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Conserved domains on  [gi|530361947|ref|XP_005270596|]
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cytochrome P450 4A11 isoform X2 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

cytochrome P450 family protein may catalyze the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 74-357 3.01e-163

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.


The actual alignment was detected with superfamily member cd20678:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 436  Bit Score: 463.29  E-value: 3.01e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRPSDP----------------- 216
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSyiqavsdlsnlifqrlr 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 217 -----------------------------TEE-------------------------------GSTTEGGGAGEDQEEEA 236
Cdd:cd20678  163 nffyhndfiyklsphgrrfrracqlahqhTDKviqqrkeqlqdegelekikkkrhldfldillFAKDENGKSLSDEDLRA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 237 ----FGFSG-----------------YPPLGQRAPGLPRPCWCSG----WncfrNHLDQMPYTTMCIKEALRLYPPVPGI 291
Cdd:cd20678  243 evdtFMFEGhdttasgiswilyclalHPEHQQRCREEIREILGDGdsitW----EHLDQMPYTTMCIKEALRLYPPVPGI 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 292 GRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 357
Cdd:cd20678  319 SRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 74-357 3.01e-163

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 463.29  E-value: 3.01e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRPSDP----------------- 216
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSyiqavsdlsnlifqrlr 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 217 -----------------------------TEE-------------------------------GSTTEGGGAGEDQEEEA 236
Cdd:cd20678  163 nffyhndfiyklsphgrrfrracqlahqhTDKviqqrkeqlqdegelekikkkrhldfldillFAKDENGKSLSDEDLRA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 237 ----FGFSG-----------------YPPLGQRAPGLPRPCWCSG----WncfrNHLDQMPYTTMCIKEALRLYPPVPGI 291
Cdd:cd20678  243 evdtFMFEGhdttasgiswilyclalHPEHQQRCREEIREILGDGdsitW----EHLDQMPYTTMCIKEALRLYPPVPGI 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 292 GRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 357
Cdd:cd20678  319 SRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-357 2.22e-61

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.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 203.66  E-value: 2.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947   52 PCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD------PKSHGSYRFLAP 125
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsgrPDEPWFATSRGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  126 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ 205
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  206 GSIQVDRPS------------------------------DPTE------------------------------------- 218
Cdd:pfam00067 162 FGSLEDPKFlelvkavqelssllsspspqlldlfpilkyFPGPhgrklkrarkkikdlldklieerretldsakksprdf 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  219 -----EGSTTEGG----------------GAGED-----------------------QEE--EAFGFSGypplgqrapgl 252
Cdd:pfam00067 242 ldallLAKEEEDGskltdeelratvlelfFAGTDttsstlswalyelakhpevqeklREEidEVIGDKR----------- 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  253 pRPCWcsgwncfrNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSIYGLHHNPKVWPNPE 331
Cdd:pfam00067 311 -SPTY--------DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPE 380

                         410       420
                  ....*....|....*....|....*...
gi 530361947  332 VFDPFRFAP--GSAQHSHAFLPFSGGSR 357
Cdd:pfam00067 381 EFDPERFLDenGKFRKSFAFLPFGAGPR 408
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 88-357 2.42e-24

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 102.66  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  88 HWLWGGKVR-VQLYDPDYMKVILGRSD--PKSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:COG2124   35 FRVRLPGGGaWLVTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 163 ADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQGSiqvDRP-----SDPTEEGSTTEGGGAGEDQEEEAF 237
Cdd:COG2124  115 REIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEE---DRDrlrrwSDALLDALGPLPPERRRRARRARA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 238 GFSGY-----------PP-------LGQRAPGLPRP-----------------------CWcsGWNCFRNHLDQM----- 271
Cdd:COG2124  188 ELDAYlreliaerraePGddllsalLAARDDGERLSdeelrdellllllaghettanalAW--ALYALLRHPEQLarlra 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 272 --PYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsaqHSHAF 349
Cdd:COG2124  266 epELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAH 337


                 ....*...
gi 530361947 350 LPFSGGSR 357
Cdd:COG2124  338 LPFGGGPH 345
PLN02936 PLN02936
epsilon-ring hydroxylase
 268-357 2.74e-17

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 82.92  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-----APGS 342
Cdd:PLN02936 333 IKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdldgpVPNE 412

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:PLN02936 413 TNTDFRYIPFSGGPR 427
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 74-357 3.01e-163

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 463.29  E-value: 3.01e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRPSDP----------------- 216
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSyiqavsdlsnlifqrlr 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 217 -----------------------------TEE-------------------------------GSTTEGGGAGEDQEEEA 236
Cdd:cd20678  163 nffyhndfiyklsphgrrfrracqlahqhTDKviqqrkeqlqdegelekikkkrhldfldillFAKDENGKSLSDEDLRA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 237 ----FGFSG-----------------YPPLGQRAPGLPRPCWCSG----WncfrNHLDQMPYTTMCIKEALRLYPPVPGI 291
Cdd:cd20678  243 evdtFMFEGhdttasgiswilyclalHPEHQQRCREEIREILGDGdsitW----EHLDQMPYTTMCIKEALRLYPPVPGI 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 292 GRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 357
Cdd:cd20678  319 SRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 83-357 1.55e-96

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.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 292.92  E-value: 1.55e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  83 PSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:cd20659    1 PRAYVFWLGPFRPILVLNHPDTIKAVLKTSEPKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 163 ADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRPSDP-------------------------- 216
Cdd:cd20659   81 NECTDILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHPyvaavhelsrlvmerflnpllhfdwi 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 217 ---TEEG----------------------STTEGGGAGE-------------------------DQE--EEA--FGFSGY 242
Cdd:cd20659  161 yylTPEGrrfkkacdyvhkfaeeiikkrrKELEDNKDEAlskrkyldfldilltardedgkgltDEEirDEVdtFLFAGH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 243 PPLgqrAPGLprpCWCSgWN--CFRNH----------------------LDQMPYTTMCIKEALRLYPPVPGIGRELSTP 298
Cdd:cd20659  241 DTT---ASGI---SWTL-YSlaKHPEHqqkcreevdevlgdrddiewddLSKLPYLTMCIKESLRLYPPVPFIARTLTKP 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530361947 299 VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd20659  314 ITI-DGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKkrDPFAFIPFSAGPR 373
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 74-357 3.43e-78

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


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 246.53  E-value: 3.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD---PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAF 150
Cdd:cd20679    3 VVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAavaPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 151 HYDILKPYVGLMADSVRVMLDKWEELLGQDSP-LEVFQHVSLMTLDTIMKCAFSHQGSIQvDRPSD-------------- 215
Cdd:cd20679   83 HFNILKPYVKIFNQSTNIMHAKWRRLASEGSArLDMFEHISLMTLDSLQKCVFSFDSNCQ-EKPSEyiaailelsalvvk 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 216 --------------------------------------------PTE----------EGSTT------------EGGG-A 228
Cdd:cd20679  162 rqqqlllhldflyyltadgrrfrracrlvhdftdaviqerrrtlPSQgvddflkakaKSKTLdfidvlllskdeDGKElS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 229 GEDQEEEA--FGFSGYPPLGQ----------RAPGLPRPCWCSGWNCFR---------NHLDQMPYTTMCIKEALRLYPP 287
Cdd:cd20679  242 DEDIRAEAdtFMFEGHDTTASglswilynlaRHPEYQERCRQEVQELLKdrepeeiewDDLAQLPFLTMCIKESLRLHPP 321

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 288 VPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH--SHAFLPFSGGSR 357
Cdd:cd20679  322 VTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGrsPLAFIPFSAGPR 393
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 90-357 1.74e-62

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.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 205.45  E-value: 1.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  90 LW-GGKVRVQLYDPDYMKVILGRSD--PKSHGsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20628    6 LWiGPKPYVVVTNPEDIEVILSSSKliTKSFL-YDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 167 RVMLDKWEELLGQDSpLEVFQHVSLMTLDTIMKCAF-------------------------------------------- 202
Cdd:cd20628   85 KILVEKLKKKAGGGE-FDIFPYISLCTLDIICETAMgvklnaqsnedseyvkavkrileiilkrifspwlrfdfifrlts 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 203 ---SHQGSIQV-------------------DRPSDPTEEGST-------------TEGGGAGEDQE--EEA--FGFSG-- 241
Cdd:cd20628  164 lgkEQRKALKVlhdftnkvikerreelkaeKRNSEEDDEFGKkkrkafldllleaHEDGGPLTDEDirEEVdtFMFAGhd 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 242 ---------------YPPLGQRA---------PGLPRPCWcsgwncfrNHLDQMPYTTMCIKEALRLYPPVPGIGRELST 297
Cdd:cd20628  244 ttasaisftlyllglHPEVQEKVyeeldeifgDDDRRPTL--------EDLNKMKYLERVIKETLRLYPSVPFIGRRLTE 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 298 PVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd20628  316 DIKL-DGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAkrHPYAYIPFSAGPR 376
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-357 2.22e-61

