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Conserved domains on  [gi|1370508148|ref|XP_024302220|]
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24-hydroxycholesterol 7-alpha-hydroxylase isoform X6 [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 ...
 1-349 0e+00

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 cd20635:

Pssm-ID: 477761  Cd Length: 410  Bit Score: 602.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   1 MGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRTASIPKNVFLALHEKLYIMLKGKMGTVNLHQFTGQLTEELHEQLE 80
Cdd:cd20635    21 AGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTASISKESFFEYHTKIHDMMKGKLASSNLAPLSDKLCEEFKEQLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  81 NLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEK 160
Cdd:cd20635   101 LLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLPEFFLRDWSSSKQWLLSLFEK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 161 NIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFG 240
Cdd:cd20635   181 VVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 241 KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPE 320
Cdd:cd20635   257 KAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPE 336

                         330       340
                  ....*....|....*....|....*....
gi 1370508148 321 RWKKANLEKHSFLDCFMAFGSGKFQCPAR 349
Cdd:cd20635   337 RWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 1-349 0e+00

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: 602.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   1 MGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRTASIPKNVFLALHEKLYIMLKGKMGTVNLHQFTGQLTEELHEQLE 80
Cdd:cd20635    21 AGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTASISKESFFEYHTKIHDMMKGKLASSNLAPLSDKLCEEFKEQLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  81 NLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEK 160
Cdd:cd20635   101 LLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLPEFFLRDWSSSKQWLLSLFEK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 161 NIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFG 240
Cdd:cd20635   181 VVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 241 KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPE 320
Cdd:cd20635   257 KAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPE 336

                         330       340
                  ....*....|....*....|....*....
gi 1370508148 321 RWKKANLEKHSFLDCFMAFGSGKFQCPAR 349
Cdd:cd20635   337 RWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 72-349 6.41e-30

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: 120.08  E-value: 6.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  72 TEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQ--------LPEC 142
Cdd:pfam00067 122 ARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYF 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQATLDIVETET----SKENSPNYGLLLLWAS---LSNAV 211
Cdd:pfam00067 202 PGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDALLLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 212 pvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNY 289
Cdd:pfam00067 282 ---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQNMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGY 354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSFldCFMAFGSGKFQCPAR 349
Cdd:pfam00067 355 LIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF--AFLPFGAGPRNCLGE 413
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 63-347 2.72e-14

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: 73.77  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  63 NLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQVYdedFEYGSQLPEC 142
Cdd:COG2124   106 RVAALRPRIREIADELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSDAL---LDALGPLPPE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWASL---SNAVPVAFWTL 218
Cdd:COG2124   178 RRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAGHettANALAWALYAL 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 219 ayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSGDLL 297
Cdd:COG2124   254 ---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATEDVELGGVTIPAGDRV 308

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370508148 298 MLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCP 347
Cdd:COG2124   309 LLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCL 348
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 216-347 2.83e-14

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 74.09  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:PLN03112  318 WAMAEVIKNPRVLRKIQEELDSV---VGRNRM-VQESDLVHLNYLRCVVRETFRMHpaGPFLIPHESLRATTINGYYIPA 393

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPER-W--KKANLEKHSFLDC-FMAFGSGKFQCP 347
Cdd:PLN03112  394 KTRVFINTHGLGRNTKIWDDVEEFRPERhWpaEGSRVEISHGPDFkILPFSAGKRKCP 451
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 1-349 0e+00

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: 602.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   1 MGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRTASIPKNVFLALHEKLYIMLKGKMGTVNLHQFTGQLTEELHEQLE 80
Cdd:cd20635    21 AGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTASISKESFFEYHTKIHDMMKGKLASSNLAPLSDKLCEEFKEQLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  81 NLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEK 160
Cdd:cd20635   101 LLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLPEFFLRDWSSSKQWLLSLFEK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 161 NIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFG 240
Cdd:cd20635   181 VVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 241 KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPE 320
Cdd:cd20635   257 KAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPE 336

                         330       340
                  ....*....|....*....|....*....
gi 1370508148 321 RWKKANLEKHSFLDCFMAFGSGKFQCPAR 349
Cdd:cd20635   337 RWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 1-349 7.10e-75

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: 239.19  E-value: 7.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   1 MGNRMTFVTEEEGINVFLKSKKV-DFELAVQNIVYRTASIP------------KNVFLALHEKLYIMLKGKMgtvNLHQF 67
Cdd:cd11040    20 GGQKIYVITDPELISAVFRNPKTlSFDPIVIVVVGRVFGSPesakkkegepggKGLIRLLHDLHKKALSGGE---GLDRL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  68 TGQLTEELHEQLENLGTHG-----TMDLNNLVRHLLYPVTVNMLFNKSLFSTNKkkikEFHQYFQVYDEDFEYG-SQLPE 141
Cdd:cd11040    97 NEAMLENLSKLLDELSLSGgtstvEVDLYEWLRDVLTRATTEALFGPKLPELDP----DLVEDFWTFDRGLPKLlLGLPR 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 142 CLLRNWSKSKKWFLELFEKNIPDIKAcksAKDNSMTLLQATLDI-VETETSKENSPNYGLLLLWASLSNAVPVAFWTLAY 220
Cdd:cd11040   173 LLARKAYAARDRLLKALEKYYQAARE---ERDDGSELIRARAKVlREAGLSEEDIARAELALLWAINANTIPAAFWLLAH 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 221 VLSHPDIHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP-VEILNYIIPSGDLLM 298
Cdd:cd11040   250 ILSDPELLERIREEIEPAVTPDsGTNAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDtVLGGGYLLRKGSLVM 329

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 299 LSPFWLHRNPKYF-PEPELFKPERWKKANLEK--HSFLDCFMAFGSGKFQCPAR 349
Cdd:cd11040   330 IPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKkgRGLPGAFRPFGGGASLCPGR 383
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 63-350 1.15e-33

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: 129.56  E-value: 1.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  63 NLHQFTGQLTEELHEQLENLGTHGTMDLNnlVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPEC 142
Cdd:cd00302    74 ALAALRPVIREIARELLDRLAAGGEVGDD--VADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLLRPLP 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWS--KSKKWFLELFEKNIpdiKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAVPVAFWTLAY 220
Cdd:cd00302   152 SPRLRRlrRARARLRDYLEELI---ARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYL 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 221 VLSHPDIHKAIMEGISSVFGKAgkdkikvSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLML 299
Cdd:cd00302   229 LARHPEVQERLRAEIDAVLGDG-------TPEDLSKLPYLEAVVEETLRLYPPvPLLPRVATEDVELGGYTIPAGTLVLL 301

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 300 SPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldCFMAFGSGKFQCPARK 350
Cdd:cd00302   302 SLYAAHRDPEVFPDPDEFDPERFLPEREEPRY---AHLPFGAGPHRCLGAR 349
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 72-349 6.41e-30

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: 120.08  E-value: 6.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  72 TEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQ--------LPEC 142
Cdd:pfam00067 122 ARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYF 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQATLDIVETET----SKENSPNYGLLLLWAS---LSNAV 211
Cdd:pfam00067 202 PGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDALLLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 212 pvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNY 289
Cdd:pfam00067 282 ---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQNMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGY 354

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSFldCFMAFGSGKFQCPAR 349
Cdd:pfam00067 355 LIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF--AFLPFGAGPRNCLGE 413
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 1-347 4.89e-25

