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 15242215   1 MYRHVKPRFSWKLQSWIGVGMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNdhfirdSHANLLTSHIKLDTTQYQL 80
Cdd:cd11064 152 AKRFIVPPWLWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEENN------VREDLLSRFLASEEEEGEP 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215  81 LDpinDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRSCSGQERP----SCDPMEYL----- 151
Cdd:cd11064 226 VS---DKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRVptyeELKKLVYLhaals 302

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 152 ----------------NKDD------------------------ESCMGRRCiriqareMDFRDRR-------------- 177
Cdd:cd11064 303 eslrlyppvpfdskeaVNDDvlpdgtfvkkgtrivysiyamgrmESIWGEDA-------LEFKPERwldedgglrpespy 375

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242215 178 --VSIQCRSRICHGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGF 232
Cdd:cd11064 376 kfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGGL 432

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 15242215   1 MYRHVKPRFSWKLQSWIGVGMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNdhfirdSHANLLTSHIKLDTTQYQL 80
Cdd:cd11064 152 AKRFIVPPWLWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEENN------VREDLLSRFLASEEEEGEP 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215  81 LDpinDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRSCSGQERP----SCDPMEYL----- 151
Cdd:cd11064 226 VS---DKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRVptyeELKKLVYLhaals 302

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 152 ----------------NKDD------------------------ESCMGRRCiriqareMDFRDRR-------------- 177
Cdd:cd11064 303 eslrlyppvpfdskeaVNDDvlpdgtfvkkgtrivysiyamgrmESIWGEDA-------LEFKPERwldedgglrpespy 375

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242215 178 --VSIQCRSRICHGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGF 232
Cdd:cd11064 376 kfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGGL 432

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 15242215    16 WIGVGMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNDhFIrdshanlltsHIKLDTTQYQLLDPINDKFLRDNVFA 95
Cdd:pfam00067 200 YFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKKSPRD-FL----------DALLLAKEEEDGSKLTDEELRATVLE 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215    96 LLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRscsgQERPSCD---PMEYLNKddescmgrrCI-------- 164
Cdd:pfam00067 269 LFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD----KRSPTYDdlqNMPYLDA---------VIketlrlhp 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215   165 -------RIQAREMDFRDR------RVSI----------------------------QCRS-----------RICHGKQR 192
Cdd:pfam00067 336 vvplllpREVTKDTVIPGYlipkgtLVIVnlyalhrdpevfpnpeefdperfldengKFRKsfaflpfgagpRNCLGERL 415

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15242215   193 AMVQMKIVAVEILQNYDIKVANGQKFEP--DTSLILKMKHGFKVKI 236
Cdd:pfam00067 416 ARMEMKLFLATLLQNFEVELPPGTDPPDidETPGLLLPPKPYKLKF 461

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 15242215   1 MYRHVKPRFSWKLQSWIGVGMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNdhfirdSHANLLTSHIKLDTTQYQL 80
Cdd:cd11064 152 AKRFIVPPWLWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEENN------VREDLLSRFLASEEEEGEP 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215  81 LDpinDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRSCSGQERP----SCDPMEYL----- 151
Cdd:cd11064 226 VS---DKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRVptyeELKKLVYLhaals 302

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 152 ----------------NKDD------------------------ESCMGRRCiriqareMDFRDRR-------------- 177
Cdd:cd11064 303 eslrlyppvpfdskeaVNDDvlpdgtfvkkgtrivysiyamgrmESIWGEDA-------LEFKPERwldedgglrpespy 375

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242215 178 --VSIQCRSRICHGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGF 232
Cdd:cd11064 376 kfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGGL 432

cytochrome P450, family 94, subfamily C protein

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215   11 WKLQSWIGVGMEKKMIEAGAIFDRVCGKYISARReevKRSQVNNNDhfirdshanLLTshikldttqyQLLDPIND-KFL 89
Cdd:PLN02426 237 WKIKRLLNIGSERKLKEAIKLVDELAAEVIRQRR---KLGFSASKD---------LLS----------RFMASINDdKYL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215   90 RDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPrscSGQERPSCDP---MEYLNK------------- 153
Cdd:PLN02426 295 RDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMG---PNQEAASFEEmkeMHYLHAalyesmrlfppvq 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215  154 -DDESC------------------------MGrRCIRIQARE-MDFRDRR---------------VSIQCRSRICHGKQR 192
Cdd:PLN02426 372 fDSKFAaeddvlpdgtfvakgtrvtyhpyaMG-RMERIWGPDcLEFKPERwlkngvfvpenpfkyPVFQAGLRVCLGKEM 450

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15242215  193 AMVQMKIVAVEILQNYDIKVANG----QKFEPdtSLILKMKHGFKVKINKR 239
Cdd:PLN02426 451 ALMEMKSVAVAVVRRFDIEVVGRsnraPRFAP--GLTATVRGGLPVRVRER 499

