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 1711057505  18 LEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGggted 97
Cdd:cd11053   273 PEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG----- 347

                          90
                  ....*....|...
gi 1711057505  98 RR---YTYIPFGG 107
Cdd:cd11053   348 RKpspYEYLPFGG 360

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This 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 1711057505  18 LEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGggted 97
Cdd:cd11053   273 PEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG----- 347

                          90
                  ....*....|...
gi 1711057505  98 RR---YTYIPFGG 107
Cdd:cd11053   348 RKpspYEYLPFGG 360

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711057505  11 RRDSPSTLEDLRRLPYLDATLNETLRTLPPSST-VTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPER 89
Cdd:pfam00067 307 GDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPER 386

                          90
                  ....*....|....*...
gi 1711057505  90 FLGG-GTEDRRYTYIPFG 106
Cdd:pfam00067 387 FLDEnGKFRKSFAFLPFG 404

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This 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 1711057505  18 LEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGggted 97
Cdd:cd11053   273 PEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG----- 347

                          90
                  ....*....|...
gi 1711057505  98 RR---YTYIPFGG 107
Cdd:cd11053   348 RKpspYEYLPFGG 360

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 1711057505  13 DSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQK-AWGLIAePRMVHGWERLYPDPGHFDPERFL 91
Cdd:cd20628   278 DRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKgTTVVIS-IYALHRNPEYFPDPEKFDPDRFL 356

                          90
                  ....*....|....*..
gi 1711057505  92 GGGTEDR-RYTYIPFGG 107
Cdd:cd20628   357 PENSAKRhPYAYIPFSA 373

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 1711057505  17 TLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGtE 96
Cdd:cd00302   251 TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPER-E 329

                          90
                  ....*....|.
gi 1711057505  97 DRRYTYIPFGG 107
Cdd:cd00302   330 EPRYAHLPFGA 340

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This 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 1711057505   7 KRQNRRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFD 86
Cdd:cd11043   255 AKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFN 334

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1711057505  87 PERFLGGGtEDRRYTYIPFGG--------ELPILQASIDLIRLQTR 124
Cdd:cd11043   335 PWRWEGKG-KGVPYTFLPFGGgprlcpgaELAKLEILVFLHHLVTR 379

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-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 1711057505  17 TLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTllqkawGLIAEPRM--------VHGWERLYPDPGHFDPE 88
Cdd:cd11056   282 TYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGT------DVVIEKGTpviipvyaLHHDPKYYPEPEKFDPE 355

                          90
                  ....*....|....*....
gi 1711057505  89 RFLGGGTEDRR-YTYIPFG 106
Cdd:cd11056   356 RFSPENKKKRHpYTYLPFG 374

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 1711057505  13 DSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLG 92
Cdd:cd20660   281 DRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLP 360

                          90
                  ....*....|....
gi 1711057505  93 GGTEDRR-YTYIPF 105
Cdd:cd20660   361 ENSAGRHpYAYIPF 374

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 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 1711057505  16 STLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGT 95
Cdd:cd20636   284 LSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVERE 363

                          90
                  ....*....|....
gi 1711057505  96 EDR--RYTYIPFGG 107
Cdd:cd20636   364 ESKsgRFNYIPFGG 377

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. 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. 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 CYP4B_4F-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 1711057505  19 EDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGTEDR 98
Cdd:cd20659   281 DDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKR 360

                  ....*...
gi 1711057505  99 R-YTYIPF 105
Cdd:cd20659   361 DpFAFIPF 368

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-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 1711057505  12 RDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKawG-LIAEPRMVHGW-ERLYPDPGHFDPER 89
Cdd:cd11054   278 DGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPK--GtLVVLSNYVMGRdEEYFPDPEEFIPER 355

                          90       100
                  ....*....|....*....|
gi 1711057505  90 FLGGGTEDRR---YTYIPFG 106
Cdd:cd11054   356 WLRDDSENKNihpFASLPFG 375

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This 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 1711057505  11 RRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGT--LLQKAWGLIAEPRMVHGWERLYPDPGHFDPE 88
Cdd:cd11042   259 DGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGgyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPE 338

                          90       100
                  ....*....|....*....|..
gi 1711057505  89 RFLGGGTEDR---RYTYIPFGG 107
Cdd:cd11042   339 RFLKGRAEDSkggKFAYLPFGA 360

