776372unnamed protein product [ Aspergillus oryzae ]26XP_74696270982869c-4 methyl sterol oxidase [ Aspergillus fumigatus Af293]27XP_68217667903840hypothetical protein AN8907.2 [ Aspergillus nidulans FGSC A4]28XP_66457767541619hypothetical protein AN6973.2 [ Aspergillus nidulans FGSC A4]29XP_64627766825845hypothetical protein DDBDRAFT_0190553 [ Dictyosteliumdiscoideum AX4]30NP_99891747523336sterol-C4-methyl oxidase-like protein [ Sus scrofa ]31AAI0788079160074Sterol-C4-methyl oxidase-like [ Homo sapiens ]32BAE0192167971158unnamed protein product [ Macaca fascicularis ]33XP_001 . . .109076099PREDICTED: sterol-C4-methyl oxidase-like isoform 3 [ Macacamulatta ]34XP_58061561871492PREDICTED: similar to C-4 methylsterol oxidase (Methylsterolmonooxygenase) isoform 1 [ Bos taurus ]35CAC2447112311696hypothetical protein [ Candida albicans ]36BAE3014374185334unnamed protein product [ Mus musculus ]37XP_53271457096891PREDICTED: similar to C-4 methylsterol oxidase (Methylsterolmonooxygenase) isoform 1 [ Canis familiaris ]38CAF9215347211304unnamed protein product [ Tetraodon nigroviridis ]39AAH6315538649308Sterol-C4-methyl oxidase-like [ Rattus norvegicus ]40NP_001 . . .57530155sterol-C4-methyl oxidase-like [ Gallus gallus ]41NP_99851847087009sterol-C4-methyl oxidase-like [ Danio rerio ]42NP_56378918390767SMO2-2; C-4 methylsterol oxidase [ Arabidopsis thaliana ]43AAI21457111309060Unknown (protein for MGC: 146461) [ Xenopus tropicalis ]44AAM6482121592871putative C-4 sterol methyl oxidase [ Arabidopsis thaliana ]45AAF795718778563F22G5.23 [ Arabidopsis thaliana ]46AAO1379527448145putative sterol 4-alpha-methyl-oxidase [ Gossypium arboreum ]47AAO4860428864263ERG25 [ Clavispora lusitaniae ]48AAQ8369234978966C-4 sterol methyl oxidase 2 [ Nicotiana benthamiana ]49ABD9715390658509C-4 methyl sterol oxidase [ Cryptococcus neoformans var.neoformans ]50ABD9714690658495C-4 methyl sterol oxidase [ Cryptococcus neoformans var. grubii ]51ABD9714790658497C-4 methyl sterol oxidase [ Cryptococcus neoformans var. grubii ]52ABD9713490658471C-4 methyl sterol oxidase [ Cryptococcus neoformans var.neoformans ]53AAL8257627447203putative sterol 4-alpha-methyl-oxidase [ Zea mays ]54NP_85013330684225SMO2-1; C-4 methylsterol oxidase [ Arabidopsis thaliana ]55NP_97355942570971SMO2-1; C-4 methylsterol oxidase [ Arabidopsis thaliana ]56AAL3228716973432sterol 4-alpha-methyl-oxidase [ Arabidopsis thaliana ]57ABE8322692875070Sterol desaturase [ Medicago truncatula ]58BAF28920113645779Os11g0707600 [ Oryza sativa ( japonica cultivar-group)]59BAF20592113610214Os07g0101500 [ Oryza sativa ( japonica cultivar-group)]60XP_78744272077919PREDICTED: similar to C-4 methylsterol oxidase (Methylsterolmonooxygenase) [ Strongylocentrotus purpuratus ]61AAM6435921592408putative C-4 sterol methyl oxidase [ Arabidopsis thaliana ]62NP_97377742571373SMO2-2; C-4 methylsterol oxidase [ Arabidopsis thaliana ]63NP_001 . . .62865628sterol-C4-methyl oxidase-like isoform 2 [ Homo sapiens ]64AAX95419627333024-alpha-methyl-sterol C4-methyl-oxidase [ Oryza sativa ( japonicacultivar-group)]65XP_88387576638226PREDICTED: similar to C-4 methylsterol oxidase (Methylsterolmonooxygenase) isoform 3 [ Bos taurus ]66ABE8743492884635Sterol desaturase [ Medicago truncatula ]67XP_64155366814748hypothetical protein DDBDRAFT_0205936 [ Dictyosteliumdiscoideum AX4]68AAM6542821593461putative C-4 sterol methyl oxidase [ Arabidopsis thaliana ]69NP_56766918416002SMO1-3 (STEROL 4-ALPHA METHYL OXIDASE); catalytic[ Arabidopsis thaliana ]70AAM6496121593012putative C-4 sterol methyl oxidase [ Arabidopsis thaliana ]71AAN1811523308291At4g12110/F16J13_180 [ Arabidopsis thaliana ]72AAK6136127446631putative sterol 4-alpha-methyl-oxidase [ Arabidopsis thaliana ]73BAF01201110738551hypothetical protein [ Arabidopsis thaliana ]74AAQ1342433337546sterol-4-methyl-oxidase [ Arabidopsis thaliana ]75BAF27120113639815Os10g0545200 [ Oryza sativa ( japonica cultivar-group)]76CAB782547267912putative C-4 sterol methyl oxidase [ Arabidopsis thaliana ]77AAQ9411837591406sterol-4-alpha methyl oxidase [ Arabidopsis thaliana ]78AAQ8369134978964C-4 sterol methyl oxidase 1 [ Nicotiana benthamiana ]79ABD6553689266491sterol-C4-methyl oxidase-like [ Ictalurus punctatus ]80BAC5796128804511putative C-4 sterol methyl oxidase [ Aster tripolium ] TABLE 64Examples of ERG24 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAB30203545906sterol delta 14 reductase; Erg24p [ Saccharomyces cerevisiae ]2XP_44738050289897hypothetical protein CAGL0I02970g [ Candida glabrata CBS138]3XP_45274450305569unnamed protein product [ Kluyveromyces lactis ]4NP_98589345198864AFR346Wp [ Eremothecium gossypii ]5XP_71067068491033sterol C-14 reductase [ Candida albicans SC5314]6XP_45837150419687hypothetical protein DEHA0C16984g [ Debaryomyces hanseniiCBS767]7XP_50126050547581hypothetical protein [ Yarrowia lipolytica ]8XP_56654858258271C-14 sterol reductase [ Cryptococcus neoformans var. neoformansJEC21]9NP_59676719113559hypothetical protein SPBC16G5.18 [ Schizosaccharomyces pombe972h-]10EAL2345450260804hypothetical protein CNBA1040 [ Cryptococcus neoformans var.neoformans B-3501A]11XP_75978671019111hypothetical protein UM03639.1 [ Ustilago maydis 521]12XP_38678246124457ER24_FUSSO Delta(14)-sterol reductase (C-14 sterol reductase)(Sterol C14-reductase) [ Gibberella zeae PH-1]13P785756015106Delta(14)-sterol reductase (C-14 sterol reductase) (Sterol C14-reductase)14Q014473929349Delta(14)-sterol reductase (C-14 sterol reductase) (Sterol C14-reductase) TABLE 65Examples of ERG11 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAA34546171354lanosterol 14-demethylase cytochrome P4502AAA34547171356lanosterol 14-demethylase cytochrome P4503AAY594176696794414alpha-demethylase [ Candida glabrata ]4XP_45410950308217unnamed protein product [ Kluyveromyces lactis ]5Q759W051701328Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)6AAB32679912807cyto chrome P-450 lanosterol-alpha-demethylase; P450-L1A1[ Candida glabrata ]7AAX3931661189834lanosterol 14 alpha demethylase [ Candida tropicalis ]8AAF005986006769cytochrome P450 lanosterol 14-alpha demethylase [ Candidaalbicans ]9XP_71676168478280lanosterol 14-alpha-demethylase [ Candida albicans SC5314]10XP_46014350423125hypothetical protein DEHA0E20383g [ Debaryomyces hanseniiCBS767]11ABC4192183728463cytochrome P450 lanosterol 14 alpha demethylase [ Candidaalbicans ]12AAX3931561189832lanosterol 14 alpha demethylase [ Candida tropicalis ]13O4CK5165689lanosterol 14alpha-demethylase (EC 1.14.14. - ) cytochrome P450 51 -yeast ( Candida albicans )14XP_71682268478161lanosterol 14-alpha-demethylase [ Candida albicans SC5314]15AAF006036006774cytochrome P450 lanosterol 14-alpha demethylase [ Candidaalbicans ]16AAF006006006771cytochrome P450 lanosterol 14-alpha demethylase [ Candidaalbicans ]17BAB034019558446CYP51 variant 3 [ Candida albicans ]18AAK5751914280372lanosterol 14-alpha demethylase Erg11p [ Candida dubliniensis ]19AAF006026006773cytochrome P450 lanosterol 14-alpha demethylase [ Candidaalbicans ]20AAF006016006772cytochrome P450 lanosterol 14-alpha demethylase [ Candidaalbicans ]21BAB034009558444CYP51 variant 2 [ Candida albicans ]22AAO8389829378393cytochrome P-450 lanosterol-alpha-demethylase [ Issatchenkiaorientalis ]23AAW5059357341382Erg11p [ Candida albicans ]24AAW5059257341380Erg11p [ Candida albicans ]25XP_50051850545962hypothetical protein [ Yarrowia lipolytica ]26BAC1651723263326cytochrome P-450 lanosterol 14alpha-demethylase [ Candidaalbicans ]27BAC1652023263332cytochrome P-450 lanosterol 14alpha-demethylase [ Candidaalbicans ]28BAC1651823263328cytochrome P-450 lanosterol 14alpha-demethylase [ Candidaalbicans ]29BAC1651923263330cytochrome P-450 lanosterol 14alpha-demethylase [ Candidaalbicans ]30Q023152493385Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)31AAO3877628395121lanosterol 14 alpha demethylase; ERG11 [ Pneumocystis carinii ]32ABG91757110816094sterol 14alpha-demethylase [ Pneumocystis carinii ]33BAE6023983770104unnamed protein product [ Aspergillus oryzae ]34XP_7491347098744114-alpha sterol demethylase Cyp51B [ Aspergillus fumigatus Af293]35XP_65950567522889hypothetical protein AN1901.2 [ Aspergillus nidulans FGSC A4]36XP_68155267902592hypothetical protein AN8283.2 [ Aspergillus nidulans FGSC A4]37AAK736591486141314-alpha sterol demethylase [ Aspergillus fumigatus ]38XP_7521377099472014-alpha sterol demethylase Cyp51A [ Aspergillus fumigatus Af293]39BAE5741783767278unnamed protein product [ Aspergillus oryzae ]40AAF792048778097cytochrome P450 sterol 14 alpha-demethylase [ Emericella nidulans ]41CAE1809133300264eburicol 14 alpha demethylase [ Blumeria graminis ]42EAS2872390299092cytochrome P450 51 [ Coccidioides immitis RS]43CAE1809433300270eburicol 14 alpha demethylase [ Blumeria graminis ]44CAC8562433300256eburicol 14alpha demethylase [ Blumeria graminis f. sp. tritici]45CAE1809533300272eburicol 14 alpha demethylase [ Blumeria graminis ]46CAE1751533284834eburicol 14 alpha demethylase [ Blumeria graminis f. sp. tritici ]47AAU4373452352491eburicol 14 alpha-demethylase [ Mycosphaerella graminicola ]48EAS3521990305588cytochrome P450 51 [ Coccidioides immitis RS]49CAE1810233300286eburicol 14 alpha demethylase [ Blumeria graminis ]50CAE1810333300288eburicol 14 alpha demethylase [ Blumeria graminis ]51CAE1810533300292eburicol 14 alpha demethylase [ Blumeria graminis ]52NP_59299019113902hypothetical protein SPAC13A11.02c [ Schizosaccharomyces pombe972h-]53CAE1810033300282eburicol 14 alpha demethylase [ Blumeria graminis ]54AAP7960132330152eburicol 14alpha-demethylase [ Mycosphaerella graminicola ]55AAC976064049645eburicol 14alpha demethylase; CYP51; cytochrome P450 sterol 14-demethylase [ Blumeria graminis f. sp. hordei ]56CAE1809933300280eburicol 14 alpha demethylase [ Blumeria graminis ]57BAE6355483773427unnamed protein product [ Aspergillus oryzae ]58XP_38117646108236hypothetical protein FG01000.1 [ Gibberella zeae PH-1]59AAF859839230788eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]60AAP8193432441730eburicol 14 alpha-demethylase [ Mycosphaerella graminicola ]61XP_36218339945292hypothetical protein MG04628.4 [ Magnaporthe grisea 70-15]62AAP1237030314338lanosterol 14 alpha-demethylase; 14 alpha lanosterol demethylase[ Cryptococcus neoformans var. grubii ]63AAF747568347731eburicol 14-alpha demethylase [ Mycosphaerella graminicola ]64AAF76464857017614 alpha-demethylase [ Venturia inaequalis]65XP_56646458258103sterol 14-demethylase [ Cryptococcus neoformans var. neoformansJEC21]66EAQ9341788185949conserved hypothetical protein [ Chaetomium globosum CBS148.51]67AAL7918018766932eburicol 14 alpha-demethylase [ Monilinia fructicola ]68AAU0115751341094lanosterol 14-alpha-demethylase [ Coccidioides posadasii ]69CAD2779319572745cytochrome P-450 14DM [ Penicillium digitatum ]70XP_38426846116500hypothetical protein FG04092.1 [ Gibberella zeae PH-1]71AAG1843310505323eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]72AAK2639113445823eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]73AAG1843110505318eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]74AAK2638613445813eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]75AAD551355881952eburicol 14-alpha demethylase; cytochrome P450 sterol 14-alphademethylase; Erg11 [ Uncinula necator ]76AAK2638913445819eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]77CAC8540915864613euburicol 14 alpha-demethylase [ Venturia nashicola ]78BAB036599664027cytochrome P-450 14DM [ Penicillium digitatum ]79AAG1843510505329eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]80AAG1843410505326eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]81AAU0115851341096lanosterol 14-alpha-demethylase [ Ajellomyces capsulatus ]82AAK2638713445815eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]83AAG1843210505321eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]84AAK2638813445817eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]85XP_39120046139019hypothetical protein FG11024.1 [ Gibberella zeae PH-1]86AAK2639013445821eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]87O1444214916976Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alphademethylase) (Eburicol 14-alpha-demethylase) (P450-14DM)88AAG1843810505336eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]89XP_75980971019157sterol 14-alpha demethylase [ Ustilago maydis 521]90AAF184686581118eburicol 14 alpha-demethylase [ Tapesia acuformis ]91AAG1843610505331eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]92AAC498015733843eburicol 14-alpha demethylase [ Uncinula necator ]93ABE011079082321114alpha demethylase [ Blumeriella jaapii ]94AAG1843710505334eburicol 14 alpha-demethylase [ Botryotinia fuckeliana ]95CAD2779219572743cytochrome P-450 14DM [ Penicillium digitatum ]96XP_96404985111674hypothetical protein [ Neurospora crassa OR74A]97AAF1846911178694eburicol 14 alpha-demethylase [ Tapesia yallundae ]98Q126642493386Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alphademethylase) (Eburicol 14-alpha-demethylase) (P450-14DM)99AAG4483212006321eburicol 14-alpha demethylase [ Tapesia yallundae ]100AAG4483112006319eburicol 14-alpha demethylase [ Tapesia yallundae ]101AAN2892723505745sterol 14 alpha-demethylase ERG11 [ Leptosphaeria maculans ]102XP_36198739944900hypothetical protein MG04432.4 [ Magnaporthe grisea 70-15]103EAT88907111067787hypothetical protein SNOG_03702 [ Phaeosphaeria nodorum SN15]104AAU0116051341100lanosterol 14-alpha-demethylase [ Phanerochaete chrysosporium ]105AAC235503220152cytochrome P450 L1A1 demethylase [ Pichia anomala ]106AAU0115951341098lanosterol 14-alpha-demethylase [ Coprinopsis cinerea ]107Q9UVC312229768Cytochrome P450 51 (CYPLI) (P450-LIA1) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (P450-14DM)108AAQ8812837039509cytochrome P450 lanosterol 14a-demethylase [ Cryptococcusneoformans var. grubii H99]109NP_06439471061451cytochrome P450, family 51 [ Mus musculus ]110EAL2415451094909cytochrome P450, family 51, subfamily A, polypeptide 1 [ Homosapiens ]111Q168503915660Cytochrome P450 51A1 (CYPLI) (P450LI) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-14DM) (P45014DM)112NP_99959747523914cytochrome P450 51 [ Sus scrofa ]113BAC2723126326975unnamed protein product [ Mus musculus ]114Q5RE7283287777Cytochrome P450 51A1 (CYPLI) (P450LI) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-14DM) (P45014DM)115Q4PJW375075066Cytochrome P450 51A1 (CYPLI) (P450LI) (Sterol 14-alphademethylase) (Lanosterol 14-alpha demethylase) (LDM) (P450-14DM) (P45014DM)116AAF745628347236lanosterol 14-alpha-demethylase [ Mus musculus ]117AAC509511698484lanosterol 14-alpha demethylase [ Homo sapiens ]118XP_53245757095976PREDICTED: similar to Cytochrome P450 51A1 (CYPLI) (P450LI)(Sterol 14-alpha demethylase) (Lanosterol 14-alpha demethylase)(LDM) (P450-14DM) (P45014DM) isoform 1 [ Canis familiaris ]119AAF739868215679lanosterol 14-alpha-demethylase [ Mus musculus ]120AAH8121051703589MGC84806 protein [ Xenopus laevis ]121AAA87074699396lanosterol 14-alpha-demethylase122XP_41865050732469PREDICTED: similar to lanosterol 14-demethylase [ Gallus gallus ]123BAE0150867970330unnamed protein product [ Macaca fascicularis ]124AAR896244074828714-alpha demethylase [ Fundulus heteroclitus ]125NP_001 . . .50053648cytochrome P450, family 51 [ Strongylocentrotus purpuratus ]126AAR896254074828914-alpha demethylase [ Danio rerio ]127NP_001 . . .99028936cytochrome P450, family 51 [ Danio rerio ]128CAJ8184189268132cytochrome P450, family 51, subfamily A, polypeptide 1 [ Xenopustropicalis ]129AAR896264074829114-alpha demethylase [ Abudefduf saxatilis ] TABLE 66Examples of ERG4 polypeptides.RowACCESSIONGIPROTEIN DESCRIPTION1AAD138954261595Unknown [ Saccharomyces cerevisiae ]2AAT9322451013861YGL012W [ Saccharomyces cerevisiae ]3AAY4296266270055C24 sterol reductase [ Candida glabrata ]4XP_45122350302575unnamed protein product [ Kluyveromyces lactis ]5NP_98657945201009AGL087Cp [ Eremothecium gossypii ]6XP_45670950407411hypothetical protein DEHA0A08888g [ Debaryomyces hansenii CBS767]7XP_71766268476402sterol C-24 (28) reductase [ Candida albicans SC5314]8XP_50302150551095hypothetical protein [ Yarrowia lipolytica ]9EAU37607114195907Delta(24(24(1)))-sterol reductase [ Aspergillus terreus NIH2624]10BAE6106483770931unnamed protein product [ Aspergillus oryzae ]11NP_59474219115654hypothetical protein SPAC20G4.07c [ Schizosaccharomyces pombe 972h-]12CAA451135109sts1+ [ Schizosaccharomyces pombe ]13XP_66278867538028hypothetical protein AN5184.2 [ Aspergillus nidulans FGSC A4]14XP_75046170991224c-24(28) sterol reductase [ Aspergillus fumigatus Af293]15EAS3711490307483hypothetical protein CIMG_02468 [ Coccidioides immitis RS]16XP_36576339968745hypothetical protein MG02465.4 [ Magnaporthe grisea 70-15]17CAC1822316944336probable sterol C-24 reductase [ Neurospora crassa ]18XP_96141985102913probable sterol C-24 reductase [MIPS] [ Neurospora crassa OR74A]19XP_66028867524453hypothetical protein AN2684.2 [ Aspergillus nidulans FGSC A4]20EAU33849114192149Delta(24(24(1)))-sterol reductase [ Aspergillus terreus NIH2624]21XP_75322170996933c-24(28) sterolreductase [ Aspergillus fumigatus Af293]22BAE5962483769489unnamed protein product [ Aspergillus oryzae ]23EAT92432111071312predicted protein [ Phaeosphaeria nodorum SN15]24XP_39017946136975hypothetical protein FG10003.1 [ Gibberella zeae PH-1]25XP_75764571005958hypothetical protein UM01498.1 [ Ustilago maydis 521]26EAS3744990307818hypothetical protein CIMG_02803 [ Coccidioides immitis RS]27NP_82020129654509c-24(28) sterol reductase, putative [ Coxiella burnetii RSA 493]28ZP_012 . . .94491050hypothetical protein CburD_01001859 [ Coxiella burnetii Dugway 7E9-12]29AAQ8813037039513sterol C-24 reductase [ Cryptococcus neoformans var. grubii H99]30XP_56969758265082delta24(24-1) sterol reductase [ Cryptococcus neoformans var.neoformans JEC21]31EAQ9072188183253hypothetical protein CHGG_02656 [ Chaetomium globosum CBS 148.51]32BAE5560683765463unnamed protein product [ Aspergillus oryzae ]33CAJ0607868128884sterol C-24 reductase, putative [ Leishmania major ]34ABD4655588601114sterol C-24 reductase-like protein [ Acanthamoeba castellanii ]35XP_63861366809779ERG4/ERG24 ergosterol biosynthesis protein family protein[ Dictyostelium discoideum AX4] TABLE 67Examples of beta-carotene 15,15′-monooxygenase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAG1538110242318beta, beta-carotene 15,15′-dioxygenase [ Mus musculus ]EDL92648149038288beta-carotene 15,15′-monooxygenase [ Rattus norvegicus ]Q91XT546397349Beta,beta-carotene 15,15′-monooxygenase (Beta-carotene dioxygenase1)XP_54681557087275PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1) [ Canis familiaris ]XP_001 . . .149699876PREDICTED: similar to beta, beta-carotene 15,15-dioxygenase[ Equus caballus ]EAW95537119615943beta-carotene 15,15′-monooxygenase 1, isoform CRA_a [ Homosapiens ]Q9HAY641688803Beta,beta-carotene 15,15′-monooxygenase (Beta-carotene dioxygenase1)BAA917767022941unnamed protein product [ Homo sapiens ]BAC3567926344045unnamed protein product [ Mus musculus ]NP_001 . . .66792910beta-carotene 15,15′-monooxygenase 1 [ Bos taurus ]XP_001 . . .126303742PREDICTED: similar to beta, beta-carotene 15,15-dioxygenase[ Monodelphis domestica ]XP_523435114663815PREDICTED: beta-carotene 15,15′-monooxygenase 1 [ Pantroglodytes ]XP_41416350753878PREDICTED: beta-carotene 15,15′-monooxygenase 1 [ Gallus gallus ]EAW95538119615944beta-carotene 15,15′-monooxygenase 1, isoform CRA_b [ Homosapiens ]AAH5678934784018Zgc: 63614 [ Danio rerio ]NP_57187342476258beta-carotene 15,15′-monooxygenase 1 [ Danio rerio ]CAC3756613872740putative b,b-carotene-15,15′-dioxygenase [ Danio rerio ]CAF9576447214429unnamed protein product [ Tetraodon nigroviridis ]CAF9246947212035unnamed protein product [ Tetraodon nigroviridis ]ABQ09267146186430beta-carotene 15,15′-monooxygenase 1 [ Oryzias latipes ]CAM14044122890964beta-carotene 15,15-dioxygenase 2 [ Danio rerio ]AAI33726126631776Bcdo2 protein [ Rattus norvegicus ]CAC3756713872742putative b,b-carotene-9′,10′-dioxygenase [ Danio rerio ]AAI0700776825286Beta-carotene 9′,10′-dioxygenase 2 [ Mus musculus ]AAI35025141795614Bcdo21 protein [ Danio rerio ]NP_001 . . .55741954beta-carotene dioxygenase 2 [ Xenopus tropicalis ]XP_417929118102019PREDICTED: similar to carotene-9,10-monooxygenase [ Gallus gallus ]Q5RF1675042584Beta,beta-carotene 9′,10′-dioxygenase (Beta-carotene dioxygenase 2)(B-diox-II)XP_001 . . .109108669PREDICTED: beta-carotene dioxygenase 2 [ Macaca mulatta ]BAC4178226449309hypothetical protein [ Macaca fascicularis ]Q8HXG847117670Beta,beta-carotene 9′,10′-dioxygenase (Beta-carotene dioxygenase 2)(B-diox-II)AAI1526092098295Beta-carotene 15,15-dioxygenase 2 [ Danio rerio ]AAS2039242560440carotene-9′,10′-monooxygenase [ Mustela putorius furo ]CAG0368047217728unnamed protein product [ Tetraodon nigroviridis ]XP_53657273955144PREDICTED: similar to Beta,beta-carotene 9,10-dioxygenase (Beta-carotene dioxygenase 2) (B-diox-II) [ Canis familiaris ]XP_001 . . .126327024PREDICTED: similar to carotene-9,10-monooxygenase [ Monodelphisdomestica ]XP_001 . . .114640348PREDICTED: beta-carotene dioxygenase 2 isoform 3 [ Pan troglodytes ]XP_001 . . .114640346PREDICTED: beta-carotene dioxygenase 2 isoform 4 [ Pan troglodytes ]AAK6943314582265putative carotene dioxygenase [ Homo sapiens ]Q9BYV741688802Beta,beta-carotene 9′,10′-dioxygenase (Beta-carotene dioxygenase 2)(B-diox-II)EAW67194119587598beta-carotene dioxygenase 2, isoform