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: 105.76  E-value: 4.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   1 MGNRMTFVTEEEGINVFLKSKkvDFELAVQNiVYR---TASIPKNVFLAL---HEKLYIMLKGKMGTVNLHQFTGQLTEE 74
Cdd:cd11042    14 LGKKVTVLLGPEANEFFFNGK--DEDLSAEE-VYGfltPPFGGGVVYYAPfaeQKEQLKFGLNILRRGKLRGYVPLIVEE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  75 LHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNkkkikeFHQYFQVYdEDFEYGSQLPECLLRNWS------ 148
Cdd:cd11042    91 VEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELL------DDEFAQLY-HDLDGGFTPIAFFFPPLPlpsfrr 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 149 --KSKKWFLELFEKNIPDIKACKSAKDNSMtlLQATLDIV---ETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLS 223
Cdd:cd11042   164 rdRARAKLKEIFSEIIQKRRKSPDKDEDDM--LQTLMDAKykdGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 224 HPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN--YIIPSGDLLMLS 300
Cdd:cd11042   242 NPEHLEALREEQKEVLGDGDDP---LTYDVLKEMPLLHACIKETLRLHPPIHsLMRKARKPFEVEGggYVIPKGHIVLAS 318

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370508148 301 PFWLHRNPKYFPEPELFKPERWKKANLE---KHSFldCFMAFGSGKFQCP 347
Cdd:cd11042   319 PAVSHRDPEIFKNPDEFDPERFLKGRAEdskGGKF--AYLPFGAGRHRCI 366
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 2-349 5.16e-23

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 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: 410725  Cd Length: 438  Bit Score: 100.07  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148   2 GNRMTFVTEE-EGINVFLKSKKVDFELAVQNIVYRTASIP---KNVFLALHEKL---YIMLKGKMGTVNLHQFTGQLTEE 74
Cdd:cd20632    19 GKYITFIMDPfLYPYVIKHGKQLDFHEFSDRLASKTFGYPplrSPKFPGLNEQIhrsYQYLQGENLDILTESMMGNLQLV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  75 LHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEY-GSQLPECLLRNWSKSKKW 153
Cdd:cd20632    99 LRQQFLGETDWETEELYEFCSRIMFEATFLTLYGKPPDDDRHKVISELRKKFRKFDAMFPYlVANIPIELLGATKSIREK 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 154 FLELFEKNipdikacKSAK-DNSMTLLQATLDIVEtetskenspNYGLL-----------LLWASLSNAVPVAFWTLAYV 221
Cdd:cd20632   179 LIKYFLPQ-------KMAKwSNPSEVIQARQELLE---------QYDVLqdydkaahhfaFLWASVGNTIPATFWAMYYL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 222 LSHPDIHKAIMEGISSVFGKAGKDK-----IKVSEDDLENLLLIKWCVLETIRLKAPGVITRkVVKPVEILN------YI 290
Cdd:cd20632   243 LRHPEALAAVRDEIDHVLQSTGQELgpdfdIHLTREQLDSLVYLESAINESLRLSSASMNIR-VVQEDFTLKlesdgsVN 321

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 291 IPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSF------LDCF-MAFGSGKFQCPAR 349
Cdd:cd20632   322 LRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFykrgqkLKYYlMPFGSGSSKCPGR 387
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 53-350 5.58e-23

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: 99.91  E-value: 5.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  53 IMLKGKmgtvNLHQFTGQL---TEELHEQLENLGTHGTMDLNNLvRHLLY----PVTVNMLFNKSLFSTNKKKIKEFHQY 125
Cdd:cd11054    76 PLLRPK----SVASYLPAInevADDFVERIRRLRDEDGEEVPDL-EDELYkwslESIGTVLFGKRLGCLDDNPDSDAQKL 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 126 FQVYDEDFEYGSQL----PEC----------LLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLdiveteTS 191
Cdd:cd11054   151 IEAVKDIFESSAKLmfgpPLWkyfptpawkkFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDSLLEYLL------SK 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 192 KENSPN--YGLL--LLWASL---SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCV 264
Cdd:cd11054   225 PGLSKKeiVTMAldLLLAGVdttSNTLAFLLYHLA---KNPEVQEKLYEEIRSVLP----DGEPITAEDLKKMPYLKACI 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 265 LETIRLK--APGvITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcFMAF 339
Cdd:cd11054   298 KESLRLYpvAPG-NGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrdDSENKNIHPFA--SLPF 374

                         330
                  ....*....|.
gi 1370508148 340 GSGKFQCPARK 350
Cdd:cd11054   375 GFGPRMCIGRR 385
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 216-346 4.13e-21

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: 94.18  E-value: 4.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 293
Cdd:cd20620   234 WTW-YLLAqHPEVAARLRAEVDRVLGGR-----PPTAEDLPQLPYTEMVLQESLRLYPPAwIIGREAVEDDEIGGYRIPA 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQC 346
Cdd:cd20620   308 GSTVLISPYVTHRDPRFWPDPEAFDPERFtPEREAARPRY--AYFPFGGGPRIC 359
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 198-349 6.11e-21

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 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: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 93.97  E-value: 6.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 198 YGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKD-KIKVSEDDLENLLLIKWCVL-----ETIRLK 271
Cdd:cd20633   228 FMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEvKPGGPLINLTRDMLLKTPVLdsaveETLRLT 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 272 APGVITRKVVKPVEIL-----NYIIPSGDLLMLSPFW-LHRNPKYFPEPELFKPERWKKANL-EKHSFLD-------CFM 337
Cdd:cd20633   308 AAPVLIRAVVQDMTLKmangrEYALRKGDRLALFPYLaVQMDPEIHPEPHTFKYDRFLNPDGgKKKDFYKngkklkyYNM 387

                         170
                  ....*....|..
gi 1370508148 338 AFGSGKFQCPAR 349
Cdd:cd20633   388 PWGAGVSICPGR 399
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 201-347 1.54e-20

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: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 201 LLLWASLSNAVPVAfWTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITR 278
Cdd:cd11049   228 LLTAGTETTASTLA-WAF-HLLArHPEVERRLHAELDAVLGGR-----PATFEDLPRLTYTRRVVTEALRLYPPVwLLTR 300

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 279 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcfmAFGSGKFQCP 347
Cdd:cd11049   301 RTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWlpgRAAAVPRGAFI----PFGAGARKCI 368
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 216-342 5.00e-20

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: 91.05  E-value: 5.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 293
Cdd:cd20628   251 FTL-YLLGlHPEVQEKVYEELDEIFGD---DDRRPTLEDLNKMKYLERVIKETLRLYPSVpFIGRRLTEDIKLDGYTIPK 326

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSG 342
Cdd:cd20628   327 GTTVVISIYALHRNPEYFPDPEKFDPDRFlPENSAKRHPY--AYIPFSAG 374
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 79-348 6.19e-20

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: 91.08  E-value: 6.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  79 LENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFE------YGSQLP--ECLLRNWSKS 150
Cdd:cd20618    97 LEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFElagafnIGDYIPwlRWLDLQGYEK 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 151 K-----KWFLELFEKNIPDIKACKSAKDNSMTLLQaTLDIVETETSKENSPN---YGLL---LLWASLSNAVPVAfWTLA 219
Cdd:cd20618   177 RmkklhAKLDRFLQKIIEEHREKRGESKKGGDDDD-DLLLLLDLDGEGKLSDdniKALLldmLAAGTDTSAVTIE-WAMA 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 220 YVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLL 297
Cdd:cd20618   255 ELLRHPEVMRKAQEELDSV---VGRERL-VEESDLPKLPYLQAVVKETLRLHPPGplLLPHESTEDCKVAGYDIPAGTRV 330