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 1711057505  11 RRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERF 90
Cdd:cd20680   290 KSDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERF 369

                          90
                  ....*....|....*.
gi 1711057505  91 LGGGTEDRR-YTYIPF 105
Cdd:cd20680   370 FPENSSGRHpYAYIPF 385

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 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 1711057505  20 DLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDG-------TLLQKAWGLIAEPRMvhgWErlypDPGHFDPERFL- 91
Cdd:cd20655   283 DLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGydipektTLFVNVYAIMRDPNY---WE----DPLEFKPERFLa 355

                          90       100
                  ....*....|....*....|..
gi 1711057505  92 ---GGGTEDRR---YTYIPFGG 107
Cdd:cd20655   356 ssrSGQELDVRgqhFKLLPFGS 377

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It 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 1711057505  17 TLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGTE 96
Cdd:cd20638   288 SMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPE 367

                          90
                  ....*....|..
gi 1711057505  97 D-RRYTYIPFGG 107
Cdd:cd20638   368 DsSRFSFIPFGG 379

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 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 1711057505  12 RDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDG---------TLLQKAWGLiaeprmvHGWERLYPDP 82
Cdd:cd11046   287 DRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGggvkvpagtDIFISVYNL-------HRSPELWEDP 359

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1711057505  83 GHFDPERFLGGG-------TEDrrYTYIPFGG--------ELPILQASIDLIRLQTRqlHDVQLPEPPESPSLT 141
Cdd:cd11046   360 EEFDPERFLDPFinppnevIDD--FAFLPFGGgprkclgdQFALLEATVALAMLLRR--FDFELDVGPRHVGMT 429

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 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 1711057505  19 EDLRRLPYLDATLNETLRTLPPSS-TVTRRLTRPVVLDGTLLQKA-------WGLIAEPRMvhgWErlypDPGHFDPERF 90
Cdd:cd11075   285 EDLPKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVLGGYDIPAGaevnfnvAAIGRDPKV---WE----DPEEFKPERF 357

                          90       100
                  ....*....|....*....|..
gi 1711057505  91 LGGGTED------RRYTYIPFG 106
Cdd:cd11075   358 LAGGEAAdidtgsKEIKMMPFG 379

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A 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 1711057505   6 RKRQNRRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVL-DGTLLQKAWGLI----AEPRMVHGWErlyP 80
Cdd:cd11064   276 PKLTTDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLpDGTFVKKGTRIVysiyAMGRMESIWG---E 352

                          90       100       110
                  ....*....|....*....|....*....|
gi 1711057505  81 DPGHFDPERFLGGGTEDRR---YTYIPFGG 107
Cdd:cd11064   353 DALEFKPERWLDEDGGLRPespYKFPAFNA 382

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 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 1711057505  24 LPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGTEDRR-YTY 102
Cdd:cd20649   320 LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHpFVY 399

                          90       100
                  ....*....|....*....|....*..
gi 1711057505 103 IPFGG--------ELPILQASIDLIRL 121
Cdd:cd20649   400 LPFGAgprscigmRLALLEIKVTLLHI 426

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-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 1711057505   6 RKRQNRRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRP--VVLDGTllqkawgLIAE------PRMV-HGWE 76
Cdd:cd11061   258 DSTFPSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPRETPPggLTIDGE-------YIPGgttvsvPIYSiHRDE 330

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1711057505  77 RLYPDPGHFDPERFLGGGTEDR--RYTYIPFG 106
Cdd:cd11061   331 RYFPDPFEFIPERWLSRPEELVraRSAFIPFS 362

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 1711057505  15 PSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGG 94
Cdd:cd11083   273 PPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGA 352

                          90
                  ....*....|....*.
gi 1711057505  95 TE---DRRYTYIPFGG 107
Cdd:cd11083   353 RAaepHDPSSLLPFGA 368

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 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 1711057505  12 RDSPSTLEDLRRLPYLDATLNETLR-------TLPPSStvtrrlTRPVVLDGTLLQKawGLIAEPRM--VHGWERLYPDP 82
Cdd:cd11028   278 RERLPRLSDRPNLPYTEAFILETMRhssfvpfTIPHAT------TRDTTLNGYFIPK--GTVVFVNLwsVNHDEKLWPDP 349