CRA_f [ Homo sapiens ]EAW67189119587593beta-carotene dioxygenase 2, isoform CRA_a [ Homo sapiens ]XP_001 . . .149716895PREDICTED: similar to carotene-9,10-monooxygenase [ Equuscaballus ]NP_001 . . .82617628beta-carotene dioxygenase 2 isoform b [ Homo sapiens ]NP_11414482617624beta-carotene dioxygenase 2 isoform a [ Homo sapiens ]CAC2799412666531putative b,b-carotene-9′,10′-dioxygenase [ Homo sapiens ]XP_508757114640350PREDICTED: hypothetical protein isoform 5 [ Pan troglodytes ]BAB5537914042749unnamed protein product [ Homo sapiens ]EAW67193119587597beta-carotene dioxygenase 2, isoform CRA_e [ Homo sapiens ]NP_001 . . .147906096hypothetical protein LOC791719 [ Danio rerio ]XP_001 . . .125824393PREDICTED: similar to retinal pigment epithelium 65b [ Danio rerio ]AAH5955937748750Zgc: 73213 [ Danio rerio ]AAC14586675485retinal pigment epithelium-specific 61 kDa protein [ Homo sapiens ]XP_001 . . .109008381PREDICTED: retinal pigment epithelium-specific protein 65 kDa[ Macaca mulatta ]NP_001 . . .71480121retinal pigment epithelium 65b [ Danio rerio ]NP_084263147902089retinal pigment epithelium 65 [ Mus musculus ]AAD420425326773retinal pigment epithelium-specific protein RPE65 [ Cercopithecusaethiops ]AAL0111915488446RPE65 [ Mus musculus ]CAA46988564membrane receptor p63 [ Bos taurus ]AAC37306163657retinal pigment epithelium-specific 65 kD proteinEDL82582149026339retinal pigment epithelium 65 [ Rattus norvegicus ]NP_44601416758332retinal pigment epithelium 65 [ Rattus norvegicus ]NP_001 . . .148228575retinal pigment epithelium-specific protein 65 kDa [ Xenopus laevis ]AAC723563851555retinal pigment epithelium-specific protein RPE65 [ Canis familiaris ]CAF9847347220374unnamed protein product [ Tetraodon nigroviridis ]NP_001 . . .50978910retinal pigment epithelium-specific protein 65 kDa [ Canis lupusfamiliaris ]AAD127584001821RPE65 protein; retinal pigment epithelium 65-protein [ Ambystomatigrinum ]XP_001 . . .126305965PREDICTED: similar to membrane receptor p63 [ Monodelphisdomestica ]NP_001 . . .156120623hypothetical protein LOC514135 [ Bos taurus ]Q9YGX248475042Retinal pigment epithelium-specific 65 kDa proteinNP_001 . . .147906384MGC85437 protein [ Xenopus laevis ]NP_001 . . .118344140beta-carotene-15,15′-monooxygenase [ Ciona intestinalis ]BAC4135126005798retinal pigment epithelium abundant protein [ Cynops pyrrhogaster ]XP_001 . . .114557125PREDICTED: retinal pigment epithelium-specific protein 65 kDa [ Pantroglodytes ]NP_001 . . .148230104beta-carotene dioxygenase 2 [ Xenopus laevis ]XP_001 . . .114640352PREDICTED: beta-carotene dioxygenase 2 isoform 2 [ Pan troglodytes ]XP_001 . . .115928922PREDICTED: similar to beta-carotene 15,15-dioxygenase[ Strongylocentrotus purpuratus ]AAL3909617432605RPE65 [ Mus musculus ]XP_001 . . .125816256PREDICTED: similar to Beta-carotene 15,15-dioxygenase 2 [ Daniorerio ]XP_001 . . .156342819hypothetical protein NEMVEDRAFT_v1g222532 [ Nematostellavectensis ]XP_001 . . .125824367PREDICTED: similar to retinal pigment epithelium 65b [ Danio rerio ]XP_001 . . .156393603predicted protein [ Nematostella vectensis ]XP_001 . . .156371447predicted protein [ Nematostella vectensis ]AAH6769645767835Bcdo2l protein [ Danio rerio ]CAD4501022657452retinal pigment epithelium-specific protein [ Canis familiaris ]NP_001 . . .118344130RPE65 homolog [ Ciona intestinalis ]XP_317319118789286ENSANGP00000006854 [ Anopheles gambiae str. PEST]EAA12399157014990AGAP008143-PA [ Anopheles gambiae str. PEST]AAY8535068132170carotenoid 9′,10′ monoxygenase II [ Rattus norvegicus ]XP_001 . . .115969938PREDICTED: similar to beta-carotene 15,15-dioxygenase, partial[ Strongylocentrotus purpuratus ]XP_001 . . .157135394beta-carotene dioxygenase [ Aedes aegypti ]XP_96746091093114PREDICTED: similar to CG9347-PA [ Tribolium castaneum ]NP_49672971998242Y46G5A.24 [ Caenorhabditis elegans ]XP_001 . . .156398339predicted protein [ Nematostella vectensis ]XP_39400066523635PREDICTED: similar to neither inactivation nor afterpotential BCG9347-PA isoform 1 [ Apis mellifera ]F8811525395537protein F53C3.12 [imported] - Caenorhabditis elegansAAC6746226251528Hypothetical protein F53C3.12 [ Caenorhabditis elegans ]XP_001 . . .149709742PREDICTED: similar to retinal pigment epithelium abundant proteinRPE65 [ Equus caballus ]CAE7149439582162Hypothetical protein CBG18419 [ Caenorhabditis briggsae ]CAE7150939582177Hypothetical protein CBG18441 [ Caenorhabditis briggsae ]XP_001 . . .156555525PREDICTED: similar to beta-carotene dioxygenase [ Nasoniavitripennis ]XP_001 . . .125824371PREDICTED: similar to retinal pigment epithelium 65b [ Danio rerio ]CAF9163947209442unnamed protein product [ Tetraodon nigroviridis ]CAG0288147222516unnamed protein product [ Tetraodon nigroviridis ]CAG0648747224917unnamed protein product [ Tetraodon nigroviridis ]EDL95460149041619beta-carotene 9′,10′-dioxygenase 2 [ Rattus norvegicus ]YP_001 . . .154707125putative dioxygenase [ Coxiella burnetii Dugway 7E9-12]NP_65030724646669neither inactivation nor afterpotential B CG9347-PA [ Drosophilamelanogaster ]BAA945087593040DRPE65 [ Drosophila melanogaster ]ZP_019 . . .153206838dioxygenase, putative [ Coxiella burnetii ‘MSU Goat Q177’]AAH9216262132948Zgc: 110538 [ Danio rerio ]YP_4442808381486715,15′ beta carotene dioxygenase [ Salinibacter ruber DSM 13855]BAB3224812861637unnamed protein product [ Mus musculus ]EAW67192119587596beta-carotene dioxygenase 2, isoform CRA_d [ Homo sapiens ]XP_001 . . .114640354PREDICTED: hypothetical protein isoform 1 [ Pan troglodytes ]BAC0374721750237unnamed protein product [ Homo sapiens ]EAW67190119587594beta-carotene dioxygenase 2, isoform CRA_b [ Homo sapiens ]XP_001 . . .125774315GA21719-PA [ Drosophila pseudoobscura ]YP_001 . . .134096631lignostilbene-alpha/beta-dioxygenase [ Saccharopolyspora erythraeaNRRL 2338]EAW67191119587595beta-carotene dioxygenase 2, isoform CRA_c [ Homo sapiens ]XP_001 . . .149486496PREDICTED: similar to b,b-carotene-9,10-dioxygenase, partial[ Ornithorhynchus anatinus ]AAO9053129541592dioxygenase, putative [ Coxiella burnetii RSA 493]XP_001 . . .109129384PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1) [ Macaca mulatta ]CAJ53109109626642beta,beta-carotene 9′,10′-dioxygenase 2 [ Haloquadratum walsbyi DSM16790]XP_001 . . .109129778PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1), partial [ Macaca mulatta ]XP_001 . . .118109416PREDICTED: similar to beta-carotene 15,15-dioxygenase, partial[ Gallus gallus ]ABF70124102139989dioxygenase-related protein [ Musa balbisiana ]AAW5943557918684decreased apical dominance protein [ Petunia x hybrida ]EAY74583125526469hypothetical protein OsI_002430 [ Oryza sativa ( indica cultivar-group)]AAL6696118377622unknown protein [ Arabidopsis thaliana ]EAY74584125526470hypothetical protein OsI_002431 [ Oryza sativa ( indica cultivar-group)]BAC0559821902049putative dioxygenase [ Oryza sativa ( japonica cultivar-group)]AAW3359657116144Dad1/CCD8 [ Petunia x hybrida ]NP_001 . . .115439899Os01g0746400 [ Oryza sativa ( japonica cultivar-group)]EAY75798125527684hypothetical protein OsI_003645 [ Oryza sativa ( indica cultivar-group)]EAZ13518125572003hypothetical