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 298 MLSPFWLHRNPKYFPEPELFKPERWKKANLEK---HSFldCFMAFGSGKFQCPA 348
Cdd:cd20618   331 LVNVWAIGRDPKVWEDPLEFKPERFLESDIDDvkgQDF--ELLPFGSGRRMCPG 382
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 218-346 6.83e-19

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: 87.64  E-value: 6.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 218 LAYVLS-HPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSGD 295
Cdd:cd11055   249 ASYLLAtNPDVQEKLIEEIDEVLPDDGS----PTYDTVSKLKYLDMVINETLRLYPPAfFISRECKEDCTINGVFIPKGV 324

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 296 LLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQC 346
Cdd:cd11055   325 DVVIPVYAIHHDPEFWPDPEKFDPERFsPENKAKRHPY--AYLPFGAGPRNC 374
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 163-348 1.89e-18

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: 86.53  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 163 PDIKACK-------SAKDNSMTLLQATLDIVETEtsKENSPNYG--LLLLWASLSNA---VPVAF-WTLAYVLSHPDIHK 229
Cdd:cd11075   189 PLIRARRkrrasgeADKDYTDFLLLDLLDLKEEG--GERKLTDEelVSLCSEFLNAGtdtTATALeWAMAELVKNPEIQE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 230 AIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLLMLSPFWLHRN 307
Cdd:cd11075   267 KLYEEIKEVVGDEAV----VTEEDLPKMPYLKAVVLETLRRHPPGhfLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRD 342

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370508148 308 PKYFPEPELFKPERWkkANLEKHSFLDC------FMAFGSGKFQCPA 348
Cdd:cd11075   343 PKVWEDPEEFKPERF--LAGGEAADIDTgskeikMMPFGAGRRICPG 387
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 104-347 2.35e-18

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: 86.11  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 104 NMLFNKSLFSTNKKKIKEFHQYFqvyDEDFEYGSQLPEC---------LLRNWSKSKKWF---LELFEKNIPDIKAcKSA 171
Cdd:cd20617   120 QFLFGKRFPDEDDGEFLKLVKPI---EEIFKELGSGNPSdfipillpfYFLYLKKLKKSYdkiKDFIEKIIEEHLK-TID 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 172 KDNSMTLLQATLDIVETETSKENSPNYGLLLLWASL--------SNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGKAG 243
Cdd:cd20617   196 PNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLflagtdttSTTL---EWFLLYLANNPEIQEKIYEEIDNVVGNDR 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 244 KDKIKvsedDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 321
Cdd:cd20617   273 RVTLS----DRSKLPYLNAVIKEVLRLRPILPLGlpRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPER 348

                         250       260
                  ....*....|....*....|....*.
gi 1370508148 322 WKKANLEKHSflDCFMAFGSGKFQCP 347
Cdd:cd20617   349 FLENDGNKLS--EQFIPFGIGKRNCV 372
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 216-346 4.71e-18

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: 85.38  E-value: 4.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLA----YVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGVITR--KVV--KPVEIL 287
Cdd:cd11062   242 RTLSvatfHLLSNPEILERLREELKTAMPD---PDSPPSLAELEKLPYLTAVIKEGLRL-SYGVPTRlpRVVpdEGLYYK 317

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 288 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKhsfldCFMAFGSGKFQC 346
Cdd:cd11062   318 GWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgaaEKGKLDR-----YLVPFSKGSRSC 375
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 151-347 5.76e-18

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: 84.96  E-value: 5.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 151 KKWFLELFEKNIPDI-----------------KACKSAKDNSMTLLQATLDIVETETS-----KENSPNYGLLLLWASLS 208
Cdd:cd20655   163 KKLDLQGFGKRIMDVsnrfdelleriikeheeKRKKRKEGGSKDLLDILLDAYEDENAeykitRNHIKAFILDLFIAGTD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 209 NAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEIL 287
Cdd:cd20655   243 TSAATTEWAMAELINNPEVLEKAREEIDSV---VGKTRL-VQESDLPNLPYLQAVVKETLRLHPPGpLLVRESTEGCKIN 318

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 288 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWkKANLEKHSFLDC------FMAFGSGKFQCP 347
Cdd:cd20655   319 GYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERF-LASSRSGQELDVrgqhfkLLPFGSGRRGCP 383
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 70-350 1.55e-17

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: 83.96  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  70 QLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKK----IKEFHQYFQVYDE-DFEYGSQLPECL- 143
Cdd:cd20658    91 NLVAYVYNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEDggpgLEEVEHMDAIFTAlKCLYAFSISDYLp 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 144 -LRNWSkskkwfLELFEKNIPD----IKAC---------KSAKDNSMTLLQATLDIVETETSKENSPnygLL-------- 201
Cdd:cd20658   171 fLRGLD------LDGHEKIVREamriIRKYhdpiideriKQWREGKKKEEEDWLDVFITLKDENGNP---LLtpdeikaq 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 202 ---LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVI 276
Cdd:cd20658   242 ikeLMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRV---VGKERL-VQESDIPNLNYVKACAREAFRLHpvAPFNV 317

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 277 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE----KHSFLdcFMAFGSGKFQCPARK 350
Cdd:cd20658   318 PHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtltEPDLR--FISFSTGRRGCPGVK 393
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 216-342 5.12e-17

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: 82.25  E-value: 5.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikvsEDDLENLLLIKWCVLETIRLKAPGVIT-RKVVKPVEILNYIIPSG 294
Cdd:cd11053   245 WAFYWLHRHPEVLARLLAELDALGGDPD-------PEDIAKLPYLDAVIKETLRLYPVAPLVpRRVKEPVELGGYTLPAG 317

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370508148 295 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSG 342
Cdd:cd11053   318 TTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSPYE----YLPFGGG 361
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 216-347 8.36e-17

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: 81.50  E-value: 8.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDI-HKAIMEgISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 292
Cdd:cd20653   249 WAMSNLLNHPEVlKKAREE-IDT---QVGQDRL-IEESDLPKLPYLQNIISETLRLYpaAPLLVPHESSEDCKIGGYDIP 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 293 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSGKFQCP 347
Cdd:cd20653   324 RGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK----LIPFGLGRRACP 374
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 217-348 1.71e-16

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: 80.66  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVL----SHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEI--LNY 289
Cdd:cd11056   248 TLSFALyelaKNPEIQEKLREEIDEVLEKHGG---ELTYEALQEMKYLDQVVNETLRKYPPlPFLDRVCTKDYTLpgTDV 324

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPA 348
Cdd:cd11056   325 VIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKrHPY--TYLPFGDGPRNCIG 382
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 216-346 1.85e-16

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: 80.77  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 293
Cdd:cd20660   254 WALYLIGSHPEVQEKVHEELDRIFGD---SDRPATMDDLKEMKYLECVIKEALRL-FPSVpmFGRTLSEDIEIGGYTIPK 329

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 346
Cdd:cd20660   330 GTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrHPY--AYIPFSAGPRNC 381
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 126-349 1.89e-16