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.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 203.66  E-value: 2.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947   52 PCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD------PKSHGSYRFLAP 125
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsgrPDEPWFATSRGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  126 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ 205
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  206 GSIQVDRPS------------------------------DPTE------------------------------------- 218
Cdd:pfam00067 162 FGSLEDPKFlelvkavqelssllsspspqlldlfpilkyFPGPhgrklkrarkkikdlldklieerretldsakksprdf 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  219 -----EGSTTEGG----------------GAGED-----------------------QEE--EAFGFSGypplgqrapgl 252
Cdd:pfam00067 242 ldallLAKEEEDGskltdeelratvlelfFAGTDttsstlswalyelakhpevqeklREEidEVIGDKR----------- 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  253 pRPCWcsgwncfrNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSIYGLHHNPKVWPNPE 331
Cdd:pfam00067 311 -SPTY--------DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPE 380

                         410       420
                  ....*....|....*....|....*...
gi 530361947  332 VFDPFRFAP--GSAQHSHAFLPFSGGSR 357
Cdd:pfam00067 381 EFDPERFLDenGKFRKSFAFLPFGAGPR 408
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 89-357 3.96e-48

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.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 167.82  E-value: 3.96e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  89 WLwGGKVRVQLYDPDYMKVILGRSD--PKSHgSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20660    7 WL-GPKPIVVLYSAETVEVILSSSKhiDKSF-EYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 167 RVMLDKWEELLGqDSPLEVFQHVSLMTLDTIMKCA----------------------------------------FS--- 203
Cdd:cd20660   85 EILVKKLKKEVG-KEEFDIFPYITLCALDIICETAmgksvnaqqnsdseyvkavyrmselvqkrqknpwlwpdfiYSltp 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 204 ----HQGSIQV--------------DRPSDPTEEGSTTEGGGAG-----------------------EDQEEE--AFGFS 240
Cdd:cd20660  164 dgreHKKCLKIlhgftnkviqerkaELQKSLEEEEEDDEDADIGkrkrlafldllleaseegtklsdEDIREEvdTFMFE 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 241 GYpplGQRAPGLprpCWCS---GWN-------------CFRN--------HLDQMPYTTMCIKEALRLYPPVPGIGRELS 296
Cdd:cd20660  244 GH---DTTAAAI---NWALyliGSHpevqekvheeldrIFGDsdrpatmdDLKEMKYLECVIKEALRLFPSVPMFGRTLS 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 297 TPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd20660  318 EDIEI-GGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAgrHPYAYIPFSAGPR 379
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 101-357 3.55e-43

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.


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 154.27  E-value: 3.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 101 DPDYMKVIL---GRSDPKShGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELl 177
Cdd:cd20620   18 HPDHIQHVLvtnARNYVKG-GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEAG- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 178 GQDSPLEVFQHVSLMTLDTIMKCAFS-----HQGSI--------------------------------------QVD--- 211
Cdd:cd20620   96 ARRGPVDVHAEMMRLTLRIVAKTLFGtdvegEADEIgdaldvaleyaarrmlspfllplwlptpanrrfrrarrRLDevi 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 212 ------RPSDPTEEG--------STTEGGGAGEDQEE---EAFGF-------------------SGYPP----------- 244
Cdd:cd20620  176 yrliaeRRAAPADGGdllsmllaARDEETGEPMSDQQlrdEVMTLflaghettanalswtwyllAQHPEvaarlraevdr 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 245 -LGQRAPGLprpcwcsgwncfrNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHN 323
Cdd:cd20620  256 vLGGRPPTA-------------EDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYR-IPAGSTVLISPYVTHRD 321

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 530361947 324 PKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd20620  322 PRFWPDPEAFDPERFTPEREAarPRYAYFPFGGGPR 357
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 87-357 1.09e-38

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.


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 141.88  E-value: 1.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  87 PHWLWGGKVRVqLYDPDYMKVILGRSDPKSHGSYRFLA---PWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd00302    5 RVRLGGGPVVV-VSDPELVREVLRDPRDFSSDAGPGLPalgDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 164 DSVRVMLDKWEELLGQDspLEVFQHVSLMTLDTIMKCAFSHQGSIQVDR------------------------------- 212
Cdd:cd00302   84 EIARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPDLGEDLEElaelleallkllgprllrplpsprlrrlrra 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 213 --------------------PSDPTEEGSTTEGGGAGEDQE--EEAFGF-------------------SGYPPLGQRapg 251
Cdd:cd00302  162 rarlrdyleeliarrraepaDDLDLLLLADADDGGGLSDEEivAELLTLllaghettasllawalyllARHPEVQER--- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 252 LPRPCWCSGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPE 331
Cdd:cd00302  239 LRAEIDAVLGDGTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVEL-GGYTIPAGTLVLLSLYAAHRDPEVFPDPD 317

                        330       340
                 ....*....|....*....|....*.
gi 530361947 332 VFDPFRFAPGSAQHSHAFLPFSGGSR 357
Cdd:cd00302  318 EFDPERFLPEREEPRYAHLPFGAGPH 343
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 75-357 8.68e-33

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.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 126.69  E-value: 8.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  75 IQKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILGRSDPKSHGSY--RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHY 152
Cdd:cd11052    4 YYHWIKQYGKNFLYWY-GTDPRLYVTEPELIKELLSKKEGYFGKSPlqPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 153 DILKPYVGLMADSVRVMLDKWEELLG-QDSPLEVFQHVSLMTLDTIMKCAF-----------SHQGSIQ---------VD 211
Cdd:cd11052   83 EKLKGMVPAMVESVSDMLERWKKQMGeEGEEVDVFEEFKALTADIISRTAFgssyeegkevfKLLRELQkicaqanrdVG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 212 RP---SDPT-------------------------EEGSTTEGGGAGED------------------------QEEEAFGF 239
Cdd:cd11052  163 IPgsrFLPTkgnkkikkldkeiedslleiikkreDSLKMGRGDDYGDDllgllleanqsddqnknmtvqeivDECKTFFF 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 240 SgypplGQRAPGLP----------RPCW-----------CSGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTP 298
Cdd:cd11052  243 A-----GHETTALLltwttmllaiHPEWqekareevlevCGKDKPPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKED 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 299 VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPN-PEVFDPFRFAPGSAQ---HSHAFLPFSGGSR 357
Cdd:cd11052  318 IKL-GGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKaakHPMAFLPFGLGPR 379
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 97-357 1.67e-31

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.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 122.69  E-value: 1.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  97 VQLYDPDYMKVILGRSDPKSHGSYRF--LAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKW 173
Cdd:cd11053   26 VVLSDPEAIKQIFTADPDVLHPGEGNslLEPLLGpNSLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITEREIDRW 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 174 eellGQDSPLEVFQHVSLMTLDTIMKCAF-SHQGSI-------------------------------------------Q 209
Cdd:cd11053  106 ----PPGQPFDLRELMQEITLEVILRVVFgVDDGERlqelrrllprlldllssplasfpalqrdlgpwspwgrflrarrR 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 210 VD---------RPSDPTEEGS---------TTEGGGAGEDQE--EEAFG--FSGYPplgQRAPGLprpCWC--------- 258
Cdd:cd11053  182 IDaliyaeiaeRRAEPDAERDdilslllsaRDEDGQPLSDEElrDELMTllFAGHE---TTATAL---AWAfywlhrhpe 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 259 -----------SGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW 327
Cdd:cd11053  256 vlarllaeldaLGGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL-GGYTLPAGTTVAPSIYLTHHRPDLY 334

                        330       340       350
                 ....*....|....*....|....*....|
gi 530361947 328 PNPEVFDPFRFApGSAQHSHAFLPFSGGSR 357
Cdd:cd11053  335 PDPERFRPERFL-GRKPSPYEYLPFGGGVR 363
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 89-357 9.04e-29

