cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  72 LQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSDPKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFH 151
Cdd:cd20678     1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462508187 152 YDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRPSDP 216
Cdd:cd20678    81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNS 145

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  72 LQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSDPKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFH 151
Cdd:cd20678     1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462508187 152 YDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRPSDP 216
Cdd:cd20678    81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNS 145

cytokinin trans-hydroxylase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  88 YWiWGGKVRVQLYDPDYMKVIL-------GRSDPKSHGSYKFlaprIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVG 160
Cdd:PLN02290   99 YW-NGTEPRLCLTETELIKELLtkyntvtGKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAG 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462508187 161 LMADSVRVMLDKWEELLGQ-DSPLEVFQHVSLMTLDTIMKSAF 202
Cdd:PLN02290  174 HMVECTKQMLQSLQKAVESgQTEVEIGEYMTRLTADIISRTEF 216

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  72 LQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSDPKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFH 151
Cdd:cd20678     1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462508187 152 YDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRPSDP 216
Cdd:cd20678    81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNS 145

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  72 LQRIQERVKTFPSACPYWIWGGKVRVQLYDPDYMKVILGRSD---PKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTP 148
Cdd:cd20679     1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAavaPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462508187 149 AFHYDILKPYVGLMADSVRVMLDKWEELLGQDSP-LEVFQHVSLMTLDTIMKSAFSHQGSIQvDRPSD 215
Cdd:cd20679    81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSArLDMFEHISLMTLDSLQKCVFSFDSNCQ-EKPSE 147

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  89 WIwGGKVRVQLYDPDYMKVILGRSD--PKSHGsYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20628     7 WI-GPKPYVVVTNPEDIEVILSSSKliTKSFL-YDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENS 84

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462508187 167 RVMLDKWEELLGQDSpLEVFQHVSLMTLDTIMKSAF 202
Cdd:cd20628    85 KILVEKLKKKAGGGE-FDIFPYISLCTLDIICETAM 119

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  90 IW-GGKVRVQLYDPDYMKVILGRSD--PKSHgSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20660     6 IWlGPKPIVVLYSAETVEVILSSSKhiDKSF-EYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQS 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462508187 167 RVMLDKWEELLGqDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQVDRPSD 215
Cdd:cd20660    85 EILVKKLKKEVG-KEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSE 132

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  90 IWGGKVR-VQLYDPDYMKVILGRSD--PKSHgSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20680    17 LWIGPVPfVILYHAENVEVILSSSKhiDKSY-LYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQS 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462508187 167 RVMLDKWEELLGQDsPLEVFQHVSLMTLDTIMKSA 201
Cdd:cd20680    96 NILVEKLEKHVDGE-AFNCFFDITLCALDIICETA 129

cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of Mycobacterium tuberculosis cytochrome P450 132 (CYP132) and similar proteins. The function of CYP132 is as yet unknown. CYP132 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187 101 DPDYMKVIL---GRSDPKShGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEElL 177
Cdd:cd20620    18 HPDHIQHVLvtnARNYVKG-GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEA-G 95

                          90       100
                  ....*....|....*....|....*.
gi 2462508187 178 GQDSPLEVFQHVSLMTLDTIMKSAFS 203
Cdd:cd20620    96 ARRGPVDVHAEMMRLTLRIVAKTLFG 121

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  88 YWIwGGKVRVQLYDPDYMKVILgrSDPKSHGSYKFLAPRI----GYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd20641    17 YWQ-GTTPRICISDHELAKQVL--SDKFGFFGKSKARPEIlklsGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462508187 164 DSVRVMLDKWEELLGQDSPLEVFQHVSL----MTLDTIMKSAF--SHQGSIQV 210
Cdd:cd20641    94 DCTERMFQEWRKQRNNSETERIEVEVSRefqdLTADIIATTAFgsSYAEGIEV 146

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  91 WGGKVRVQLYDPDYMKVILGRSD---PKSHGSYKFLAPRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11069    10 LFGSERLLVTDPKALKHILVTNSydfEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAE 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508187 168 VMLDKWEELL----GQDSPLEVFQHVSLMTLDTIMKSAFSHQ-GSIQvdRPSDPTEE 219
Cdd:cd11069    90 ELVDKLEEEIeesgDESISIDVLEWLSRATLDIIGLAGFGYDfDSLE--NPDNELAE 144

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  87 PYWIWGGKVRVqLYDPDYMKVILGRSDPKSHGSYKFLA---PRIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd00302     5 RVRLGGGPVVV-VSDPELVREVLRDPRDFSSDAGPGLPalgDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIR 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462508187 164 DSVRVMLDKWEELLGQDspLEVFQHVSLMTLDTIMKSAFS 203
Cdd:cd00302    84 EIARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGG 121

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  88 YWIWGgKVRVQLYDPDYMKVILGRSD-PKSHGSYKFLA----PR-IGYGLL-LLNGQTWFQHRRMLTPAFHYDILKpyvG 160
Cdd:cd20613    17 FWILH-RPIVVVSDPEAVKEVLITLNlPKPPRVYSRLAflfgERfLGNGLVtEVDHEKWKKRRAILNPAFHRKYLK---N 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462508187 161 LM------ADsvrVMLDKWEELlgQDSPLEV--FQHVSLMTLDTIMKSAFS 203
Cdd:cd20613    93 LMdefnesAD---LLVEKLSKK--ADGKTEVnmLDEFNRVTLDVIAKVAFG 138

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187 130 GLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQGSIQ 209
Cdd:cd11055    51 SLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQ 130

                  ....*
gi 2462508187 210 VDRPS 214
Cdd:cd11055   131 NNPDD 135

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187 115 KSHGSYKFLAPR--IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLM 192
Cdd:COG2124    65 SDGGLPEVLRPLplLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAA----RGPVDLVEEFARP 140

                          90
                  ....*....|
gi 2462508187 193 TLDTIMKSAF 202
Cdd:COG2124   141 LPVIVICELL 150

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462508187 127 IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllGQdsPLEVFQHVSLMTLDTIMKSAFS 203
Cdd:cd11049    58 LGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRP--GR--VVDVDAEMHRLTLRVVARTLFS 130

unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  86 CPYWIW-GGKVRVQLYDPDYMKVILgRSDPKSHGSYKFLAPRI----GYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVG 160
Cdd:cd11083     2 SAYRFRlGRQPVLVISDPELIREVL-RRRPDEFRRISSLESVFremgINGVFSAEGDAWRRQRRLVMPAFSPKHLRYFFP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462508187 161 LMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQ 205
Cdd:cd11083    81 TLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYD 125

carotene beta-ring hydroxylase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462508187  91 WGGKVRVQLYDPDYMKVILgRSDPKSHgSYKFLAP----RIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:PLN02738  172 FGPKSFLIVSDPSIAKHIL-RDNSKAY-SKGILAEilefVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQAS 249

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462508187 167 RVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKSAFSHQ 205
Cdd:PLN02738  250 DRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYD 288