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 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: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 80.50  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 126 FQVYDEDF-EYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLD-IVETETSKENspnygLLLL 203
Cdd:cd20631   162 FKEFDKVFpALVAGLPIHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLStLDEMEKARTH-----VAML 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 204 WASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGK------DKIKVSEDDLENLLLIKWCVLETIRLKAPGVIT 277
Cdd:cd20631   237 WASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQkvsdggNPIVLTREQLDDMPVLGSIIKEALRLSSASLNI 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 278 RKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--------FMAFGSGKF 344
Cdd:cd20631   317 RVAKEDFTLHldsgeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKngrklkyyYMPFGSGTS 396


                  ....*
gi 1370508148 345 QCPAR 349
Cdd:cd20631   397 KCPGR 401
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 214-331 3.61e-16

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: 79.87  E-value: 3.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 214 AFwTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLlliKW--CVL-ETIRLKAP-GVITRKVVKPVEILNY 289
Cdd:cd20613   255 SF-TLLELGRHPEILKRLQAEVDEVLG----SKQYVEYEDLGKL---EYlsQVLkETLRLYPPvPGTSRELTKDIELGGY 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHS 331
Cdd:cd20613   327 KIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIP 368
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 216-346 4.92e-16

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: 79.33  E-value: 4.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEI--LNYIIP 292
Cdd:cd11046   262 WTLYELSQNPELMAKVQAEVDAVLG----DRLPPTYEDLKKLKYTRRVLNESLRLyPQPPVLIRRAVEDDKLpgGGVKVP 337

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 293 SGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLD-CFMAFGSGKFQC 346
Cdd:cd11046   338 AGTDIFISVYNLHRSPELWEDPEEFDPERFldPFINPPNEVIDDfAFLPFGGGPRKC 394
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 216-347 8.71e-16

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: 78.61  E-value: 8.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVfgkaGKDKIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 293
Cdd:cd20652   256 WFLLYMALFPKEQRRIQRELDEV----VGRPDLVTLEDLSSLPYLQACISESQRIRSvvPLGIPHGCTEDAVLAGYRIPK 331

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFldcFMAFGSGKFQCP 347
Cdd:cd20652   332 GSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEA---FIPFQTGKRMCL 384
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 216-350 2.13e-15

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: 77.31  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPS 293
Cdd:cd11069   257 WAL-YLLAkHPDVQERLREEIRAA--LPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPvPLTSREATKDTVIKGVPIPK 333

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 294 GDLLMLSPFWLHRNPK-YFPEPELFKPERW-----KKANLEKHSFlDCFMAFGSGKFQCPARK 350
Cdd:cd11069   334 GTVVLIPPAAINRSPEiWGPDAEEFNPERWlepdgAASPGGAGSN-YALLTFLHGPRSCIGKK 395
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 216-348 2.81e-15

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: 77.12  E-value: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDI-HKAIMEgISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 292
Cdd:cd11072   250 WAMTELIRNPRVmKKAQEE-VREVVG----GKGKVTEEDLEKLKYLKAVIKETLRLHppAPLLLPRECREDCKINGYDIP 324

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 293 SGDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCPA 348
Cdd:cd11072   325 AKTRVIVNAWAIGRDPKYWEDPEEFRPER----------FLDSsidfkgqdfeLIPFGAGRRICPG 380
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 217-346 3.58e-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: 76.68  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVL----SHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP-VEILNYII 291
Cdd:cd20650   247 TLSFLLyelaTHPDVQQKLQEEIDAVL----PNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKdVEINGVFI 322

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 292 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQC 346
Cdd:cd20650   323 PKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPY-IYLPFGSGPRNC 376
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 216-348 4.24e-15

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: 76.50  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPS 293
Cdd:cd20654   263 WALSLLLNNPHVLKKAQEELDT---HVGKDRW-VEESDIKNLVYLQAIVKETLRLYPPGPLLgpREATEDCTVGGYHVPK 338

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFLdcFMAFGSGKFQCPA 348
Cdd:cd20654   339 GTRLLVNVWKIQRDPNVWSDPLEFKPERFltthKDIDVRGQNFE--LIPFGSGRRSCPG 395
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 216-347 4.71e-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: 76.42  E-value: 4.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd11073   253 WAMAELLRNPEKMAKARAELDEVIGK---DKI-VEESDISKLPYLQAVVKETLRLHppAPLLLPRKAEEDVEVMGYTIPK 328

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCP 347
Cdd:cd11073   329 GTQVLVNVWAIGRDPSVWEDPLEFKPER----------FLGSeidfkgrdfeLIPFGSGRRICP 382
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 216-350 6.17e-15

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: 75.82  E-value: 6.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdKIKVSEDDLENLLLIKWCVLETIRLK--APgVITRKVVKPVEILNYIIPS 293
Cdd:cd11083   244 WMLYYLASRPDVQARVREEVDAVLGGA---RVPPLLEALDRLPYLEAVARETLRLKpvAP-LLFLEPNEDTVVGDIALPA 319

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 294 GD--LLMLSPFWLhrNPKYFPEPELFKPERW--KKANLEKHSFLDcFMAFGSGKFQCPARK 350
Cdd:cd11083   320 GTpvFLLTRAAGL--DAEHFPDPEEFDPERWldGARAAEPHDPSS-LLPFGAGPRLCPGRS 377
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 217-346 6.30e-15

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: 75.82  E-value: 6.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLS-HPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 294
Cdd:cd11045   233 SMAYFLArHPEWQERLREESLAL------GKGTLDYEDLGQLEVTDWVFKEALRLVPPvPTLPRRAVKDTEVLGYRIPAG 306

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 295 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLdcFMAFGSGKFQC 346
Cdd:cd11045   307 TLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEdkVHRYA--WAPFGGGAHKC 358
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 216-346 9.35e-15

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: 75.37  E-value: 9.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd20621   251 MCLYYLAKYPEIQEKLRQEIKSVV----GNDDDITFEDLQKLNYLNAFIKEVLRLYnpAPFLFPRVATQDHQIGDLKIKK 326

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQC 346
Cdd:cd20621   327 GWIVNVGYIYNHFNPKYFENPDEFNPERWlNQNNIEDNPFV--FIPFSAGPRNC 378
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 66-347 9.85e-15

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: 75.29  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  66 QFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNkslfSTNKKKIKEFHQYFQvydeDFEYGS-QLPECLL 144
Cdd:cd11043    82 RLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLG----IDPEEVVEELRKEFQ----AFLEGLlSFPLNLP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 145 -----RNWsKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSK---ENSPNYGLLLLWASLSNAVPVAFW 216
Cdd:cd11043   154 gttfhRAL-KARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGDSltdEEILDNILTLLFAGHETTSTTLTL 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLSHPDI-------HKAIMegissvfgKAGKDKIKVSEDDLENLlliK--WCV-LETIRLK--APGVItRKVVKPV 284
Cdd:cd11043   233 AVKFLAENPKVlqelleeHEEIA--------KRKEEGEGLTWEDYKSM---KytWQViNETLRLApiVPGVF-RKALQDV 300

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 285 EILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhSFldCFMAFGSGKFQCP 347
Cdd:cd11043   301 EYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV-PY--TFLPFGGGPRLCP 360
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 216-346 1.04e-14

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: 75.18  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 293
Cdd:cd20680   265 WSLYLLGSHPEVQRKVHKELDEVFGKSDR---PVTMEDLKKLRYLECVIKESLRL-FPSVplFARSLCEDCEIRGFKVPK 340