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong 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.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 115.39  E-value: 9.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  89 WLwGGKVRVQLYDPDYMKVILGRSDPKSHGS-YRFLapWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11057    7 WL-GPRPFVITSDPEIVQVVLNSPHCLNKSFfYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 168 VMLDKWEELLGQDsPLEVFQHVSLMTLDTI-------------------------------------------------- 197
Cdd:cd11057   84 KLVQRLDTYVGGG-EFDILPDLSRCTLEMIcqttlgsdvndesdgneeylesyerlfeliakrvlnpwlhpefiyrltgd 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 198 ----MKC-----AFSHQ---------GSIQVDRPSDPTEEGST-----------TEGGGAGEDQE--EEAF-----GF-- 239
Cdd:cd11057  163 ykeeQKArkilrAFSEKiiekklqevELESNLDSEEDEENGRKpqifidqllelARNGEEFTDEEimDEIDtmifaGNdt 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 240 SG------------YPPLGQRA--------PglprpcwcsgwNCFRNH----LDQMPYTTMCIKEALRLYPPVPGIGREL 295
Cdd:cd11057  243 SAttvaytllllamHPEVQEKVyeeimevfP-----------DDGQFItyedLQQLVYLEMVLKETMRLFPVGPLVGRET 311

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530361947 296 STPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd11057  312 TADIQLSNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAqrHPYAFIPFSAGPR 376
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 92-357 1.56e-28

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.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 115.15  E-value: 1.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  92 GGKVRVQLYDPDYMKVILgRSDPKSHGSYRFLA----PWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11046   19 GPKSFLVISDPAIAKHVL-RSNAFSYDKKGLLAeilePIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 168 VMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQVDRPSDPT--------EEGSTTE-----GGGAG---- 229
Cdd:cd11046   98 RLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDfGSVTEESPVIKAvylplveaEHRSVWEppywdIPAALfivp 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 230 ------------------------EDQEEEAFGFSGYPPLGQRAPGLPRPCWCSG------------------------- 260
Cdd:cd11046  178 rqrkflrdlkllndtlddlirkrkEMRQEEDIELQQEDYLNEDDPSLLRFLVDMRdedvdskqlrddlmtmliaghetta 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 261 ----WNCF---------------------RNH------LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLP 308
Cdd:cd11046  258 avltWTLYelsqnpelmakvqaevdavlgDRLpptyedLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGvKVP 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530361947 309 KGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH------AFLPFSGGSR 357
Cdd:cd11046  338 AGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNeviddfAFLPFGGGPR 392
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 268-357 3.00e-28

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.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 114.17  E-value: 3.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG--SAQ 344
Cdd:cd11056  286 LQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPEnkKKR 365

                         90
                 ....*....|...
gi 530361947 345 HSHAFLPFSGGSR 357
Cdd:cd11056  366 HPYTYLPFGDGPR 378
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 270-357 3.27e-28

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


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 113.83  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSH 347
Cdd:cd11055  284 KLKYLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAkrHPY 362

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd11055  363 AYLPFGAGPR 372
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 90-357 2.44e-27

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.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 111.78  E-value: 2.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  90 LWGGKVR-VQLYDPDYMKVILGRSD--PKSHgSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20680   17 LWIGPVPfVILYHAENVEVILSSSKhiDKSY-LYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 167 RVMLDKWEELLGQDsPLEVFQHVSLMTLDTIMKCAF-------------------------------------------- 202
Cdd:cd20680   96 NILVEKLEKHVDGE-AFNCFFDITLCALDIICETAMgkkigaqsnkdseyvqavyrmsdiiqrrqkmpwlwldlwylmfk 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 203 ----------------------------SHQGSIQVDRPSDPTEEG---------STTEGGG---AGEDQEEE--AFGFS 240
Cdd:cd20680  175 egkehnknlkilhtftdnviaeraeemkAEEDKTGDSDGESPSKKKrkafldmllSVTDEEGnklSHEDIREEvdTFMFE 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 241 GYPP-----------LGQRaPGLPRPCWCSGWNCFRNH--------LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTF 301
Cdd:cd20680  255 GHDTtaaamnwslylLGSH-PEVQRKVHKELDEVFGKSdrpvtmedLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEI 333

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 302 pDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 357
Cdd:cd20680  334 -RGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSgrHPYAYIPFSAGPR 390
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 268-357 1.68e-26

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.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 109.15  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGS--AQH 345
Cdd:cd20613  290 LGKLEYLSQVLKETLRLYPPVPGTSRELTKDIEL-GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEApeKIP 368

                         90
                 ....*....|..
gi 530361947 346 SHAFLPFSGGSR 357
Cdd:cd20613  369 SYAYFPFSLGPR 380
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 88-357 2.42e-24

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 102.66  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  88 HWLWGGKVR-VQLYDPDYMKVILGRSD--PKSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:COG2124   35 FRVRLPGGGaWLVTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 163 ADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQGSiqvDRP-----SDPTEEGSTTEGGGAGEDQEEEAF 237
Cdd:COG2124  115 REIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEE---DRDrlrrwSDALLDALGPLPPERRRRARRARA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 238 GFSGY-----------PP-------LGQRAPGLPRP-----------------------CWcsGWNCFRNHLDQM----- 271
Cdd:COG2124  188 ELDAYlreliaerraePGddllsalLAARDDGERLSdeelrdellllllaghettanalAW--ALYALLRHPEQLarlra 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 272 --PYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsaqHSHAF 349
Cdd:COG2124  266 epELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAH 337


                 ....*...
gi 530361947 350 LPFSGGSR 357
Cdd:COG2124  338 LPFGGGPH 345
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 87-357 2.56e-24

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 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.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 102.91  E-value: 2.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  87 PHWLW-GGKVRVQLYDPDYMK-VILGRSDP-KSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd20639   14 TFLYWfGPTPRLTVADPELIReILLTRADHfDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 164 DSVRVMLDKWEELLGQDSPLEV-----FQHVslmTLDTIMKCAF------------------------------------ 202
Cdd:cd20639   94 KSVADMLDKWEAMAEAGGEGEVdvaewFQNL---TEDVISRTAFgssyedgkavfrlqaqqmllaaeafrkvyipgyrfl 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 203 ---SHQGSIQVDR-----------------PSDPTEEGSTTEGGG---AGEDQEEEA------------FGFSG------ 241
Cdd:cd20639  171 ptkKNRKSWRLDKeirksllklierrqtaaDDEKDDEDSKDLLGLmisAKNARNGEKmtveeiieecktFFFAGkettsn 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 242 -----------YPPLGQRA----------PGLPRpcwcsgwncfRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 300
Cdd:cd20639  251 lltwttvllamHPEWQERArrevlavcgkGDVPT----------KDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVK 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530361947 301 FpDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGS---AQHSHAFLPFSGGSR 357
Cdd:cd20639  321 L-GGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVaraAKHPLAFIPFGLGPR 380
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 266-357 1.73e-23

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.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 100.36  E-value: 1.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSA 343
Cdd:cd20617  277 SDRSKLPYLNAVIKEVLRLRPILPlGLPRVTTEDTEI-GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGN 355

                         90
                 ....*....|....
gi 530361947 344 QHSHAFLPFSGGSR 357
Cdd:cd20617  356 KLSEQFIPFGIGKR 369
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 267-357 2.49e-22

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.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 97.21  E-value: 2.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF----APGS 342
Cdd:cd11054  286 DLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVL-SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrddSENK 364

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:cd11054  365 NIHPFASLPFGFGPR 379
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 267-357 1.65e-21

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 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.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 94.94  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQ- 344
Cdd:cd11068  284 QVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRk 363

                         90
                 ....*....|....
gi 530361947 345 -HSHAFLPFSGGSR 357
Cdd:cd11068  364 lPPNAWKPFGNGQR 377
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 268-357 7.88e-21

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.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 92.71  E-value: 7.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG--SAQH 345
Cdd:cd11049  275 LPRLTYTRRVVTEALRLYPPVWLLTRRTTADVEL-GGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGraAAVP 353

                         90
                 ....*....|..
gi 530361947 346 SHAFLPFSGGSR 357
Cdd:cd11049  354 RGAFIPFGAGAR 365
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 266-357 1.05e-20

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.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 92.24  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH 345
Cdd:cd11043  267 EDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEY-KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV 345

                         90
                 ....*....|..
gi 530361947 346 SHAFLPFSGGSR 357
Cdd:cd11043  346 PYTFLPFGGGPR 357
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 91-357 1.67e-20

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.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 91.95  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  91 WGGKVRVQLYDPDYMKVILGRSD---PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11069   10 LFGSERLLVTDPKALKHILVTNSydfEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 168 VMLDKWEELL----GQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQvdRPSDPT------------------------- 217
Cdd:cd11069   90 ELVDKLEEEIeesgDESISIDVLEWLSRATLDIIGLAGFGYDfDSLE--NPDNELaeayrrlfeptllgsllfilllflp 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 218 -------------------------------------EEGSTTEG----------GGAGEDQ---EEEA------FGFSG 241
Cdd:cd11069  168 rwlvrilpwkanreirrakdvlrrlareiirekkaalLEGKDDSGkdilsillraNDFADDErlsDEELidqiltFLAAG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 242 YPPLGQrapGLPRPCWC----------------------SGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPv 299
Cdd:cd11069  248 HETTST---ALTWALYLlakhpdvqerlreeiraalpdpPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKD- 323