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 15242215  82 DPINDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLprscsGQERPSCDPMEYLNKD----DES 157
Cdd:cd20620 206 EPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVL-----GGRPPTAEDLPQLPYTemvlQES 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 158 --------CMGRRCI--------RIQAREMDF-------RDRRV---------------SIQCR-----------SRICH 188
Cdd:cd20620 281 lrlyppawIIGREAVeddeiggyRIPAGSTVLispyvthRDPRFwpdpeafdperftpeREAARpryayfpfgggPRICI 360

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15242215 189 GKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGFKV 234
Cdd:cd20620 361 GNHFAMMEAVLLLATIAQRFRLRLVPGQPVEPEPLITLRPKNGVRM 406

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. 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 15242215  83 PINDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQE---IDMNLPRSCSGQERpscdpMEYLNkddesCM 159
Cdd:cd11044 218 PLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEqdaLGLEEPLTLESLKK-----MPYLD-----QV 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 160 GRRCIRIQA------REM--DF--------RDRRVSIQCRS--------------------------------------- 184
Cdd:cd11044 288 IKEVLRLVPpvgggfRKVleDFelggyqipKGWLVYYSIRDthrdpelypdperfdperfsparsedkkkpfslipfggg 367

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15242215 185 -RICHGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGFKVKI 236
Cdd:cd11044 368 pRECLGKEFAQLEMKILASELLRNYDWELLPNQDLEPVVVPTPRPKDGLRVRF 420

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
                ....*....|....*....|....*....|....*....|....*..
gi 15242215  82 DPINDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQE 128
Cdd:cd11043 204 DSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEE 250

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 15242215    16 WIGVGMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNDhFIrdshanlltsHIKLDTTQYQLLDPINDKFLRDNVFA 95
Cdd:pfam00067 200 YFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKKSPRD-FL----------DALLLAKEEEDGSKLTDEELRATVLE 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215    96 LLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRscsgQERPSCD---PMEYLNKddescmgrrCI-------- 164
Cdd:pfam00067 269 LFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD----KRSPTYDdlqNMPYLDA---------VIketlrlhp 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215   165 -------RIQAREMDFRDR------RVSI----------------------------QCRS-----------RICHGKQR 192
Cdd:pfam00067 336 vvplllpREVTKDTVIPGYlipkgtLVIVnlyalhrdpevfpnpeefdperfldengKFRKsfaflpfgagpRNCLGERL 415

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 15242215   193 AMVQMKIVAVEILQNYDIKVANGQKFEP--DTSLILKMKHGFKVKI 236
Cdd:pfam00067 416 ARMEMKLFLATLLQNFEVELPPGTDPPDidETPGLLLPPKPYKLKF 461

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 15242215   7 PRFSWKLQSWIGVGMEKKMIEAGAIFDRVCGKYISARREEVKR-SQVNNNDHFIRDSHANLLTSHIKLDttqyqlldpin 85
Cdd:cd11069 164 LFLPRWLVRILPWKANREIRRAKDVLRRLAREIIREKKAALLEgKDDSGKDILSILLRANDFADDERLS----------- 232

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15242215  86 DKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLP 134
Cdd:cd11069 233 DEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALP 281

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 15242215  90 RDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLprscSGQERPSCD---PMEYLNkddescmgrRCI-- 164
Cdd:cd20659 229 RDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVL----GDRDDIEWDdlsKLPYLT---------MCIke 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 165 ------------RIQAREMDFRDRR--------VSIQC-----------------R--------------------SRIC 187
Cdd:cd20659 296 slrlyppvpfiaRTLTKPITIDGVTlpagtliaINIYAlhhnptvwedpeefdpeRflpenikkrdpfafipfsagPRNC 375

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15242215 188 HGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPDTSLILKMKHGFKVK 235
Cdd:cd20659 376 IGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPGLVLRSKNGIKLK 423

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
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15242215  92 NVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRSCSGQERPSCDPMEYLN 152
Cdd:cd11083 226 NVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALDRLPYLE 286

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 15242215  60 RDSHANLLTS---HIKLDTTqyqllDPINDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEID 130
Cdd:cd11049 194 SGTDRDDLLSlllAARDEEG-----RPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELD 262

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this 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 15242215  38 KYISARREEVKRS-QVNNNDHFIRDSHANLLtshikldttQYQLLDPINDKFLRDNVFALLLAGRDTTASALTWFFWFLS 116
Cdd:cd20617 181 DFIEKIIEEHLKTiDPNNPRDLIDDELLLLL---------KEGDSGLFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLA 251

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15242215 117 ENPLVVTKIRQEIDMNLPRSCSG--QERPSCdPmeYLN 152
Cdd:cd20617 252 NNPEIQEKIYEEIDNVVGNDRRVtlSDRSKL-P--YLN 286

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 15242215  23 KKMIEAGAIFDRVCGKYISARREEVKRSQVNNndhfirDSHANLLTshikldttqyQLL--DPINDKFLRDNVFALLLAG 100
Cdd:cd11054 180 KKFVKAWDTIFDIASKYVDEALEELKKKDEED------EEEDSLLE----------YLLskPGLSKKEIVTMALDLLLAG 243

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15242215 101 RDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRS 136
Cdd:cd11054 244 VDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDG 279

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. 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
                ....*....|....*....|....*....|....*....|....
gi 15242215  87 KFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEID 130
Cdd:cd11051 184 ERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHD 227