protein OsJ_003343 [ Oryza sativa ( japonica cultivar-group)]ABQ08577146160696beta-carotene 15,15′-monooxygenase 2 [ Oryzias latipes ]BAB6348515289786retinal pigment epithelium 65-like [ Oryza sativa ( japonica cultivar-group)]AAS6690645504725dioxygenase RAMOSUS1 [ Pisum sativum ]ZP_013 . . .95927318hypothetical protein CburR_01000925 [ Coxiella burnetii RSA 331]YP_658115110668304beta,beta-carotene 15,15′-monooxygenase; beta-carotene dioxygenase 1[ Haloquadratum walsbyi DSM 16790]CAL90971121495644torulene oxygenase [ Gibberella fujikuroi ]YP_13467755376826retinal pigment epithelial membrane protein [ Haloarcula marismortuiATCC 43049]CAL90970121495642torulene oxygenase [ Gibberella fujikuroi ]XP_38280146111487hypothetical protein FG02625.1 [ Gibberella zeae PH-1]XP_001 . . .149480289PREDICTED: similar to carotene-9,10-monooxygenase, partial[ Ornithorhynchus anatinus ]ABQ76053148508268beta,beta-carotene 9′,10′-dioxygenase 2 [uncultured haloarchaeon]YP_657779110667968beta,beta-carotene 9′,10′-dioxygenase 2 [ Haloquadratum walsbyi DSM16790]XP_001 . . .109149184PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1), partial [ Macaca mulatta ]AAP9257733086530Ab2-079 [ Rattus norvegicus ]ABN50352125662819carotenoid cleavage dioxygenase 1 [ Hypocrea jecorina ]EAL9373666853412dioxygenase, putative [ Aspergillus fumigatus Af293]XP_001 . . .125876361PREDICTED: hypothetical protein, partial [ Danio rerio ]XP_001 . . .119481741dioxygenase, putative [ Neosartorya fischeri NRRL 181]XP_001 . . .119494253retinal pigment epithelial membrane family protein [ Neosartoryafischeri NRRL 181]XP_95845285090512hypothetical protein [ Neurospora crassa OR74A]EDO64867157069539predicted protein [ Neurospora crassa OR74A]XP_001 . . .121716178dioxygenase, putative [ Aspergillus clavatus NRRL 1]CAL64769148353839putative carotene oxygenase [ Blakeslea trispora ]BAD7950556686283lignostilbene-alpha beta-dioxygenase [ Synechococcus elongatus PCC6301]ZP_016 . . .119509407Retinal pigment epithelial membrane protein [ Nodularia spumigenaCCY9414]BAE5688683766746unnamed protein product [ Aspergillus oryzae ]BAE5924783769110unnamed protein product [ Aspergillus oryzae ]ECC98172139038333hypothetical protein GOS_5249294 [marine metagenome]ZP_017 . . .126656631Beta-carotene 15,15′-dioxygenase [ Cyanothece sp. CCY0110]BAC9163035214261gll3689 [ Gloeobacter violaceus PCC 7421]EAT90277111069157hypothetical protein SNOG_02065 [ Phaeosphaeria nodorum SN15]CAB799987270228putative protein [ Arabidopsis thaliana ]CAL49287117557505putative carotene-dioxygenase [ Rhizopus oryzae ]XP_65930867522495hypothetical protein AN1704.2 [ Aspergillus nidulans FGSC A4]XP_001 . . .125824373PREDICTED: similar to retinal pigment epithelium 65b [ Danio rerio ]XP_001 . . .119185939hypothetical protein CIMG_03017 [ Coccidioides immitis RS]2BIWB66361521Chain B, Crystal Structure Of Apocarotenoid Cleavage OxygenaseFrom Synechocystis, Native EnzymeABA2086075701184Retinal pigment epithelial membrane protein [ Anabaena variabilisATCC 29413]XP_001 . . .116207620hypothetical protein CHGG_03103 [ Chaetomium globosum CBS148.51]XP_001 . . .145257182hypothetical protein An04g02710 [ Aspergillus niger ]BAB7598317133419lignostilbene-alpha,beta-dioxygenase [ Nostoc sp. PCC 7120]XP_50195850548975hypothetical protein [ Yarrowia lipolytica ]XP_001 . . .109129782PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1), partial [ Macaca mulatta ]ZP_016 . . .119484919Retinal pigment epithelial membrane protein [ Lyngbya sp. PCC 8106]ZP_017 . . .126656882Retinal pigment epithelial membrane protein [ Cyanothece sp.CCY0110]XP_001 . . .109149035PREDICTED: similar to Beta,beta-carotene 15,15-monooxygenase(Beta-carotene dioxygenase 1), partial [ Macaca mulatta ]CAL49288117557507putative carotene-dioxygenase [ Rhizopus oryzae ]ZP_001 . . .23130610COG3670: Lignostilbene-alpha,beta-dioxygenase and related enzymes[ Nostoc punctiforme PCC 73102]XP_36243339945792hypothetical protein MGG_08016 [ Magnaporthe grisea 70-15]XP_001 . . .115951205PREDICTED: hypothetical protein [ Strongylocentrotus purpuratus ]AAC128753033545lignostilbene-alpha,beta-dioxygenase [ Synechococcus sp. PCC 7942]XP_001 . . .154282379conserved hypothetical protein [ Ajellomyces capsulatus NAm1]ABG52331110167791Carotenoid oxygenase [ Trichodesmium erythraeum IMS101]ABC9926386554305putative lignostilbene-alpha,beta-dioxygenase [ Synechococcus sp. JA-3-3Ab]NP_93151137528166hypothetical protein plu4336 [ Photorhabdus luminescens subsp.laumondii TTO1]EDD33453143171893hypothetical protein GOS_1320815 [marine metagenome]XP_001 . . .115387251predicted protein [ Aspergillus terreus NIH2624]YP_885943118467371lignostilbene-alpha,beta-dioxygenase [ Mycobacterium smegmatis str.MC2 155] TABLE 68Examples of beta-carotene retinol dehydrogenase polypeptides.ACCESSIONGIPROTEIN DESCRIPTIONAAX3367060678607epithelial retinol dehydrogenase [ Mus musculus ]BAC3411026340896unnamed protein product [ Mus musculus ]XP_001 . . .149730699PREDICTED: similar to short-chain dehydrogenase/reductaseRETSDR8 [ Equus caballus ]XP_54551374004823PREDICTED: similar to NADP-dependent retinoldehydrogenase/reductase [ Canis familiaris ]Q8HYR675064969Dehydrogenase/reductase SDR family member 9 precursor (3-alphahydroxysteroid dehydrogenase) (3alpha-HSD) (Short-chaindehydrogenase/reductase retSDR8)XP_001 . . .114581559PREDICTED: NADP-dependent retinol dehydrogenase/reductaseisoform 3 [ Pan troglodytes ]XP_001 . . .109099963PREDICTED: similar to NADP-dependent retinoldehydrogenase/reductase isoform 3 [ Macaca mulatta ]AAL3703717224600short-chain dehydrogenase/reductase RETSDR8 [ Homo sapiens ]AAD324584894382retinol dehydrogenase homolog [ Homo sapiens ]XP_001 . . .126326289PREDICTED: similar to short-chain dehydrogenase/reductaseRETSDR8 [ Monodelphis domestica ]XP_001 . . .149639643PREDICTED: similar to short-chain dehydrogenase/reductaseRETSDR8 [ Ornithorhynchus anatinus ]XP_001 . . .114581568PREDICTED: NADP-dependent retinol dehydrogenase/reductaseisoform 1 [ Pan troglodytes ]AAF827489082139retinol dehydrogenase homolog isoform-1 [ Homo sapiens ]XP_001 . . .109099969PREDICTED: similar to NADP-dependent retinoldehydrogenase/reductase isoform 1 [ Macaca mulatta ]AAY2430662988919unknown [ Homo sapiens ]XP_422015118093666PREDICTED: similar to short-chain dehydrogenase/reductaseRETSDR8 [ Gallus gallus ]XP_001 . . .114581566PREDICTED: NADP-dependent retinol dehydrogenase/reductaseisoform 2 [ Pan troglodytes ]NP_001 . . .147905288NADP-dependent retinol dehydrogenase/reductase [ Xenopus laevis ]AAH6730445501367Dehydrogenase/reductase (SDR family) member 9 [ Xenopus tropicalis ]EDM16447149066574rCG60176, isoform CRA_a [ Rattus norvegicus ]AAH6200038303814Rdh2 protein [ Rattus norvegicus ]AAC523161072046retinol dehydrogenase type IINP_001 . . .148227174hypothetical protein LOC398882 [ Xenopus laevis ]NP_0330666677697retinol dehydrogenase 16 [ Mus musculus ]NP_001 . . .147900576hypothetical protein LOC432178 [ Xenopus laevis ]NP_69477323680945retinol dehydrogenase 9 [ Mus musculus ]NP_00371619743808hydroxysteroid (17-beta) dehydrogenase 6 [ Homo sapiens ]BAE2101774205129unnamed protein product [ Mus musculus ]EDL24523148692576mCG140848 [ Mus musculus ]AAL1486022651436cis-retinol/3alpha hydroxysterol short-chain dehydrogenase-like protein[ Mus musculus ]P550061710631Retinol dehydrogenase 7 (Retinol dehydrogenase type III) (RODH III)AAH8289652354822LOC494781 protein [ Xenopus laevis ]XP_001 . . .109097334PREDICTED: similar to 3-hydroxysteroid epimerase [ Macaca mulatta ]AAI35515134023801LOC100124842 protein [ Xenopus tropicalis ]P501691710629Retinol dehydrogenase 3 (Retinol dehydrogenase type I) (RODH I)BAC9830437360649cis-retinol/androgen dehydrogenase type 3 [ Mus musculus ]NP_66339921703846cis-retinol/3alpha hydroxysterol short-chain dehydrogenase-like [ Musmusculus ]AAB07997841197retinol dehydrogenase type IXP_001 . . .126343946PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 [ Monodelphis domestica ]NP_77542727545384hydroxysteroid (17-beta) dehydrogenase 6 [ Rattus norvegicus ]EDL24527148692580mCG134493 [ Mus musculus ]XP_53164173968454PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 isoform 1 [ Canis familiaris ]AAH2460319354049Retinol dehydrogenase 7 [ Mus musculus ]AAL0213422074192retinol dehydrogenase similar protein 2 [ Mus musculus ]NP_53668420147789retinol dehydrogenase 1 (all trans) [ Mus musculus ]AAH8810456789874Hydroxysteroid (17-beta) dehydrogenase 6 [ Rattus norvegicus ]EDL24532148692585hydroxysteroid (17-beta) dehydrogenase 9, isoform CRA_a [ Musmusculus ]ABG81445110665598microsomal NAD+-dependent retinol dehydrogenase 4 [ Bos taurus ]EDL24533148692586hydroxysteroid (17-beta) dehydrogenase 9, isoform CRA_b [ Musmusculus ]XP_53823973968448PREDICTED: similar to 3-hydroxysteroid epimerase isoform 3 [ Canisfamiliaris ]CAJ8133389272084novel retinol dehydrogenase protein [ Xenopus tropicalis ]AAH4669428302191Rodh-A-prov protein [ Xenopus laevis ]XP_001 . . .149715148PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 [ Equus caballus ]XP_001 . . .109097338PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 isoform 2 [ Macaca mulatta ]XP_001 . . .109097336PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 isoform 3 [ Macaca mulatta ]XP_85818273968456PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 isoform 2 [ Canis familiaris ]AAI0262774354657Similar to 3-hydroxysteroid epimerase [ Bos taurus ]XP_85805973968446PREDICTED: similar to 3-hydroxysteroid epimerase isoform 4 [ Canisfamiliaris ]AAC399223372592sterol/retinol dehydrogenase [ Homo sapiens ]AAY4482366354281retinol dehydrogenase 5 [ Danio rerio ]XP_52260455639443PREDICTED: retinol dehydrogenase 16 [ Pan troglodytes ]AAH9715166911361Retinol dehydrogenase 5 (11-cis/9-cis) [ Danio rerio ]CAK0504994732559novel protein similar to vertebrate retinol dehydrogenase family [ Daniorerio ]NP_9900444538264911-cis retinol dehydrogenase [ Gallus gallus ]EAW96968119617374retinol dehydrogenase 16 (all-trans and 13-cis) [ Homo sapiens ]NP_001 . . .148233310hypothetical protein LOC398939 [ Xenopus laevis ]CAG0495947218630unnamed protein product [ Tetraodon nigroviridis ]AAH8801456789076Hypothetical LOC496749 [ Xenopus tropicalis ]AAI23192114107846Rdh9 protein [ Xenopus laevis ]AAC729233859946retinol dehydrogenase [ Homo sapiens ]AAF827479082137retinol dehydrogenase homolog isoform-2 [ Homo sapiens ]AAH7545549522586MGC89248 protein [ Xenopus tropicalis ]AAH5961437590384Retinol dehydrogenase 1, like [ Danio rerio ]AAB882522661211oxidative 3 alpha hydroxysteroid dehydrogenase [ Homo sapiens ]EDL24633148692686retinol dehydrogenase 5, isoform CRA_b [ Mus musculus ]BAE2243574149341unnamed protein product [ Mus musculus ]XP_53822073968269PREDICTED: similar to 11-cis retinol dehydrogenase (11-cis RDH)[ Canis familiaris ]NP_001 . . .147899633MGC84134 protein [ Xenopus laevis ]XP_001 . . .109097121PREDICTED: retinol dehydrogenase 5 (11-cis and 9-cis) [ Macacamulatta ]NP_001 . . .147905378MGC84099 protein [ Xenopus laevis ]CAF9245147210426unnamed protein product [ Tetraodon nigroviridis ]XP_52242955638373PREDICTED: similar to 11-cis retinol dehydrogenase isoform 2 [ Pantroglodytes ]AAH8852956788840Hypothetical LOC496830 [ Xenopus tropicalis ]NP_00289650726952retinol dehydrogenase 5 (11-cis and 9-cis) [ Homo sapiens ]CAA5771566317111-cis retinol dehydrogenase [ Bos taurus ]AAH2829820271410Retinol dehydrogenase 5 (11-cis/9-cis) [ Homo sapiens ]NP_001 . . .148230094hypothetical protein LOC399015 [ Xenopus laevis ]AAA80694105453111-cis-retinol dehydrogenaseNP_93233537620196retinol dehydrogenase 1 [ Danio rerio ]XP_53824073968424PREDICTED: similar to orphan short-chain dehydrogenase/reductase[ Canis familiaris ]AAI34659134024746MGC151815 protein [ Bos taurus ]AAH6482040673988Orphan short chain dehydrogenase/reductase [ Mus musculus ]EDL24531148692584orphan short chain dehydrogenase/reductase [ Mus musculus ]AAB9366819169359-cis-retinol specific dehydrogenase [ Homo sapiens ]XP_001 . . .149715290PREDICTED: hypothetical protein [ Equus caballus ]XP_001 . . .109482100PREDICTED: similar to retinol dehydrogenase similar protein [ Rattusnorvegicus ]EAW96967119617373orphan short-chain dehydrogenase/reductase [ Homo sapiens ]XP_522439114644207PREDICTED: orphan short-chain dehydrogenase/reductase [ Pantroglodytes ]EDL24528148692581mCG134494, isoform CRA_a [ Mus musculus ]ABQ09278146186452retinol dehydrogenase 1 [ Oryzias latipes ]ABQ09279146186454retinol dehydrogenase 5 [ Oryzias latipes ]XP_001 . . .109097340PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 isoform 1 [ Macaca mulatta ]EDM16444149066571orphan short chain dehydrogenase/reductase [ Rattus norvegicus ]AAG4484912006418microsomal retinol dehydrogenase [ Branchiostoma lanceolatum ]BAE8876090078160unnamed protein product [ Macaca fascicularis ]AAG4484712006414microsomal retinol dehydrogenase 1 [ Branchiostoma floridae ]XP_782726115665382PREDICTED: similar to retinol dehydrogenase type 1, partial[ Strongylocentrotus purpuratus ]XP_001 . . .115939186PREDICTED: similar to retinol dehydrogenase type 1[ Strongylocentrotus purpuratus ]XP_001 . . .118093664PREDICTED: similar to MGC83505 protein [ Gallus gallus ]XP_781379115654644PREDICTED: similar to retinol dehydrogenase type 1, partial[ Strongylocentrotus purpuratus ]XP_001 . . .115958895PREDICTED: similar to retinol dehydrogenase type 1[ Strongylocentrotus purpuratus ]AAG4484812006416microsomal retinol dehydrogenase 2 [ Branchiostoma floridae ]XP_001 . . .115960451PREDICTED: similar to retinol dehydrogenase type III[ Strongylocentrotus purpuratus ]EDL84786149029615rCG42422, isoform CRA_a [ Rattus norvegicus ]AAL1486122651438cis-retinol/3alpha hydroxysterol short-chain dehydrogenase-like proteinisoform [ Mus musculus ]XP_001 . . .156386264predicted protein [ Nematostella vectensis ]XP_001 . . .156389613predicted protein [ Nematostella vectensis ]XP_001 . . .156368581predicted protein [ Nematostella vectensis ]XP_001 . . .156362183predicted protein [ Nematostella vectensis ]BAC2814226328807unnamed protein product [ Mus musculus ]XP_001 . . .156367012predicted protein [ Nematostella vectensis ]XP_001 . . .156367010predicted protein [ Nematostella vectensis ]CAG1452747203967unnamed protein product [ Tetraodon nigroviridis ]XP_001 . . .156367016predicted protein [ Nematostella vectensis ]XP_001 . . .156401057predicted protein [ Nematostella vectensis ]AAB698842384782Dehydrogenases, short chain protein 16 [ Caenorhabditis elegans ]XP_001 . . .156367014predicted protein [ Nematostella vectensis ]XP_001 . . .156367008predicted protein [ Nematostella vectensis ]NP_87181532563809DeHydrogenases, Short chain family member (dhs-2) [ Caenorhabditiselegans ]NP_49157517507613DeHydrogenases, Short chain family member (dhs-2) [ Caenorhabditiselegans ]NP_505941115534660DeHydrogenases, Short chain family member (dhs-20) [ Caenorhabditiselegans ]CAE7488639583813Hypothetical protein CBG22749 [ Caenorhabditis briggsae ]XP_001 . . .156408325predicted protein [ Nematostella vectensis ]XP_001 . . .126343453PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1[ Monodelphis domestica ]CAE6453339593064Hypothetical protein CBG09275 [ Caenorhabditis briggsae ]XP_001 . . .149571441PREDICTED: similar to retinol dehydrogenase similar protein, partial[ Ornithorhynchus anatinus ]NP_95501749227085truncated cis-retinol/3alpha-hydroxysterol short-chain dehydrogenase[ Mus musculus ]XP_001 . . .156363786predicted protein [ Nematostella vectensis ]XP_001 . . .109097342PREDICTED: similar to microsomal NAD+-dependent retinoldehydrogenase 4 [ Macaca mulatta ]NP_001 . . .147899736hypothetical protein LOC100037356 [ Danio rerio ]XP_001 . . .156366980predicted protein [ Nematostella vectensis ]XP_001 . . .125853068PREDICTED: hypothetical protein [ Danio rerio ]AAH11964150804293-hydroxybutyrate dehydrogenase, type 1 [ Homo sapiens ]XP_345771109480152PREDICTED: similar to retinol dehydrogenase 5 [ Rattus norvegicus ]XP_001 . . .149731507PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1[ Equus caballus ]NP_976059446801363-hydroxybutyrate dehydrogenase precursor [ Homo sapiens ]XP_001 . . .149633623PREDICTED: similar to 3-hydroxybutyrate dehydrogenase, type 1[ Ornithorhynchus anatinus ]AAH8959758476255BC089597 protein [ Mus musculus ]XP_001 . . .114591350PREDICTED: 3-hydroxybutyrate dehydrogenase isoform 1 [ Pantroglodytes ]XP_516981114591348PREDICTED: 3-hydroxybutyrate dehydrogenase isoform 2 [ Pantroglodytes ]XP_001 . . .156405501predicted protein [ Nematostella vectensis ]CAG0426747223406unnamed protein product [ Tetraodon nigroviridis ]XP_54516074002972PREDICTED: similar to 3-hydroxybutyrate dehydrogenase precursor[ Canis familiaris ]AAI03052735873653-hydroxybutyrate dehydrogenase, type 1 [ Bos taurus ]BAF3526011626759511beta-hydroxysteroid dehydrogenase short form [ Anguilla japonica ]AAH6561341350974Hydroxysteroid 11-beta dehydrogenase 2 [ Danio rerio ]AAB59684203921D-beta-hydroxybutyrate dehydrogenaseBAE2707674226863unnamed protein product [ Mus musculus ]NP_446447557428133-hydroxybutyrate dehydrogenase, type 1 [ Rattus norvegicus ]P2914768837285D-beta-hydroxybutyrate dehydrogenase, mitochondrial precursor(BDH) (3-hydroxybutyrate dehydrogenase)EDK977501486653343-hydroxybutyrate dehydrogenase, type 1 [ Mus musculus ]CAE7533139592111Hypothetical protein CBG23309 [ Caenorhabditis briggsae ]BAE2352374206030unnamed protein product [ Mus musculus ]BAC3645326345604unnamed protein product [ Mus musculus ]ABH0293711093188017-beta hydroxysteroid dehydrogenase 2 [ Bos taurus ]NP_50941517568189F55E10.6 [ Caenorhabditis elegans ]XP_54681073957269PREDICTED: similar to hydroxysteroid (17-beta) dehydrogenase 2[ Canis familiaris ]XP_001 . . .115925077PREDICTED: similar to retinol dehydrogenase type 1[ Strongylocentrotus purpuratus ]AAA58352177198(R)-3-hydroxybutyrate dehydrogenaseXP_42270350752249PREDICTED: hypothetical protein [ Gallus gallus ]XP_001 . . .149640222PREDICTED: similar to 17-beta hydroxysteroid dehydrogenase 2[ Ornithorhynchus anatinus ]XP_511130114663836PREDICTED: hydroxysteroid (17-beta) dehydrogenase 2 [ Pantroglodytes ]P37059544152Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (Microsomal 17-beta-hydroxysteroid dehydrogenase) (20 alpha-hydroxysteroiddehydrogenase) (20-alpha-HSD) (E2DH)AAV3855654696368hydroxysteroid (17-beta) dehydrogenase 2 [synthetic construct]AAH9044860649586Hsd17b2 protein [ Danio rerio ]XP_001 . . .118087716PREDICTED: hypothetical protein [ Gallus gallus ]NP_001 . . .93277072hydroxysteroid (17-beta) dehydrogenase 2 [ Danio rerio ]P516582507561Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (17-beta-hydroxysteroid dehydrogenase 2)BAC767093084423211-beta-hydroxysteroid dehydrogenase [ Oncorhynchus mykiss ]AAY845676797519917-beta hydroxysteroid dehydrogenase 2 [ Macaca fascicularis ]BAD9672162897563hydroxysteroid (17-beta) dehydrogenase 2 variant [ Homo sapiens ]XP_414168118096516PREDICTED: similar to 17 beta hydroxysteroid dehydrogenase type 2[ Gallus gallus ]CAE6693339589698Hypothetical protein CBG12325 [ Caenorhabditis briggsae ]AAK9585722074155retinol dehydrogenase similar protein [ Rattus norvegicus ]AAH7414449257832MGC81883 protein [ Xenopus laevis ]XP_001 . . .125850087PREDICTED: hypothetical protein [ Danio rerio ]AAH9018158701977Zgc: 113142 [ Danio rerio ]AAA8700775557411-beta-hydroxylsteroid dehydrogenase type 2Q627303334165Estradiol 17-beta-dehydrogenase 2 (17-beta-HSD 2) (17-beta-hydroxysteroid dehydrogenase 2)XP_001 . . .115956172PREDICTED: similar to Retinol dehydrogenase 3 (Retinoldehydrogenase type I) (RODH I) [Strongylocentrotus purpuratus]CAA64982120009717-beta-hydroxysteroid dehydrogenase type II [ Mus musculus ]EDL11587148679640hydroxysteroid (17-beta) dehydrogenase 2 [ Mus musculus ]EDL92656149038296hydroxysteroid (17-beta) dehydrogenase 2 [ Rattus norvegicus ]XP_001 . . .149626583PREDICTED: similar to 11 beta-hydroxysteroid dehydrogenase type 2[ Ornithorhynchus anatinus ]XP_001 . . .109482098PREDICTED: similar to Retinol dehydrogenase 2 (Retinoldehydrogenase type II) (RODH II) (29 k-protein) [ Rattus norvegicus ]XP_001 . . .109128927PREDICTED: similar to Corticosteroid 11-beta-dehydrogenaseisozyme 2 (11-DH2) (11-beta-hydroxysteroid dehydrogenase type 2)(11-beta-HSD2) (NAD-dependent 11-beta-hydroxysteroiddehydrogenase) [ Macaca mulatta ] TABLE 69Genes Comprising the SAGA Complex.S. cerevisiae geneY lipolytica geneSPT3YALI0E21417gSPT7none identifiedSPT8YALI0E23804gSPT20YALI0C04070gADA2YALI0F14443gADA3none identifiedGCN5YALI0E02772gADA1none identifiedTRA1YALI0C02057g EQUIVALENTS Those skilled in the art will recognize, or be able to ascertain using no more than routine experimentation, many equivalents to the specific embodiments of the invention described herein. The scope of the present invention is not intended to be limited to the above Description, but rather is as set forth in the following claims:","lang":"en","source":"USPTO_FULLTEXT","data_format":"ORIGINAL"}},"description_lang":["en"],"has_description":true,"has_docdb":true,"has_inpadoc":true,"has_full_text":true,"biblio_lang":"en"},"jurisdiction":"US","collections":[],"usersTags":[],"lensId":"004-388-887-583-285","publicationKey":"US_8691555_B2","displayKey":"US 8691555 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fungi","documentTitle":"Production of carotenoids in oleaginous yeast and fungi"},"claims":{"source":"xml_claims","claims":[{"lines":["An engineered Y. lipolytica strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one retinologenic modification selected from the group consisting of increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide, increased expression or activity of a retinol dehydrogenase polypeptide, and combinations thereof;\n
wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and\n
wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight."],"number":1,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the strain does not naturally produce the at least one retinolic compound."],"number":2,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, further comprising at least one oleaginic modification."],"number":3,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 3, wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide, selected from the group consisting of acetyl-CoA carboxylase polypeptide, pyruvate decarboxylase polypeptide, isocitrate dehydrogenase polypeptide, ATP-citrate lyase polypeptide, malic enzyme polypeptide, AMP deaminase polypeptide, malate dehydrogenase polypeptide, glucose-6-phosphate dehydrogenase polypeptide, 6-phosphogluconate dehydrogenase polypeptide, fructose 1,6 bisphosphatase polypeptide, NADH kinase polypeptide, transhydrogenase polypeptide, acyl-CoA:diacylglycerol acyltransferase polypeptide, phospholipid:diacylglycerol acyltransferase polypeptide, acyl-CoA:cholesterol acyltransferase polypeptide, triglyceride lipase polypeptide, acyl-coenzyme A oxidase polypeptide and combinations thereof."],"number":4,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 3, wherein the at least one oleaginic modification increases or decreases expression or activity of at least one oleaginic polypeptide selected from the group consisting of a polypeptide in any one of Tables 1 through 6 or 31-47."],"number":5,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the at least one retinologenic modification confers to the engineered strain the ability to produce the at least one retinolic compound to a level at least about 1% of its dry cell weight."],"number":6,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the at least one retinologenic modification confers to the engineered strain the ability to produce at least one retinolic compound which a non-engineered strain does not naturally produce."],"number":7,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the at least one retinologenic modification increases expression or activity of beta-carotene 15,15′-monoxygenase or beta carotene retinol dehydrogenase."],"number":8,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the beta-carotene 15,15′-monooxygenase polypeptide is selected from the group consisting of a polypeptide in Table 67."],"number":9,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the at least one retinologenic modification further comprises decreasing the expression or activity of one or more components of the SAGA histone acetyltransferase complex."],"number":10,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 10, wherein the at least one retinologenic modification comprises disruption of the endogenous SPT8 gene."],"number":11,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 10 wherein the one or more components of the SAGA histone acetyltransferase complex are selected from the polypeptides listed in Table 69."],"number":12,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the retinologenic modification further comprises altering the expression or activity of one or more carotenoid biosynthesis polypeptides."],"number":13,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 13, wherein the one or more carotenoid biosynthesis polypeptides are selected from the group consisting of phytoene synthase, phytoene dehydrogenase, lycopene cyclase, carotene ketolase, carotene hydroxylase, astaxanthin synthase, carotenoid epsilon hydroxylase, lycopene cyclase, carotenoid glucosyltransferase, acyl CoA:diacyglycerol acyltransferase, geranylgeranylpyrophosphate synthase, and truncated HMG-CoA reductase."],"number":14,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 13, wherein the one or more carotenoid biosynthesis polypeptides are selected from the sequences provided in Tables 17a-25."],"number":15,"annotation":false,"claim":true,"title":false},{"lines":["A method of producing a retinolic compound, the method comprising steps of:\n
a. cultivating the fungus of claim 1 under conditions that allow production of the retinolic compound;\n
b. and isolating the produced retinolic compound."],"number":16,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the at least one retinologenic modification comprises introduction of a gene encoding a heterologous beta-carotene 15,15′-monooxygenase polypeptide, a heterologous retinol dehydrogenase polypeptide, or combinations thereof."],"number":17,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 1, wherein the retinol dehydrogenase polypeptide is selected from the group consisting of a polypeptide in Table 68."],"number":18,"annotation":false,"claim":true,"title":false},{"lines":["An engineered Y. lipolytica strain that produces at least one retinolic compound selected from the group consisting of retinol, retinal, retinoic acid, retinyl palmitate and combinations thereof, the strain comprising at least one genetic modification selected from the group consisting of:\n
increased expression or activity of a beta-carotene 15,15′-monooxygenase polypeptide;\n
increased expression or activity of a retinol dehydrogenase polypeptide;\n
increased expression or activity of phytoene synthase;\n
increased expression or activity of lycopene cyclase;\n
increased expression or activity of phytoene dehydrogenease;\n
increased expression or activity of geranylgeranylpyrophosphate synthase;\n
increased expression or activity of truncated HMG-CoA reductase; and\n
combinations thereof;\n
wherein the engineered strain can accumulate lipid to at least about 20% of its dry cell weight; and\n
wherein as a result of genetic engineering, the engineered strain produces the at least one retinolic compound to a level at least about 1% of its dry cell weight."],"number":19,"annotation":false,"claim":true,"title":false},{"lines":["The engineered Y. lipolytica strain of claim 19, wherein the genetic modification comprises introduction of one or more heterologous genes encoding metabolic enzymes selected from the group consisting of: beta-carotene 15,15′-monooxygenase, phytoene synthase, lycopene cyclase, phytoene dehydrogenease, geranylgeranylpyrophosphate synthase, truncated HMG-CoA reductase, and combinations thereof."],"number":20,"annotation":false,"claim":true,"title":false}]}},"filters":{"npl":[],"notNpl":[],"applicant":[],"notApplicant":[],"inventor":[],"notInventor":[],"owner":[],"notOwner":[],"tags":[],"dates":[],"types":[],"notTypes":[],"j":[],"notJ":[],"fj":[],"notFj":[],"classIpcr":[],"notClassIpcr":[],"classNat":[],"notClassNat":[],"classCpc":[],"notClassCpc":[],"so":[],"notSo":[],"sat":[]},"sequenceFilters":{"s":"SEQIDNO","d":"ASCENDING","p":0,"n":10,"sp":[],"si":[],"len":[],"t":[],"loc":[]}}