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361947 300 TFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF-------APGSAQHSHAFLPFSGGSR 357
Cdd:cd11069  324 TVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgaaSPGGAGSNYALLTFLHGPR 389
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 89-355 7.11e-20

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. 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.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 90.07  E-value: 7.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  89 WLWGGKVR-VQLYDPDYMKVILgRSDPKSHGSYR----FLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd11045   15 WTGMLGLRvVALLGPDANQLVL-RNRDKAFSSKQgwdpVIGPFFHRGLMLLDFDEHRAHRRIMQQAFTRSALAGYLDRMT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 164 DSVRVMLDKW------------EELLgQDSPLEVFQHVSLMTL-DTIMKcAFSH--QGSIQVDRPSDPteeGSTTEGG-- 226
Cdd:cd11045   94 PGIERALARWptgagfqfypaiKELT-LDLATRVFLGVDLGPEaDKVNK-AFIDtvRASTAIIRTPIP---GTRWWRGlr 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 227 ------------------GAGED--------QEEEAFGFSG-------------------------------YPPLGQR- 248
Cdd:cd11045  169 grryleeyfrrriperraGGGDDlfsalcraEDEDGDRFSDddivnhmiflmmaahdtttstltsmayflarHPEWQERl 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 249 -----APGLPRPCWcsgwncfrNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHN 323
Cdd:cd11045  249 reeslALGKGTLDY--------EDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LGYRIPAGTLVAVSPGVTHYM 319

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 530361947 324 PKVWPNPEVFDPFRFAPGSA---QHSHAFLPFSGG 355
Cdd:cd11045  320 PEYWPNPERFDPERFSPERAedkVHRYAWAPFGGG 354
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 75-357 8.55e-20

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 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.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 90.03  E-value: 8.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  75 IQKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILGRSD--PKSHgsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHY 152
Cdd:cd20642    4 IHHTVKTYGKNSFTWF-GPIPRVIIMDPELIKEVLNKVYdfQKPK--TNPLTKLLATGLASYEGDKWAKHRKIINPAFHL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 153 DILKPYVGLMADSVRVMLDKWEELLGQD--SPLEVFQHVSLMTLDTIMKCAF--------------SHQGSI-------- 208
Cdd:cd20642   81 EKLKNMLPAFYLSCSEMISKWEKLVSSKgsCELDVWPELQNLTSDVISRTAFgssyeegkkifelqKEQGELiiqalrkv 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 209 -----------------QVDR----------------------PSD------------PTEEGSTTEGGGAGEDQEEE-- 235
Cdd:cd20642  161 yipgwrflptkrnrrmkEIEKeirsslrgiinkrekamkageaTNDdllgillesnhkEIKEQGNKNGGMSTEDVIEEck 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 236 AFGFSG-----------------YPPLGQRA------------P---GLprpcwcsgwncfrNHLDQMpytTMCIKEALR 283
Cdd:cd20642  241 LFYFAGqettsvllvwtmvllsqHPDWQERAreevlqvfgnnkPdfeGL-------------NHLKVV---TMILYEVLR 304

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 284 LYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPN-PEVFDPFRFAPGSAQHSH---AFLPFSGGSR 357
Cdd:cd20642  305 LYPPVIQLTRAIHKDTKLGD-LTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAEGISKATKgqvSYFPFGWGPR 381
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 268-357 8.60e-20

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.


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 90.08  E-value: 8.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRS----LPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGS 342
Cdd:cd11070  281 FPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGqeivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTS 360

                         90       100
                 ....*....|....*....|....
gi 530361947 343 -----AQHSH----AFLPFSGGSR 357
Cdd:cd11070  361 geigaATRFTpargAFIPFSAGPR 384
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 267-357 1.59e-19

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.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 88.88  E-value: 1.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP-GSAQH 345
Cdd:cd11044  277 SLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPaRSEDK 355

                         90
                 ....*....|....
gi 530361947 346 SHAF--LPFSGGSR 357
Cdd:cd11044  356 KKPFslIPFGGGPR 369
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 77-357 2.98e-19

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 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.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 88.24  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  77 KWVETFPSACPHWLwGGKVRVQLYDPDYMKVI-------LGRSD--PKSHGsyrflaPWIGYGLLLLNGQTWFQHRRMLT 147
Cdd:cd20640    6 KWRKQYGPIFTYST-GNKQFLYVSRPEMVKEInlcvsldLGKPSylKKTLK------PLFGGGILTSNGPHWAHQRKIIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 148 PAFHYDILKPYVGLMADSVRVMLDKWEELL----GQDSPLEVFQHVSLMTLDTIMKCAF--------------------- 202
Cdd:cd20640   79 PEFFLDKVKGMVDLMVDSAQPLLSSWEERIdragGMAADIVVDEDLRAFSADVISRACFgssyskgkeifsklrelqkav 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 203 SHQ---------------GSIQVDR-----------PSDPTEEGSTTE-----------GGGAGEDQEEEAF-------- 237
Cdd:cd20640  159 SKQsvlfsipglrhlptkSNRKIWElegeirslileIVKEREEECDHEkdllqailegaRSSCDKKAEAEDFivdnckni 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 238 GFSGYPPLGQRAP------GLpRPCW-----------CSGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 300
Cdd:cd20640  239 YFAGHETTAVTAAwclmllAL-HPEWqdrvraevlevCKGGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMK 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530361947 301 FPDGRsLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFA---PGSAQHSHAFLPFSGGSR 357
Cdd:cd20640  318 LGGLV-VPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSngvAAACKPPHSYMPFGAGAR 377
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 266-356 3.92e-19

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.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 87.66  E-value: 3.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ 344
Cdd:cd11042  267 DVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAE 346

                         90
                 ....*....|....*.
gi 530361947 345 HSH----AFLPFSGGS 356
Cdd:cd11042  347 DSKggkfAYLPFGAGR 362
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 76-357 3.97e-19

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 87.89  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947  76 QKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILgrSDPKSHGSYRFLAPWI----GYGLLLLNGQTWFQHRRMLTPAFH 151
Cdd:cd20641    5 QQWKSQYGETFLYWQ-GTTPRICISDHELAKQVL--SDKFGFFGKSKARPEIlklsGKGLVFVNGDDWVRHRRVLNPAFS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 152 YDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSL----MTLDTIMKCAF--SHQGSIQVDRPSD---------- 215
Cdd:cd20641   82 MDKLKSMTQVMADCTERMFQEWRKQRNNSETERIEVEVSRefqdLTADIIATTAFgsSYAEGIEVFLSQLelqkcaaasl 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 216 -----------PT---------------------EEGSTTEGGGAGED----------------------------QEEE 235
Cdd:cd20641  162 tnlyipgtqylPTprnlrvwklekkvrnsikriiDSRLTSEGKGYGDDllglmleaassneggrrterkmsideiiDECK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 236 AFGFSGYpplGQRAPGLP--------RPCW-----------CSGWNC-FRNHLDQMPYTTMCIKEALRLYPPVPGIGREL 295
Cdd:cd20641  242 TFFFAGH---ETTSNLLTwtmfllslHPDWqeklreevfreCGKDKIpDADTLSKLKLMNMVLMETLRLYGPVINIARRA 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361947 296 STPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPG---SAQHSHAFLPFSGGSR 357
Cdd:cd20641  319 SEDMKL-GGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGvsrAATHPNALLSFSLGPR 383
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 268-357 5.79e-19

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 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.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 87.23  E-value: 5.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFP-----DGRS---LPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF 338
Cdd:cd11063  272 LKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggpDGKSpifVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERW 351

                         90
                 ....*....|....*....
gi 530361947 339 APGSaQHSHAFLPFSGGSR 357
Cdd:cd11063  352 EDLK-RPGWEYLPFNGGPR 369
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 268-357 1.70e-18

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.