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 346
Cdd:cd20680   341 GVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrHPY--AYIPFSAGPRNC 392
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 70-347 1.50e-14

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: 74.56  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  70 QLTEELHEQLENLgthgtmdLNNLVRHLLYPVTVNMLFNKSL------------FSTNKKKIKE----FHQYFQVYDEDF 133
Cdd:cd20651    79 SMEEVIQEEAEEL-------IDLLKKGEKGPIQMPDLFNVSVlnvlwamvagerYSLEDQKLRKllelVHLLFRNFDMSG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 134 EYGSQLPecLLR----NWSK------SKKWFLELFEKNIPDIKAcKSAKDNSMTLLQATLDIVETETSKENSPNY----- 198
Cdd:cd20651   152 GLLNQFP--WLRfiapEFSGynllveLNQKLIEFLKEEIKEHKK-TYDEDNPRDLIDAYLREMKKKEPPSSSFTDdqlvm 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 199 GLL-LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLK--APGV 275
Cdd:cd20651   229 ICLdLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGR---DRLP-TLDDRSKLPYTEAVILEVLRIFtlVPIG 304

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 276 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDCFMAFGSGKFQCP 347
Cdd:cd20651   305 IPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDED-GKLLKDEWFLPFGAGKRRCL 375
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 47-355 2.44e-14

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: 74.17  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  47 LHEKLyIMLKGKMGTVNLHQFTGQLTEELHEQLENLGTHG--TMDLNNLVRHLLYPVTVNMLFNKSlFSTNKKKIKEFHQ 124
Cdd:cd11027    64 LHRKL-AHSALRLYASGGPRLEEKIAEEAEKLLKRLASQEgqPFDPKDELFLAVLNVICSITFGKR-YKLDDPEFLRLLD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 125 YFQVYDEDFEYGSQ---------LPECLLRNWSKSKKWFLELFEK------------NIPDIkacksakdnSMTLLQATL 183
Cdd:cd11027   142 LNDKFFELLGAGSLldifpflkyFPNKALRELKELMKERDEILRKkleehketfdpgNIRDL---------TDALIKAKK 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 184 DIvetetSKENSPNYGLL-----------LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSED 252
Cdd:cd11027   213 EA-----EDEGDEDSGLLtddhlvmtisdIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGR---DRLP-TLS 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 253 DLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKH 330
Cdd:cd11027   284 DRKRLPYLEATIAEVLRLSsvVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLV 363

                         330       340
                  ....*....|....*....|....*
gi 1370508148 331 SFLDCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd11027   364 PKPESFLPFSAGRRVCLGESLAKAE 388
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 63-347 2.72e-14

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: 73.77  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  63 NLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQVYdedFEYGSQLPEC 142
Cdd:COG2124   106 RVAALRPRIREIADELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSDAL---LDALGPLPPE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWASL---SNAVPVAFWTL 218
Cdd:COG2124   178 RRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAGHettANALAWALYAL 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 219 ayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSGDLL 297
Cdd:COG2124   254 ---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATEDVELGGVTIPAGDRV 308

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370508148 298 MLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCP 347
Cdd:COG2124   309 LLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCL 348
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 216-347 2.83e-14

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 74.09  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:PLN03112  318 WAMAEVIKNPRVLRKIQEELDSV---VGRNRM-VQESDLVHLNYLRCVVRETFRMHpaGPFLIPHESLRATTINGYYIPA 393

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPER-W--KKANLEKHSFLDC-FMAFGSGKFQCP 347
Cdd:PLN03112  394 KTRVFINTHGLGRNTKIWDDVEEFRPERhWpaEGSRVEISHGPDFkILPFSAGKRKCP 451
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 216-349 3.07e-14

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: 73.90  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPGVI---TRKVVKPVEILNYIIP 292
Cdd:cd11076   246 WIMARMVLHPDIQSKAQAEIDAAVGGSRR----VADSDVAKLPYLQAVVKETLRLHPPGPLlswARLAIHDVTVGGHVVP 321

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 293 SGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFL--DCFMA-FGSGKFQCPAR 349
Cdd:cd11076   322 AGTTAMVNMWAITHDPHVWEDPLEFKPERFvAAEGGADVSVLgsDLRLApFGAGRRVCPGK 382
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 200-350 6.31e-14

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. 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: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 72.87  E-value: 6.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 200 LLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDK---IKVSEDDLENLLLIKWCVLETIRLKAPGVI 276
Cdd:cd20634   227 LLQLWATQGNAGPAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVsqtLTINQELLDNTPVFDSVLSETLRLTAAPFI 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 277 TRKVVKPVEIL-----NYIIPSGDLLMLSPFWL-HRNPKYFPEPELFKPERWKKA-NLEKHSF------LDCF-MAFGSG 342
Cdd:cd20634   307 TREVLQDMKLRladgqEYNLRRGDRLCLFPFLSpQMDPEIHQEPEVFKYDRFLNAdGTEKKDFykngkrLKYYnMPWGAG 386


                  ....*...
gi 1370508148 343 KFQCPARK 350
Cdd:cd20634   387 DNVCIGRH 394
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 61-346 6.81e-14

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: 72.70  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  61 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLfnksLFSTNKKKIKEFHQYFQVYDED-FEYGSQL 139
Cdd:cd11044    92 REALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLL----LGLDPEVEAEALSQDFETWTDGlFSLPVPL 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 140 PECLLRNWSKSKKWFLELFEKNIPDIKAC--KSAKDNSMTLLQATLDIVE---TETSKENSpnygLLLLWASLSNAVPVA 214
Cdd:cd11044   168 PFTPFGRAIRARNKLLARLEQAIRERQEEenAEAKDALGLLLEAKDEDGEplsMDELKDQA----LLLLFAGHETTASAL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 215 FWTLAYVLSHPDIHKAImegissvfgKAGKDKIKVSED-DLENLLLIKW--CVL-ETIRLKAP-GVITRKVVKPVEILNY 289
Cdd:cd11044   244 TSLCFELAQHPDVLEKL---------RQEQDALGLEEPlTLESLKKMPYldQVIkEVLRLVPPvGGGFRKVLEDFELGGY 314

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQC 346
Cdd:cd11044   315 QIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPREC 371
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 217-346 7.43e-14

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: 72.72  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRkVVKP--VEILN 288
Cdd:cd11059   240 TLTYliweLSRPPNLQEKLREELAGLPGPFRGP---PDLEDLDKLPYLNAVIRETLRLYPpiPGSLPR-VVPEggATIGG 315

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 289 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN----LEKHSFldcFMAFGSGKFQC 346
Cdd:cd11059   316 YYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSgetaREMKRA---FWPFGSGSRMC 374
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 197-346 7.50e-14

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: 72.47  E-value: 7.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 197 NYGLLLLWASLSNAVPVAfWTLAYVLSHPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GV 275
Cdd:cd20614   212 NLRLLVLAGHETTASIMA-WMVIMLAEHPAVWDALCDEAAAA------GDVPRTPAELRRFPLAEALFRETLRLHPPvPF 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 276 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDcFMAFGSGKFQC 346
Cdd:cd20614   285 VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRD-RAPNPVE-LLQFGGGPHFC 353
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 139-349 1.18e-13