                          90       100
                  ....*....|....*....|....*..
gi 1711057505  83 GHFDPERFLGGGTE-DRRYT--YIPFG 106
Cdd:cd11028   350 SVFRPERFLDDNGLlDKTKVdkFLPFG 376

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-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 1711057505  12 RDSPSTLEDLRRLPYLDATLNETLRTLPPSST-VTRRLTRPVVLDG-------TLLQKAWGliaeprMVHGwERLYPDPG 83
Cdd:cd11065   270 PDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGyfipkgtTVIPNAWA------IHHD-PEVYPDPE 342

                          90       100
                  ....*....|....*....|....*.
gi 1711057505  84 HFDPERFLGGGTEDRRYT---YIPFG 106
Cdd:cd11065   343 EFDPERYLDDPKGTPDPPdppHFAFG 368

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 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 1711057505   3 MDHRKRQNRRDSPStleDLRRLPYLDATLNETLRTLPPSS-TVTRRLTRPVVLDG-------TLLQKAWGLIAEPRmvhg 74
Cdd:cd20657   269 MDQVIGRDRRLLES---DIPNLPYLQAICKETFRLHPSTPlNLPRIASEACEVDGyyipkgtRLLVNIWAIGRDPD---- 341

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1711057505  75 werLYPDPGHFDPERFLGGGTED-----RRYTYIPFG 106
Cdd:cd20657   342 ---VWENPLEFKPERFLPGRNAKvdvrgNDFELIPFG 375

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-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 1711057505  12 RDSPSTLEDLRRLPYLDATLNETLRtLppSSTVTRRLTRpVVLDGTLLQKAWGLiaePR---------MVHGWERLYPDP 82
Cdd:cd11062   272 PDSPPSLAELEKLPYLTAVIKEGLR-L--SYGVPTRLPR-VVPDEGLYYKGWVI---PPgtpvsmssyFVHHDEEIFPDP 344

                          90       100
                  ....*....|....*....|....*.
gi 1711057505  83 GHFDPERFLGGGTEDR--RYtYIPFG 106
Cdd:cd11062   345 HEFRPERWLGAAEKGKldRY-LVPFS 369

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This 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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1711057505  21 LRRLPYLDATLNETLRTLPPSSTVTRRL-TRPVVL-DGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFL 91
Cdd:cd11041   283 LNKLKKLDSFMKESQRLNPLSLVSLRRKvLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFY 355

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-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 1711057505  19 EDLRRLPYLDATLNETLRTLPPSS-TVTRRLTRPVVLDGTLLQK-------AWGLIAEPRMvhgWErlypDPGHFDPERF 90
Cdd:cd11073   285 SDISKLPYLQAVVKETLRLHPPAPlLLPRKAEEDVEVMGYTIPKgtqvlvnVWAIGRDPSV---WE----DPLEFKPERF 357

                          90
                  ....*....|....*....
gi 1711057505  91 LGGGTE--DRRYTYIPFGG 107
Cdd:cd11073   358 LGSEIDfkGRDFELIPFGS 376

cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-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 1711057505  10 NRRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKawglIAEPRMVH-GW---------ERLY 79
Cdd:cd11070   270 DEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGQE----IVIPKGTYvGYnayathrdpTIWG 345

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1711057505  80 PDPGHFDPERFLGGG--------TEDRRYTYIPFGG 107
Cdd:cd11070   346 PDADEFDPERWGSTSgeigaatrFTPARGAFIPFSA 381

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 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 1711057505  17 TLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDPGHFDPERFLGGGTE 96
Cdd:cd20645   278 RAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHS 357

                          90
                  ....*....|
gi 1711057505  97 DRRYTYIPFG 106
Cdd:cd20645   358 INPFAHVPFG 367

brassinosteroid-6-oxidase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1711057505   3 MDHRKRQnRRDSPSTLEDLRRLPYLDATLNETLRTLPPSSTVTRRLTRPVVLDGTLLQKAWGLIAEPRMVHGWERLYPDP 82
Cdd:PLN02774  306 LAIRERK-RPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDP 384

                          90       100
                  ....*....|....*....|....*
gi 1711057505  83 GHFDPERFLGGGTEDRRYTYIpFGG 107
Cdd:PLN02774  385 MTFNPWRWLDKSLESHNYFFL-FGG 408