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 85.81  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIG-RELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHS 346
Cdd:cd11059  278 LDKLPYLNAVIRETLRLYPPIPGSLpRVVPEGGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETA 357

                         90
                 ....*....|....*
gi 530361947 347 H----AFLPFSGGSR 357
Cdd:cd11059  358 RemkrAFWPFGSGSR 372
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 265-357 2.15e-18

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-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.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 85.72  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 265 RNHLdqmPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 343
Cdd:cd11027  285 RKRL---PYLEATIAEVLRLSSVVPlALPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENG 360

                         90
                 ....*....|....*..
gi 530361947 344 Q---HSHAFLPFSGGSR 357
Cdd:cd11027  361 KlvpKPESFLPFSAGRR 377
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 112-357 6.09e-18

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.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 84.23  E-value: 6.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 112 SDPKSHGSYRFLAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVS 190
Cdd:cd11051   29 NLPKPPPLRKFLTPLTGgSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILRELAESGEVFSLEELTT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 191 LMTLDTIMKCAFshqgsiqvDRPSDPTEEGSTTEGGGAGEDQEEEAFG--FSGYPPLG-------------------QRA 249
Cdd:cd11051  109 NLTFDVIGRVTL--------DIDLHAQTGDNSLLTALRLLLALYRSLLnpFKRLNPLRplrrwrngrrldrylkpevRKR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 250 PGLPRP-------------------CWC----------------------------------SGWNCfrnhLDQMPYTTM 276
Cdd:cd11051  181 FELERAidqiktflfaghdttsstlCWAfyllskhpevlakvraehdevfgpdpsaaaellrEGPEL----LNQLPYTTA 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 277 CIKEALRLYPPV-------PGIGrelstpVTFPDGRSLP-KGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQH- 345
Cdd:cd11051  257 VIKETLRLFPPAgtarrgpPGVG------LTDRDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWlvDEGHELYp 330

                        330
                 ....*....|...
gi 530361947 346 -SHAFLPFSGGSR 357
Cdd:cd11051  331 pKSAWRPFERGPR 343
PLN02936 PLN02936
epsilon-ring hydroxylase
 268-357 2.74e-17

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 82.92  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-----APGS 342
Cdd:PLN02936 333 IKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdldgpVPNE 412

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:PLN02936 413 TNTDFRYIPFSGGPR 427
PTZ00404 PTZ00404
cytochrome P450; Provisional
 272-357 1.40e-16

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 80.54  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 272 PYTTMCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAqhSHAFL 350
Cdd:PTZ00404 343 PYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS--NDAFM 420


                 ....*..
gi 530361947 351 PFSGGSR 357
Cdd:PTZ00404 421 PFSIGPR 427
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 267-357 1.72e-16

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.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 79.96  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIG-RElsTP---VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGS 342
Cdd:cd11061  272 KLKSLPYLRACIDEALRLSPPVPSGLpRE--TPpggLTI-DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRP 348

                         90
                 ....*....|....*...
gi 530361947 343 AQHSH---AFLPFSGGSR 357
Cdd:cd11061  349 EELVRarsAFIPFSIGPR 366
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 266-357 2.53e-16

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-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.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 79.43  E-value: 2.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIG-RELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA- 343
Cdd:cd11072  282 EDLEKLKYLKAVIKETLRLHPPAPLLLpRECREDCKI-NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSId 360

                         90
                 ....*....|....*.
gi 530361947 344 --QHSHAFLPFSGGSR 357
Cdd:cd11072  361 fkGQDFELIPFGAGRR 376
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 266-357 3.05e-16

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.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 79.50  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH 345
Cdd:cd20649  315 ANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVV-LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQR 393

                         90
                 ....*....|....
gi 530361947 346 SH--AFLPFSGGSR 357
Cdd:cd20649  394 RHpfVYLPFGAGPR 407
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 268-356 1.09e-15

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 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.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 77.67  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPkvWPNPEVFDPFRFAPGSA---Q 344
Cdd:cd11082  277 LEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQedrK 354

                         90
                 ....*....|..
gi 530361947 345 HSHAFLPFSGGS 356
Cdd:cd11082  355 YKKNFLVFGAGP 366
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 270-357 1.74e-15

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A 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.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 77.07  E-value: 1.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH--SH 347
Cdd:cd20650  286 QMEYLDMVVNETLRLFPIAGRLERVCKKDVEI-NGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNidPY 364

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd20650  365 IYLPFGSGPR 374
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 267-357 3.70e-15

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. 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. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. 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 CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. 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.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 76.05  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-- 343
Cdd:cd20618  284 DLPKLPYLQAVVKETLRLHPPGPlLLPHESTEDCKV-AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIdd 362

                         90
                 ....*....|....*..
gi 530361947 344 ---QHSHaFLPFSGGSR 357
Cdd:cd20618  363 vkgQDFE-LLPFGSGRR 378
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 267-357 8.01e-15

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.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 75.26  E-value: 8.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ- 344
Cdd:cd11073  286 DISKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEV-MGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDf 364

                         90
                 ....*....|....*
gi 530361947 345 --HSHAFLPFSGGSR 357
Cdd:cd11073  365 kgRDFELIPFGSGRR 379
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 266-338 8.14e-15

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.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 74.92  E-value: 8.14e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:cd11065  277 EDRPNLPYVNAIVKEVLRWRPVAPlGIPHALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERY 349
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 267-341 1.29e-14

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.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 74.59  E-value: 1.29e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG 341
Cdd:cd11075  286 DLPKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAG 360
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 267-357 1.77e-14

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.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 74.16  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF--APGSA 343
Cdd:cd11064  290 ELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWldEDGGL 369

                         90
                 ....*....|....*.
gi 530361947 344 QH--SHAFLPFSGGSR 357
Cdd:cd11064  370 RPesPYKFPAFNAGPR 385
PLN02655 PLN02655
ent-kaurene oxidase
 267-357 1.91e-14

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 74.01  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHS 346
Cdd:PLN02655 316 DLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESA 395

                         90
                 ....*....|...
gi 530361947 347 --HAFLPFSGGSR 357
Cdd:PLN02655 396 dmYKTMAFGAGKR 408
PLN02290 PLN02290
cytokinin trans-hydroxylase
 110-357 2.23e-14

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 74.08  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 110 GRSDPKSHGSYRFlapwIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQ-DSPLEVFQH 188
Cdd:PLN02290 127 GKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESgQTEVEIGEY 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 189 VSLMTLDTIMKCAF--------------------SHQGSIQ-------------------------------VDRPSDPT 217
Cdd:PLN02290 203 MTRLTADIISRTEFdssyekgkqifhlltvlqrlCAQATRHlcfpgsrffpskynreikslkgeverllmeiIQSRRDCV 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 218 EEG-STTEGGG-----AGEDQEEEAFGFSGYPPL-----------GQRAPGL----------PRPCW-----------CS 259
Cdd:PLN02290 283 EIGrSSSYGDDllgmlLNEMEKKRSNGFNLNLQLimdecktfffaGHETTALlltwtlmllaSNPTWqdkvraevaevCG 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 260 GWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF 338
Cdd:PLN02290 363 GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF 441

                        330
                 ....*....|....*....
gi 530361947 339 APGSAQHSHAFLPFSGGSR 357
Cdd:PLN02290 442 AGRPFAPGRHFIPFAAGPR 460
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 268-356 2.97e-14

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.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 73.48  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-----PG 341
Cdd:cd11041  283 LNKLKKLDSFMKESQRLNPLSLvSLRRKVLKDVTLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlreqPG 362

                         90       100
                 ....*....|....*....|.
gi 530361947 342 SAQHSHA------FLPFSGGS 356
Cdd:cd11041  363 QEKKHQFvstspdFLGFGHGR 383
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 278-357 3.58e-14

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.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 73.03  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ-----HSHAFLPF 352
Cdd:cd20654  307 VKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDidvrgQNFELIPF 386


                 ....*
gi 530361947 353 SGGSR 357
Cdd:cd20654  387 GSGRR 391
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 266-357 3.67e-14

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-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.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 73.21  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGS 342
Cdd:cd20652  288 EDLSSLPYLQACISESQRIRSVVPlGIPHGCTEDAVL-AGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGK 366

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:cd20652  367 YLKPEAFIPFQTGKR 381
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 268-357 7.24e-14

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.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 72.29  E-value: 7.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPG-----IGRElstPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR-FAPG 341
Cdd:cd11062  281 LEKLPYLTAVIKEGLRLSYGVPTrlprvVPDE---GLYY-KGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERwLGAA 356

                         90
                 ....*....|....*..
gi 530361947 342 SAQHSHAFL-PFSGGSR 357
Cdd:cd11062  357 EKGKLDRYLvPFSKGSR 373
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 269-357 1.29e-13

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-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.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 71.48  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 269 DQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHS 346
Cdd:cd20651  282 SKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFldEDGKLLKD 361

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20651  362 EWFLPFGAGKR 372
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 268-357 1.82e-13

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.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 71.00  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGR-ELSTPVTfpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHS 346
Cdd:cd20638  292 LEQLKYTGCVIKETLRLSPPVPGGFRvALKTFEL--NGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDS 369

                         90
                 ....*....|...
gi 530361947 347 H--AFLPFSGGSR 357
Cdd:cd20638  370 SrfSFIPFGGGSR 382
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 268-357 3.56e-13