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: 71.84  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 139 LPECLLRNW-SKSKKWF---LELFEKNIPDIK---ACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAV 211
Cdd:cd11065   162 LPSWLGAPWkRKARELReltRRLYEGPFEAAKermASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTAS 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 212 PVAFWTLAYVLsHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNY 289
Cdd:cd11065   242 TLQTFILAMAL-HPEVQKKAQEELDRV---VGPDRL-PTFEDRPNLPYVNAIVKEVLRWRpvAPLGIPHALTEDDEYEGY 316

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC-FMAFGSGKFQCPAR 349
Cdd:cd11065   317 FIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPpHFAFGFGRRICPGR 377
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 217-349 2.13e-13

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: 71.10  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKvSEDDLENLLLIKWCVLETIRLK--APGVITRKVVK-PVEILNYIIPS 293
Cdd:cd11061   239 IFYYLARNPEAYEKLRAELDSTF--PSDDEIR-LGPKLKSLPYLRACIDEALRLSppVPSGLPRETPPgGLTIDGEYIPG 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHsfLDCFMAFGSGKFQCPAR 349
Cdd:cd11061   316 GTTVSVPIYSIHRDERYFPDPFEFIPERWlsRPEELVRA--RSAFIPFSIGPRGCIGK 371
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 208-355 2.46e-13

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: 71.03  E-value: 2.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 208 SNAVPVAFwTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 286
Cdd:cd20644   247 TTAFPLLF-TLFELARNPDVQQILRQESLAAAAQISEHPQKA----LTELPLLKAALKETLRLYPVGItVQRVPSSDLVL 321

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 287 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARKTNRKE 355
Cdd:cd20644   322 QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH--LAFGFGMRQCLGRRLAEAE 388
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 216-333 2.50e-13

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: 71.05  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 294
Cdd:cd20659   249 WTLYSLAKHPEHQQKCREEVDEVLG----DRDDIEWDDLSKLPYLTMCIKESLRLYPPvPFIARTLTKPITIDGVTLPAG 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370508148 295 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK---HSFL 333
Cdd:cd20659   325 TLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKrdpFAFI 366
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 216-347 2.76e-13

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 71.30  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 293
Cdd:PLN02394  315 WGIAELVNHPEIQKKLRDELDTVLGPGNQ----VTEPDTHKLPYLQAVVKETLRLHMaiPLLVPHMNLEDAKLGGYDIPA 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLDCFMAFGSGKFQCP 347
Cdd:PLN02394  391 ESKILVNAWWLANNPELWKNPEEFRPERFleEEAKVEANGNDFRFLPFGVGRRSCP 446
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 153-350 3.80e-13

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: 70.44  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 153 WFLELFEKniPDIKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWAS----------------LSNAVpvaFW 216
Cdd:cd11070   157 PFLDRLPW--VLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASrlkrarrsggltekelLGNLF---IF 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLA-------------YVLS-HPDIHKAIMEGISSVFGKAGKDKIKvsEDDLENLLLIKWCVLETIRLKAP-GVITRKVV 281
Cdd:cd11070   232 FIAghettantlsfalYLLAkHPEVQDWLREEIDSVLGDEPDDWDY--EEDFPKLPYLLAVIYETLRLYPPvQLLNRKTT 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 282 KPVEILN-----YIIPSGDLLMLSPFWLHRNPKY-FPEPELFKPERW-----KKANLEKHSFLDC-FMAFGSGKFQCPAR 349
Cdd:cd11070   310 EPVVVITglgqeIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWgstsgEIGAATRFTPARGaFIPFSAGPRACLGR 389


                  .
gi 1370508148 350 K 350
Cdd:cd11070   390 K 390
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 216-355 8.37e-13

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: 69.25  E-value: 8.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd11028   253 WSLLYMIRYPEIQEKVQAELDRVIGRERLPRL----SDRPNLPYTEAFILETMRHSsfVPFTIPHATTRDTTLNGYFIPK 328

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKhSFLDCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd11028   329 GTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDK-TKVDKFLPFGAGRRRCLGEELARME 391
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 216-357 1.38e-12

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: 68.63  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKA--PG---VITRKvvkPVEILNY 289
Cdd:cd20648   256 WSL-YELSrHPDVQTALHREITAAL----KDNSVPSAADVARMPLLKAVVKEVLRLYPviPGnarVIPDR---DIQVGEY 327

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARKTNRKEQH 357
Cdd:cd20648   328 IIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHHPYAS--LPFGFGKRSCIGRRIAELEVY 393
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 217-349 2.98e-12

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: 67.61  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLSHPDIHKAIMEGISSvFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKP--VEILNYIIPS 293
Cdd:cd11060   245 ILYYLLKNPRVYAKLRAEIDA-AVAEGKLSSPITFAEAQKLPYLQAVIKEALRLHPPvGLPLERVVPPggATICGRFIPG 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEKHSFLD-CFMAFGSGKFQCPAR 349
Cdd:cd11060   324 GTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRRMMDrADLTFGAGSRTCLGK 381
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 216-357 4.29e-12

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: 67.05  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 294
Cdd:cd20643   256 WTLYELARNPNVQEMLRAEVLAARQEAQGDMVKM----LKSVPLLKAAIKETLRLHPVAVsLQRYITEDLVLQNYHIPAG 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 295 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCPARKTNRKEQH 357
Cdd:cd20643   332 TLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNL----GFGFGPRQCLGRRIAETEMQ 390
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 217-350 4.50e-12

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: 67.24  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVL----SHPDIHKAIMEGISSVFGKAGkdkIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YI 290
Cdd:cd11057   246 TVAYTLlllaMHPEVQEKVYEEIMEVFPDDG---QFITYEDLQQLVYLEMVLKETMRLFPVGpLVGRETTADIQLSNgVV 322

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 291 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARK 350
Cdd:cd11057   323 IPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrHPY--AFIPFSAGPRNCIGWR 382
PLN02966 PLN02966
cytochrome P450 83A1
 188-350 8.82e-12

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 66.69  E-value: 8.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 188 TETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkIKVSEDDLENLLLIKWCVLET 267
Cdd:PLN02966  283 SEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGS--TFVTEDDVKNLPYFRALVKET 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 268 IRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKF 344
Cdd:PLN02966  361 LRIEPviPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKeWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRR 440


                  ....*.
gi 1370508148 345 QCPARK 350
Cdd:PLN02966  441 MCPGMR 446
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 216-347 1.30e-11

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: 65.96  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 293
Cdd:cd11074   255 WGIAELVNHPEIQKKLRDELDTVLGPG----VQITEPDLHKLPYLQAVVKETLRLRMaiPLLVPHMNLHDAKLGGYDIPA 330

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLDC------FMAFGSGKFQCP 347
Cdd:cd11074   331 ESKILVNAWWLANNPAHWKKPEEFRPERF----LEEESKVEAngndfrYLPFGVGRRSCP 386
PLN02183 PLN02183
ferulate 5-hydroxylase
 216-347 1.60e-11

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 65.64  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 294
Cdd:PLN02183  326 WAMAELMKSPEDLKRVQQELADVVGL----NRRVEESDLEKLTYLKCTLKETLRLHPPiPLLLHETAEDAEVAGYFIPKR 401

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 295 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLDcFMAFGSGKFQCP 347
Cdd:PLN02183  402 SRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPdfKGSHFE-FIPFGSGRRSCP 455
PLN02655 PLN02655
ent-kaurene oxidase
 200-346 1.75e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 65.53  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 200 LLLLWASLSNAVPVAF----WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRL--KAP 273
Cdd:PLN02655  264 MMLVWEPIIEAADTTLvtteWAMYELAKNPDKQERLYREIREVCGDE-----RVTEEDLPNLPYLNAVFHETLRKysPVP 338