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-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
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15242215  89 LRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLPRSCSGQERPSC 145
Cdd:cd20622 263 IHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAVAEGRLPTA 319

unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized fungal 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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15242215  82 DPINDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDmNLPRSCSGQERPS-CDPMEYLN 152
Cdd:cd11059 215 QGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELA-GLPGPFRGPPDLEdLDKLPYLN 285

abscisic acid 8'-hydroxylase

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15242215   84 INDKFLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQE 128
Cdd:PLN02196 260 LTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEE 304

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 15242215   9 FSW--KLQSWIGVGMEKKMI---EAGAIFDRVCGKYISARREEVKRSQVNNNDHFIRDS--HANLLTSHIKLDTtqyqll 81
Cdd:cd11062 151 FPWllKLLRSLPESLLKRLNpglAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHAllNSDLPPSEKTLER------ 224

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15242215  82 dpindkfLRDNVFALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDMNLP 134
Cdd:cd11062 225 -------LADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMP 270

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 15242215  32 FDRVCGKYISARREEVKRSQVNNNDHFIRDSHANLLTSHIKLDTTQYQLlDPINDKFLRDNVFALLLAGRDTTASALTWF 111
Cdd:cd11028 176 FKELLNRLNSFILKKVKEHLDTYDKGHIRDITDALIKASEEKPEEEKPE-VGLTDEHIISTVQDLFGAGFDTISTTLQWS 254

                        90       100       110
                ....*....|....*....|....*....|....
gi 15242215 112 FWFLSENPLVVTKIRQEIDMNLprscsGQERPSC 145
Cdd:cd11028 255 LLYMIRYPEIQEKVQAELDRVI-----GRERLPR 283

Plant cytochrome P450s, clan CYP72; 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). The CYP72 clan is 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. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan 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 15242215  38 KYISARREEVKRSQVNNNDHfirDSHANLLTSHIKLDTTQyqlldPINDKFLRDNVFALLLAGRDTTASALTWFFWFLSE 117
Cdd:cd11052 190 EIIKKREDSLKMGRGDDYGD---DLLGLLLEANQSDDQNK-----NMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAI 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 118 NPLVVTKIRQEIdmnlpRSCSGQERP---SCDPMEYLN--------------------KDDESCMGRR-------CIRIQ 167
Cdd:cd11052 262 HPEWQEKAREEV-----LEVCGKDKPpsdSLSKLKTVSmvineslrlyppavfltrkaKEDIKLGGLVipkgtsiWIPVL 336

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 168 A---------------REMDFRDrRVSIQCRS-----------RICHGKQRAMVQMKIVAVEILQNYDIKVANGQKFEPD 221
Cdd:cd11052 337 AlhhdeeiwgedanefNPERFAD-GVAKAAKHpmaflpfglgpRNCIGQNFATMEAKIVLAMILQRFSFTLSPTYRHAPT 415

                       250
                ....*....|
gi 15242215 222 TSLILKMKHG 231
Cdd:cd11052 416 VVLTLRPQYG 425

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 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 15242215  15 SWIGV-GMEKKMIEAGAIFDRVCGKYISARREEVKRSQVNNNDHFirDSHANLLTShikLDTTQYQLLDPinDKFLRDNV 93
Cdd:cd20654 174 GWLDFgGHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKSKNDED--DDDVMMLSI---LEDSQISGYDA--DTVIKATC 246

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15242215  94 FALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEIDM 131
Cdd:cd20654 247 LELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDT 284

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 15242215  23 KKMIEAgAIFDRVCGK-YISARREEVKRSQvnnndhfirDSHANLLTSHIKLdttqYQLLDPINDKFLRDNVFALLLAGR 101
Cdd:cd20613 182 REVREA-IKFLRETGReCIEERLEALKRGE---------EVPNDILTHILKA----SEEEPDFDMEELLDDFVTFFIAGQ 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 102 DTTASALTWFFWFLSENPLVVTKIRQEIDMNLprscsGQERPSC----DPMEYLN---KddESCmgRRC------IRIQA 168
Cdd:cd20613 248 ETTANLLSFTLLELGRHPEILKRLQAEVDEVL-----GSKQYVEyedlGKLEYLSqvlK--ETL--RLYppvpgtSRELT 318

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15242215 169 REMDFRDRRV----SIQC------RS-----------------------------------RICHGKQRAMVQMKIVAVE 203
Cdd:cd20613 319 KDIELGGYKIpagtTVLVstyvmgRMeeyfedplkfdperfspeapekipsyayfpfslgpRSCIGQQFAQIEAKVILAK 398

                       250       260       270
                ....*....|....*....|....*....|.
gi 15242215 204 ILQNYDIKVANGQKFEPDTSLILKMKHGFKV 234
Cdd:cd20613 399 LLQNFKFELVPGQSFGILEEVTLRPKDGVKC 429

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
                ....*....|....*....|....*....|....*.
gi 15242215  95 ALLLAGRDTTASALTWFFWFLSENPLVVTKIRQEID 130
Cdd:cd11065 230 SLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELD 265