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-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.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 69.92  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ-- 344
Cdd:cd11058  273 LAQLPYLNAVIQEALRLYPPVPaGLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFef 352

                         90
                 ....*....|....*.
gi 530361947 345 ---HSHAFLPFSGGSR 357
Cdd:cd11058  353 dndKKEAFQPFSVGPR 368
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 270-357 3.75e-13

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 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.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 69.90  E-value: 3.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHS 346
Cdd:cd11026  284 KMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKF-RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFldEQGKFKKN 362

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd11026  363 EAFMPFSAGKR 373
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 268-355 7.07e-13

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. 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.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 69.32  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPpVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF-----APG 341
Cdd:cd11040  284 LTSCPLLDSTYLETLRLHS-SSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgDKK 362

                         90
                 ....*....|....
gi 530361947 342 SAQHSHAFLPFSGG 355
Cdd:cd11040  363 GRGLPGAFRPFGGG 376
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 266-357 1.72e-12

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. 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.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 68.05  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGS 342
Cdd:cd20621  283 EDLQKLNYLNAFIKEVLRLYNPAPFlFPRVATQDHQIGD-LKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWlnQNNI 361

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:cd20621  362 EDNPFVFIPFSAGPR 376
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 251-357 2.57e-12

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.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 67.55  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 251 GLPRPCWCSGWNCFRNHLDQMPYTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHNPKVWPN 329
Cdd:cd20636  272 GLIDQCQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYR--TALQTFElDGYQIPKGWSVMYSIRDTHETAAVYQN 349

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530361947 330 PEVFDPFRFAPG---SAQHSHAFLPFSGGSR 357
Cdd:cd20636  350 PEGFDPDRFGVEreeSKSGRFNYIPFGGGVR 380
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 269-357 3.56e-12

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), 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. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 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.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 67.05  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 269 DQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-PGSAqhSH 347
Cdd:cd20674  283 ARLPLLNATIAEVLRLRPVVPLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLePGAA--NR 360

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd20674  361 ALLPFGCGAR 370
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 269-357 6.42e-12

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J 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.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 66.36  E-value: 6.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 269 DQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP-GSAQHS 346
Cdd:cd20662  282 ESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLEnGQFKKR 360

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20662  361 EAFLPFSMGKR 371
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 268-357 7.54e-12

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.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 66.08  E-value: 7.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA---- 343
Cdd:cd20655  284 LPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRsgqe 362

                         90
                 ....*....|....*....
gi 530361947 344 -----QHSHaFLPFSGGSR 357
Cdd:cd20655  363 ldvrgQHFK-LLPFGSGRR 380
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 270-357 7.63e-12

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of 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.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 65.99  E-value: 7.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVP-GIGRELSTPvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HS 346
Cdd:cd20661  296 KMPYTEAVLHEVLRFCNIVPlGIFHATSKD-AVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQfaKK 374

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20661  375 EAFVPFSLGRR 385
PLN02738 PLN02738
carotene beta-ring hydroxylase
 270-357 1.03e-11

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 66.09  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPG-IGRELSTPV--TFPDGRslpkGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-----PG 341
Cdd:PLN02738 448 KLKYTTRVINESLRLYPQPPVlIRRSLENDMlgGYPIKR----GEDIFISVWNLHRSPKHWDDAEKFNPERWPldgpnPN 523

                         90
                 ....*....|....*.
gi 530361947 342 SAQHSHAFLPFSGGSR 357
Cdd:PLN02738 524 ETNQNFSYLPFGGGPR 539
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 283-355 1.27e-11

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 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.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 65.24  E-value: 1.27e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 283 RLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGG 355
Cdd:cd11067  274 RFYPFFPFVGARARRDFEW-QGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFL-GWEGDPFDFIPQGGG 344
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 258-357 1.71e-11

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-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.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 65.03  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 258 CSGWNCFRNhlDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPF 336
Cdd:cd11066  280 DAWEDCAAE--EKCPYVVALVKETLRYFTVLPlGLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPE 356

                         90       100
                 ....*....|....*....|...
gi 530361947 337 RF--APGSAQHSHAFLPFSGGSR 357
Cdd:cd11066  357 RWldASGDLIPGPPHFSFGAGSR 379
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 273-357 1.75e-11

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 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.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 65.08  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 273 YTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSH 347
Cdd:cd20658  298 YVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSevtltEPDL 377

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd20658  378 RFISFSTGRR 387
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 269-357 2.55e-11

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.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 64.24  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 269 DQMPYTTMCIKEALRLYPPVPgigrelstpVTFP---------DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA 339
Cdd:cd11028  288 PNLPYTEAFILETMRHSSFVP---------FTIPhattrdttlNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFL 358

                         90       100
                 ....*....|....*....|..
gi 530361947 340 PGSAQ----HSHAFLPFSGGSR 357
Cdd:cd11028  359 DDNGLldktKVDKFLPFGAGRR 380
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 265-357 3.05e-11

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 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.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 64.26  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 265 RNHLdqmPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA 339
Cdd:cd20673  288 RNHL---PLLEATIREVLRIRPVAP-----LLIPhVALQDssigEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL 359

                         90       100
                 ....*....|....*....|..
gi 530361947 340 PGSAQH----SHAFLPFSGGSR 357
Cdd:cd20673  360 DPTGSQlispSLSYLPFGAGPR 381
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 268-357 3.10e-11

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.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 64.36  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGsaqhS 346
Cdd:cd20657  284 IPNLPYLQAICKETFRLHPSTPlNLPRIASEACEV-DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPG----R 358

                         90       100
                 ....*....|....*....|.
gi 530361947 347 HA----------FLPFSGGSR 357
Cdd:cd20657  359 NAkvdvrgndfeLIPFGAGRR 379
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 265-357 4.16e-11

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-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.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 63.82  E-value: 4.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 265 RNHldqMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APG 341
Cdd:cd20665  282 RSH---MPYTDAVIHEIQRYIDLVPnNLPHAVTCDTKF-RNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFldENG 357

                         90
                 ....*....|....*.
gi 530361947 342 SAQHSHAFLPFSGGSR 357
Cdd:cd20665  358 NFKKSDYFMPFSAGKR 373
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 270-357 5.36e-11

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-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.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 63.37  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVpGIGRELSTP---VTFPdGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF--APGS- 342
Cdd:cd11060  283 KLPYLQAVIKEALRLHPPV-GLPLERVVPpggATIC-GRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEq 360

                         90
                 ....*....|....*.
gi 530361947 343 -AQHSHAFLPFSGGSR 357
Cdd:cd11060  361 rRMMDRADLTFGAGSR 376
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 261-355 5.97e-11

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 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.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 63.10  E-value: 5.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 261 WNCFRNHLDQMPYTTMCIKEALRLYPPvpG-IGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA 339
Cdd:cd20635  263 IKISEDDLKKMPYIKRCVLEAIRLRSP--GaITRKVVKPIKIKN-YTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWK 339

                         90
                 ....*....|....*....
gi 530361947 340 ---PGSAQHSHAFLPFSGG 355
Cdd:cd20635  340 kadLEKNVFLEGFVAFGGG 358
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 270-357 6.21e-11

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of 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.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 63.26  E-value: 6.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSH 347
Cdd:cd20666  286 QMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQliKKE 365

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd20666  366 AFIPFGIGRR 375
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 268-357 6.24e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 63.29  E-value: 6.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPpvpgigrelSTPVTFP---------DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:PLN02687 353 LPQLTYLQAVIKETFRLHP---------STPLSLPrmaaeeceiNGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRF 423

                         90       100
                 ....*....|....*....|....*....
gi 530361947 339 APGSaqhSHA----------FLPFSGGSR 357
Cdd:PLN02687 424 LPGG---EHAgvdvkgsdfeLIPFGAGRR 449
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 271-343 1.32e-10

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 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.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 62.35  E-value: 1.32e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIG-RELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 343
Cdd:cd11076  283 LPYLQAVVKETLRLHPPGPLLSwARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEG 356
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 271-357 2.17e-10

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 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.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 61.47  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFL 350
Cdd:cd20653  286 LPYLQNIISETLRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE-GEEREGYKLI 364


                 ....*..
gi 530361947 351 PFSGGSR 357
Cdd:cd20653  365 PFGLGRR 371
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 270-357 5.60e-10

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 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.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 60.19  E-value: 5.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ---HS 346
Cdd:cd20656  288 QLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDikgHD 367

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20656  368 FRLLPFGAGRR 378
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 270-357 7.04e-10

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 60.11  E-value: 7.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQhSHAF 349
Cdd:PLN02302 349 KMEYLSQVIDETLRLINISLTVFREAKTDVEV-NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPK-AGTF 426