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 274 GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER-----WKKANLEKhsfldcFMAFGSGKFQC 346
Cdd:PLN02655  339 LLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERflgekYESADMYK------TMAFGAGKRVC 410
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 205-350 2.28e-11

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: 64.96  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 205 ASLSNAVpvafWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKP 283
Cdd:cd11082   235 ASTSSLV----WALQLLADHPDVLAKVREEQARL---RPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPmVPHIAKKD 307

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 284 VEIL-NYIIPSGDLLMLSPFWLHRNPkyFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARK 350
Cdd:cd11082   308 FPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQE 373
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 162-349 7.46e-11

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: 63.47  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 162 IPDIKACKSAK-----DNSMTLLQATLDIVETETskENSPN---YGLLLLW-ASLSNAVPVAFWTLAYVLSHPDIHKAIM 232
Cdd:cd11041   188 IPEIERRRKLKkgpkeDKPNDLLQWLIEAAKGEG--ERTPYdlaDRQLALSfAAIHTTSMTLTHVLLDLAAHPEYIEPLR 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 233 EGISSVFGKAGKdkikVSEDDLENLLL----IKwcvlETIRLKAPGVIT--RKVVKPVEILN-YIIPSGDLLMLSPFWLH 305
Cdd:cd11041   266 EEIRSVLAEHGG----WTKAALNKLKKldsfMK----ESQRLNPLSLVSlrRKVLKDVTLSDgLTLPKGTRIAVPAHAIH 337

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 306 RNPKYFPEPELFKPERW-----KKANLEKHSFLDC---FMAFGSGKFQCPAR 349
Cdd:cd11041   338 RDPDIYPDPETFDGFRFyrlreQPGQEKKHQFVSTspdFLGFGHGRHACPGR 389
PLN02774 PLN02774
brassinosteroid-6-oxidase
 218-350 9.56e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 63.26  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 218 LAYVLSHPDI-------HKAIMEGissvfgKAGKDKIKVseDDLENLLLIKWCVLETIRLKA--PGVItRKVVKPVEILN 288
Cdd:PLN02774  288 VKYLHDHPKAlqelrkeHLAIRER------KRPEDPIDW--NDYKSMRFTRAVIFETSRLATivNGVL-RKTTQDMELNG 358

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 289 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFldcFMAFGSGKFQCPARK 350
Cdd:PLN02774  359 YVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNY---FFLFGGGTRLCPGKE 417
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 216-322 1.16e-10

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 62.91  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 293
Cdd:PLN02687  319 WAIAELIRHPDILKKAQEELDAV---VGRDRL-VSESDLPQLTYLQAVIKETFRLhpSTPLSLPRMAAEECEINGYHIPK 394

                          90       100
                  ....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW 322
Cdd:PLN02687  395 GATLLVNVWAIARDPEQWPDPLEFRPDRF 423
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 210-348 1.27e-10

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 62.79  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 210 AVPVAFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEIL 287
Cdd:PLN03234  304 AAAVVVWAMTYLIKYPEAMKKAQDEVRNVIG----DKGYVSEEDIPNLPYLKAVIKESLRLEPviPILLHRETIADAKIG 379

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 288 NYIIPSGDLLMLSPFWLHRNPKYFPE-PELFKPERWkkanLEKHSFLDC------FMAFGSGKFQCPA 348
Cdd:PLN03234  380 GYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF----MKEHKGVDFkgqdfeLLPFGSGRRMCPA 443
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 216-346 2.01e-10

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: 61.91  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN-YIIPS 293
Cdd:cd20678   261 WILYCLALHPEHQQRCREEIREILG----DGDSITWEHLDQMPYTTMCIKEALRLYPPVPgISRELSKPVTFPDgRSLPA 336

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 346
Cdd:cd20678   337 GITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKrHSH--AFLPFSAGPRNC 388
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 216-357 3.40e-10

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: 61.47  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLKA--PGViTRKVVKPVEILNYIIPS 293
Cdd:cd20647   259 WATYLLARHPEVQQQVYEEIVRNLGK---RVVPTAED-VPKLPLIRALLKETLRLFPvlPGN-GRVTQDDLIVGGYLIPK 333

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKhsfLDCF--MAFGSGKFQCPARKTNRKEQH 357
Cdd:cd20647   334 GTQLALCHYSTSYDEENFPRAEEFRPERWlRKDALDR---VDNFgsIPFGYGIRSCIGRRIAELEIH 397
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 208-350 6.23e-10

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: 60.62  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 208 SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 286
Cdd:cd20649   278 TNTLSFATYLLA---THPECQKKLLREVDEFFSK----HEMVDYANVQELPYLDMVIAETLRMYPPAFrFAREAAEDCVV 350

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 287 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQCPARK 350
Cdd:cd20649   351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFtAEAKQRRHPFV--YLPFGAGPRSCIGMR 413
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 202-348 6.32e-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: 60.58  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 202 LLW----ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--V 275
Cdd:cd20656   234 LLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRV---VGSDRV-MTEADFPQLPYLQCVVKEALRLHPPTplM 309

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 276 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLdcFMAFGSGKFQCPA 348
Cdd:cd20656   310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFleEDVDIKGHDFR--LLPFGAGRRVCPG 382
PLN02971 PLN02971
tryptophan N-hydroxylase
 190-348 7.55e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 60.44  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 190 TSKENSPNYGLLLLWA--SLSNAVPvafWTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLET 267
Cdd:PLN02971  324 TADEIKPTIKELVMAApdNPSNAVE---WAMAEMINKPEILHKAMEEIDRVVGK----ERFVQESDIPKLNYVKAIIREA 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 268 IRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER----WKKANLEKHSFLdcFMAFGS 341
Cdd:PLN02971  397 FRLHpvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlneCSEVTLTENDLR--FISFST 474


                  ....*..
gi 1370508148 342 GKFQCPA 348
Cdd:PLN02971  475 GKRGCAA 481
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 216-350 8.13e-10

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: 60.21  E-value: 8.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 293
Cdd:cd20645   248 WILYNLSRNPQAQQKLLQEIQSVLPA---NQTPRAED-LKNMPYLKACLKESMRL-TPSVpfTSRTLDKDTVLGDYLLPK 322

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSfLDCF--MAFGSGKFQCPARK 350
Cdd:cd20645   323 GTVLMINSQALGSSEEYFEDGRQFKPERWLQ---EKHS-INPFahVPFGIGKRMCIGRR 377
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 216-346 1.29e-09

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: 59.74  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKiKVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 293
Cdd:cd20657   250 WALAELIRHPDILKKAQEEMDQVIGR---DR-RLLESDIPNLPYLQAICKETFRLhpSTPLNLPRIASEACEVDGYYIPK 325

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSFLDC------FMAFGSGKFQC 346
Cdd:cd20657   326 GTRLLVNIWAIGRDPDVWENPLEFKPERFLP---GRNAKVDVrgndfeLIPFGAGRRIC 381
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 202-355 1.65e-09

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 59.18  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 202 LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVIT-RKV 280
Cdd:PLN02196  272 VIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIR-KDKEEGESLTWEDTKKMPLTSRVIQETLRVASILSFTfREA 350