                 ....*...
gi 530361947 350 LPFSGGSR 357
Cdd:PLN02302 427 LPFGLGSR 434
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 271-357 9.49e-10

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 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.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 59.67  E-value: 9.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHA 348
Cdd:cd20646  292 MPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFG 371


                 ....*....
gi 530361947 349 FLPFSGGSR 357
Cdd:cd20646  372 SIPFGYGVR 380
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 270-355 1.06e-09

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 59.56  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApgSAQHSHAF 349
Cdd:PLN02196 325 KMPLTSRVIQETLRVASILSFTFREAVEDVEY-EGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFE--VAPKPNTF 401


                 ....*.
gi 530361947 350 LPFSGG 355
Cdd:PLN02196 402 MPFGNG 407
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 273-357 1.12e-09

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 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.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 59.48  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 273 YTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHA--- 348
Cdd:cd20637  293 YLDCVIKEVLRLFTPVSGGYR--TALQTFElDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGrfh 370


                 ....*....
gi 530361947 349 FLPFSGGSR 357
Cdd:cd20637  371 YLPFGGGVR 379
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 268-357 1.15e-09

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 59.45  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG----- 341
Cdd:PLN03112 352 LVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTI-NGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAegsrv 430

                         90
                 ....*....|....*...
gi 530361947 342 SAQHSHAF--LPFSGGSR 357
Cdd:PLN03112 431 EISHGPDFkiLPFSAGKR 448
PLN02183 PLN02183
ferulate 5-hydroxylase
 268-357 2.74e-09

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 58.32  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF----APGSA 343
Cdd:PLN02183 360 LEKLTYLKCTLKETLRLHPPIPLLLHETAED-AEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFlkpgVPDFK 438

                         90
                 ....*....|....
gi 530361947 344 QHSHAFLPFSGGSR 357
Cdd:PLN02183 439 GSHFEFIPFGSGRR 452
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 247-337 4.00e-09

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. 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.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 57.45  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 247 QRAPGLPRPcwcsgwncfRNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKV 326
Cdd:cd20614  250 AAAGDVPRT---------PAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSRDPEL 319

                         90
                 ....*....|.
gi 530361947 327 WPNPEVFDPFR 337
Cdd:cd20614  320 YPDPDRFRPER 330
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 278-356 4.68e-09

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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.


Pssm-ID: 410719  Cd Length: 381  Bit Score: 57.42  E-value: 4.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 278 IKEALRLYPPVPGIGRelstpvTFPDgRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGS 356
Cdd:cd20626  262 VKEALRLYPPTRRIYR------AFQR-PGSSKPEIIAADIEACHRSESIWgPDALEFNPSRWSKLTPTQKEAFLPFGSGP 334
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 264-357 9.10e-09

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A 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.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 56.73  E-value: 9.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 264 FRNHLdQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--P 340
Cdd:cd20668  279 FEDRA-KMPYTEAVIHEIQRFGDVIPmGLARRVTKDTKF-RDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLddK 356

                         90
                 ....*....|....*..
gi 530361947 341 GSAQHSHAFLPFSGGSR 357
Cdd:cd20668  357 GQFKKSDAFVPFSIGKR 373
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 267-353 1.40e-08

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.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 55.97  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFapgsAQHS 346
Cdd:cd20645  281 DLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQALGSSEEYFEDGRQFKPERW----LQEK 355


                 ....*..
gi 530361947 347 HAFLPFS 353
Cdd:cd20645  356 HSINPFA 362
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 269-338 2.07e-08

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-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.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 55.40  E-value: 2.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 269 DQ--MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:cd20675  290 DQpnLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRF 361
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 268-357 2.40e-08

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 55.51  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAqHSH 347
Cdd:PLN02394 349 THKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA-KVE 427

                         90
                 ....*....|....*.
gi 530361947 348 A------FLPFSGGSR 357
Cdd:PLN02394 428 AngndfrFLPFGVGRR 443
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 278-355 3.72e-08

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-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.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 54.23  E-value: 3.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsAQHSHafLPFSGG 355
Cdd:cd20629  240 IEEGLRWEPPVASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-----KPKPH--LVFGGG 309
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 272-355 5.79e-08

unknown subfamily of actinobacterial 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.


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 54.00  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 272 PYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLP 351
Cdd:cd20624  242 PYLRACVLDAVRLWPTTPAVLRESTED-TVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEGLVP 320


                 ....
gi 530361947 352 FSGG 355
Cdd:cd20624  321 FSAG 324
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 280-337 6.09e-08

C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; This family contains Gaeumannomyces graminis linoleate diol synthase (LDS) and similar proteins including Ssp1 from the phytopathogenic basidiomycete Ustilago maydis. LDS, also called linoleate (8R)-dioxygenase, catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and the isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate. Ssp1 is expressed in mature teliospores, which are produced by U. maydis only after infection of its host plant, maize. Ssp1 is localized on lipid bodies in germinating teliospores, suggesting a role in the mobilization of storage lipids. LDS and Ssp1 contain an N-terminal dioxygenase domain related to animal heme peroxidases, and a C-terminal cytochrome P450 domain. The LDS-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.


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 53.88  E-value: 6.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 280 EALRLYPPVPGIGRELSTPVTFPDG----RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd20612  246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR 307
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 271-357 1.10e-07

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 53.44  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--PGSAQHSHA 348
Cdd:PLN02987 329 MPFTQCVVNETLRVANIIGGIFRRAMTDIEV-KGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQsnSGTTVPSNV 407


                 ....*....
gi 530361947 349 FLPFSGGSR 357
Cdd:PLN02987 408 FTPFGGGPR 416
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 268-357 1.29e-07

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 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.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 52.83  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHS 346
Cdd:cd20648  290 VARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHP 369

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20648  370 YASLPFGFGKR 380
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 268-357 1.85e-07

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B 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.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 52.54  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP--GSAQH 345
Cdd:cd20644  288 LTELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYH-IPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDirGSGRN 366

                         90
                 ....*....|..
gi 530361947 346 SHAfLPFSGGSR 357
Cdd:cd20644  367 FKH-LAFGFGMR 377
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 270-357 2.03e-07

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F 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.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 52.46  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHS 346
Cdd:cd20669  284 RMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFldDNGSFKKN 362

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20669  363 DAFMPFSAGKR 373
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 267-357 2.33e-07

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.


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 52.32  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKG--IMVLLSIYGLhhNPKVWPNPEVFDPFRF-APGSA 343
Cdd:cd11083  278 ALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVV-GDIALPAGtpVFLLTRAAGL--DAEHFPDPEEFDPERWlDGARA 354

                         90
                 ....*....|....*..
gi 530361947 344 QHSH---AFLPFSGGSR 357
Cdd:cd11083  355 AEPHdpsSLLPFGAGPR 371
PLN02971 PLN02971
tryptophan N-hydroxylase
 270-357 2.58e-07

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 52.35  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----Q 344
Cdd:PLN02971 385 KLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevtltE 464

                         90
                 ....*....|...
gi 530361947 345 HSHAFLPFSGGSR 357
Cdd:PLN02971 465 NDLRFISFSTGKR 477
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 271-357 2.76e-07

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of 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.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 51.76  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSH 347
Cdd:cd20667  284 LPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTM-HGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFldKDGNFVMNE 362

                         90
                 ....*....|
gi 530361947 348 AFLPFSGGSR 357
Cdd:cd20667  363 AFLPFSAGHR 372
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 268-357 2.86e-07

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 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.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 52.03  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH 347
Cdd:cd20643  290 LKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYH-IPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFR 368

                         90
                 ....*....|
gi 530361947 348 AfLPFSGGSR 357
Cdd:cd20643  369 N-LGFGFGPR 377
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 278-337 3.69e-07

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-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.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 51.45  E-value: 3.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd11032  246 IEEVLRYRPPVQRTARVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR 304
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 268-338 4.98e-07

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 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.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 51.11  E-value: 4.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVP---GIGRELSTpVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:cd11071  282 LEKMPLLKSVVYETLRLHPPVPlqyGRARKDFV-IESHDASyKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRF 355
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 268-357 5.55e-07

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 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.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 50.93  E-value: 5.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA---- 343
Cdd:cd11074  289 LHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkvea 368

                         90
                 ....*....|....*
gi 530361947 344 -QHSHAFLPFSGGSR 357
Cdd:cd11074  369 nGNDFRYLPFGVGRR 383
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 268-357 5.74e-07

flavonoid 3',5'-hydroxylase (F3'5'H); Provisional


Pssm-ID: 177725  Cd Length: 504  Bit Score: 51.01  E-value: 5.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--- 344
Cdd:PLN00110 345 LPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAkid 424

                         90
                 ....*....|....*.
gi 530361947 345 ---HSHAFLPFSGGSR 357
Cdd:PLN00110 425 prgNDFELIPFGAGRR 440
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 270-357 1.44e-06

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B 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.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 49.78  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHS 346
Cdd:cd20672  284 KMPYTDAVIHEIQRFSDLIPiGVPHRVTKDTLF-RGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGALKKS 362

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20672  363 EAFMPFSTGKR 373
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 267-357 1.69e-06

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K 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.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 49.42  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 267 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 343
Cdd:cd20664  279 HRKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFldSQGKF 357

                         90
                 ....*....|....
gi 530361947 344 QHSHAFLPFSGGSR 357
Cdd:cd20664  358 VKRDAFMPFSAGRR 371
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 278-356 2.54e-06

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-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.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 48.75  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfaPGSAQHshafLPFSGGS 356
Cdd:cd11078  257 VEETLRYDSPVQGLRRTATRDVEI-GGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNARKH----LTFGHGI 328
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 265-355 3.32e-06

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-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.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 48.32  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 265 RNHLDQMPYTtmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSaq 344
Cdd:cd20625  239 RADPELIPAA---VEELLRYDSPVQLTARVALEDVEI-GGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNRH-- 312

                         90
                 ....*....|.
gi 530361947 345 hshafLPFSGG 355
Cdd:cd20625  313 -----LAFGAG 318
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 266-355 4.60e-06

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). 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.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 47.85  E-value: 4.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQM-------PYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR- 337
Cdd:cd11080  222 NNPEQLaavradrSLVPRAIAETLRYHPPVQLIPRQASQDVVVSGME-IKKGTTVFCLIGAANRDPAAFEDPDTFNIHRe 300

                         90       100
                 ....*....|....*....|....*
gi 530361947 338 -------FAPgSAQHshafLPFSGG 355
Cdd:cd11080  301 dlgirsaFSG-AADH----LAFGSG 320
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 271-338 6.29e-06

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 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.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 47.78  E-value: 6.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:cd20677  295 LHYTEAFINEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERF 362
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 270-357 7.83e-06

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G 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.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 47.61  E-value: 7.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHS 346
Cdd:cd20670  284 KMPYTDAVIHEIQRLTDIVPlGVPHNVIRDTQF-RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQGRFKKN 362

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:cd20670  363 EAFVPFSSGKR 373
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 260-357 2.81e-05

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of 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.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 45.56  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 260 GWNCFRNHLDQ--MPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd20671  269 GPGCLPNYEDRkaLPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNH 347

                         90       100
                 ....*....|....*....|..
gi 530361947 338 F--APGSAQHSHAFLPFSGGSR 357
Cdd:cd20671  348 FldAEGKFVKKEAFLPFSAGRR 369
PLN03018 PLN03018
homomethionine N-hydroxylase
 273-357 4.35e-05

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 45.39  E-value: 4.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 273 YTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--------Q 344
Cdd:PLN03018 375 YLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGitkevtlvE 454

                         90
                 ....*....|...
gi 530361947 345 HSHAFLPFSGGSR 357
Cdd:PLN03018 455 TEMRFVSFSTGRR 467
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 271-357 5.49e-05

3-epi-6-deoxocathasterone 23-monooxygenase; Provisional


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 44.73  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHShAFL 350
Cdd:PLN03141 314 LPFTQNVITETLRMGNIINGVMRKAMKDVEI-KGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNNS-SFT 391


                 ....*..
gi 530361947 351 PFSGGSR 357
Cdd:PLN03141 392 PFGGGQR 398
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 277-334 5.78e-05

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. 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.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 44.50  E-value: 5.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530361947 277 CIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFD 334
Cdd:cd11037  249 AFEEAVRLESPVQTFSRTTTRDTEL-AGVTIPAGSRVLVFLGSANRDPRKWDDPDRFD 305
PLN02966 PLN02966
cytochrome P450 83A1
 271-357 6.60e-05

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 44.74  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 271 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHS--- 346
Cdd:PLN02966 350 LPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKgtd 429

                         90
                 ....*....|.
gi 530361947 347 HAFLPFSGGSR 357
Cdd:PLN02966 430 YEFIPFGSGRR 440
PLN02774 PLN02774
brassinosteroid-6-oxidase
 266-357 6.82e-05

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 44.38  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH 345
Cdd:PLN02774 321 NDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLES 399

                         90
                 ....*....|..
gi 530361947 346 SHAFLPFSGGSR 357
Cdd:PLN02774 400 HNYFFLFGGGTR 411
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 304-337 1.48e-04

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This 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.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 43.18  E-value: 1.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 530361947 304 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd20630  277 GVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR 310
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 270-338 2.60e-04

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 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.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 42.60  E-value: 2.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRelstpVTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 338
Cdd:cd20647  295 KLPLIRALLKETLRLFPVLPGNGR-----VTQDDlivgGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERW 362
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 270-357 2.72e-04

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D 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.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 42.76  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGS 342
Cdd:cd20663  288 RMPYTNAVIHEVQRFGDIVP-----LGVPhMTSRDievqGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldAQGH 362

                         90
                 ....*....|....*
gi 530361947 343 AQHSHAFLPFSGGSR 357
Cdd:cd20663  363 FVKPEAFMPFSAGRR 377
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 277-357 5.14e-04

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-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.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 41.50  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 277 CIKEALRLYPpvpgigrelSTPVTFP---------DGRSLPKGIMVLLSIYGLHHN-PKVWPNPEVFDPFRFA-PGSAQH 345
Cdd:cd20615  281 CVLESLRLRP---------LLAFSVPessptdkiiGGYRIPANTPVVVDTYALNINnPFWGPDGEAYRPERFLgISPTDL 351

                         90
                 ....*....|..
gi 530361947 346 SHAFLPFSGGSR 357
Cdd:cd20615  352 RYNFWRFGFGPR 363
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 268-357 6.81e-04

fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 41.53  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV-FDPFRFAP--GSAQ 344
Cdd:PLN02169 351 LEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISdnGGLR 430

                         90
                 ....*....|....*
gi 530361947 345 H--SHAFLPFSGGSR 357
Cdd:PLN02169 431 HepSYKFMAFNSGPR 445
PLN02500 PLN02500
cytochrome P450 90B1
 270-357 7.66e-04

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 41.39  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-----APGSAQ 344
Cdd:PLN02500 342 KMEFTQCVINETLRLGNVVRFLHRKALKDVRY-KGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWqqnnnRGGSSG 420

                         90
                 ....*....|....*..
gi 530361947 345 HSHA----FLPFSGGSR 357
Cdd:PLN02500 421 SSSAttnnFMPFGGGPR 437
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 268-338 8.73e-04

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 40.92  E-value: 8.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 268 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF 338
Cdd:PLN03195 368 LGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERW 439
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 266-337 1.29e-03

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 40.44  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 266 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFR 337
Cdd:PLN02426 348 EEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPER 420
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 278-337 1.69e-03

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-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.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 39.82  E-value: 1.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530361947 278 IKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd11029  259 VEELLRYDGPVAlATLRFATEDVEV-GGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR 318
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 270-343 1.73e-03

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A 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.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 40.00  E-value: 1.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 343
Cdd:cd20676  295 QLPYLEAFILETFRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltADGTE 370
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 265-337 2.07e-03

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. 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.


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 39.65  E-value: 2.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361947 265 RNHLDQMPyttMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd11079  221 RANPALLP---AAIDEILRLDDPFVANRRITTRDVEL-GGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR 289
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 268-354 2.90e-03

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 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.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 39.42  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 268 LDQMPYTTMCIKEALRL--YPPVPGIGRELSTPVtfpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH 345
Cdd:cd20627  257 IEQLRYCQQVLCETVRTakLTPVSARLQELEGKV---DQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMK 333


                 ....*....
gi 530361947 346 SHAFLPFSG 354
Cdd:cd20627  334 SFSLLGFSG 342
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 278-339 2.91e-03

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. 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.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 39.24  E-value: 2.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA 339
Cdd:cd11034  238 VEEFLRFYSPVAGLARTVTQEVEV-GGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTP 298
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 278-337 5.02e-03

AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes.


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 38.63  E-value: 5.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361947 278 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 337
Cdd:cd11036  225 VAETLRYDPPVRLERRFAAEDLEL-AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR 283
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 270-332 8.51e-03

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.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 38.05  E-value: 8.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530361947 270 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPdGRSLPKGIMVLLSIYGlhhnPKVW-PNPEV 332
Cdd:cd20622  326 RIPYLDAVIEEILRCANTAPILSREATVDTQVL-GYSIPKGTNVFLLNNG----PSYLsPPIEI 384
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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