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 281 VKPVEILNYIIPSGDLLMlsPFW--LHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQCPARKTNRKE 355
Cdd:PLN02196  351 VEDVEYEGYLIPKGWKVL--PLFrnIHHSADIFSDPGKFDPSRFEVAPKP-----NTFMPFGNGTHSCPGNELAKLE 420
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 216-346 3.68e-09

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: 58.12  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 294
Cdd:cd11052   254 WTTMLLAIHPEWQEKAREEVLEVCGKD-----KPPSDSLSKLKTVSMVINESLRLYPPAVfLTRKAKEDIKLGGLVIPKG 328

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 295 DLLMLSPFWLHRNPKYFPE-PELFKPERWKK--ANLEKHSflDCFMAFGSGKFQC 346
Cdd:cd11052   329 TSIWIPVLALHHDEEIWGEdANEFNPERFADgvAKAAKHP--MAFLPFGLGPRNC 381
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 217-357 7.75e-09

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: 56.98  E-value: 7.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLSH----PDIHKAIMEGISSVfgkAGKDKIKVSEDdLENLLLIKWCVLETIRLkAPGVIT--RKVV-KPVEILNY 289
Cdd:cd20646   252 TLSWALYHlardPEIQERLYQEVISV---CPGDRIPTAED-IAKMPLLKAVIKETLRL-YPVVPGnaRVIVeKEVVVGDY 326

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 290 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARKTNRKEQH 357
Cdd:cd20646   327 LFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlRDGGLKHHPF--GSIPFGYGVRACVGRRIAELEMY 393
PLN03018 PLN03018
homomethionine N-hydroxylase
 205-321 1.04e-08

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 56.94  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 205 ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVK 282
Cdd:PLN03018  325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEV---VGKDRL-VQESDIPNLNYLKACCRETFRIhpSAHYVPPHVARQ 400

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370508148 283 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 321
Cdd:PLN03018  401 DTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPER 439
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 216-346 1.27e-08

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: 56.62  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILN-YIIPS 293
Cdd:cd20679   266 WILYNLARHPEYQERCRQEVQELL--KDREPEEIEWDDLAQLPFLTMCIKESLRLHPPvTAISRCCTQDIVLPDgRVIPK 343

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQC 346
Cdd:cd20679   344 GIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPL-AFIPFSAGPRNC 395
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 214-346 2.94e-08

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: 55.27  E-value: 2.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 214 AFwTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YII 291
Cdd:cd11068   251 SF-ALYYLLKNPEVLAKARAEVDEVLGDDP-----PPYEQVAKLRYIRRVLDETLRLWPTApAFARKPKEDTVLGGkYPL 324

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 292 PSGD-LLMLSPFwLHRNPK-YFPEPELFKPERWKKANLEKHSfLDCFMAFGSGKFQC 346
Cdd:cd11068   325 KKGDpVLVLLPA-LHRDPSvWGEDAEEFRPERFLPEEFRKLP-PNAWKPFGNGQRAC 379
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 216-355 4.82e-08

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: 54.78  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 293
Cdd:cd20666   250 WCLLYMSLYPEVQEKVQAEIDTVIGP---DRAP-SLTDKAQMPFTEATIMEVQRMTVvvPLSIPHMASENTVLQGYTIPK 325

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN---LEKHSfldcFMAFGSGKFQCPARKTNRKE 355
Cdd:cd20666   326 GTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENgqlIKKEA----FIPFGIGRRVCMGEQLAKME 386
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 216-346 7.05e-08

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: 54.25  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd20673   254 WIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTL----SDRNHLPLLEATIREVLRIRpvAPLLIPHVALQDSSIGEFTIPK 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLD-----------CFMAFGSGKFQC 346
Cdd:cd20673   330 GTRVVINLWALHHDEKEWDQPDQFMPER----------FLDptgsqlispslSYLPFGAGPRVC 383
PTZ00404 PTZ00404
cytochrome P450; Provisional
 216-346 9.85e-08

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.96  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGkaGKDKIKVSedDLENLLLIKWCVLETIRLKAPGV--ITRKVVKPVEILN-YIIP 292
Cdd:PTZ00404  305 WMVLMLCNYPEIQEKAYNEIKSTVN--GRNKVLLS--DRQSTPYTVAIIKETLRYKPVSPfgLPRSTSNDIIIGGgHFIP 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 293 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQC 346
Cdd:PTZ00404  381 KDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSN-----DAFMPFSIGPRNC 429
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 216-347 1.13e-07

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: 53.33  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVFGKAGKDKikvsEDDLENLLLIKWCVLETIRLkAPGVI--TRKVVK---------- 282
Cdd:cd11063   238 FLF-YELArHPEVWAKLREEVLSLFGPEPTPT----YEDLKNMKYLRAVINETLRL-YPPVPlnSRVAVRdttlprgggp 311

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 283 ----PVeilnyIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWkkANLEKHSFLdcFMAFGSGKFQCP 347
Cdd:cd11063   312 dgksPI-----FVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERW--EDLKRPGWE--YLPFNGGPRICL 372
PLN02738 PLN02738
carotene beta-ring hydroxylase
 202-346 1.57e-07

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 53.38  E-value: 1.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 202 LLWASLSNAVPVAFWTLaYVLS-HPDIHKAIMEGISSVFGkagkDKIKVSEDdLENLLLIKWCVLETIRL-KAPGVITRK 279
Cdd:PLN02738  399 MLIAGHETSAAVLTWTF-YLLSkEPSVVAKLQEEVDSVLG----DRFPTIED-MKKLKYTTRVINESLRLyPQPPVLIRR 472

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370508148 280 VVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFldCFMAFGSGKFQC 346
Cdd:PLN02738  473 SLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgPNPNETNQNF--SYLPFGGGPRKC 541
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 216-346 2.04e-07

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: 52.80  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd20674   248 WAVAFLLHHPEIQDRLQEELDRVLGPGASPSYK----DRARLPLLNATIAEVLRLRpvVPLALPHRTTRDSSIAGYDIPK 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQC 346
Cdd:cd20674   324 GTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANRALL----PFGCGARVC 372
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 217-322 2.37e-07

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: 52.58  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAYVLSHPDIHKAIMEGISSVFGkagkdkikvSEDD-----LENLLLIKWCVLETIRL--KAPGVITRKVVKP-VEILN 288
Cdd:cd11058   240 LTYYLLKNPEVLRKLVDEIRSAFS---------SEDDitldsLAQLPYLNAVIQEALRLypPVPAGLPRVVPAGgATIDG 310

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370508148 289 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW 322
Cdd:cd11058   311 QFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERW 344
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 143-355 4.78e-07

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: 51.34  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 143 LLRNWSKSKKWFLELFEKNIPDIKAcksakDNSMTLLQATLdiveTETSKENSPNYG----------LLLLWASLSNAVP 212
Cdd:cd20662   173 VFSNWKKLKLFVSDMIDKHREDWNP-----DEPRDFIDAYL----KEMAKYPDPTTSfneenlicstLDLFFAGTETTST 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 213 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 290
Cdd:cd20662   244 TLRWALLYMALYPEIQEKVQAEIDRVIGQKRQ----PSLADRESMPYTNAVIHEVQRMGniIPLNVPREVAVDTKLAGFH 319

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 291 IPSGDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFL--DCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd20662   320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHF----LENGQFKkrEAFLPFSMGKRACLGEQLARSE 382
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 216-347 9.24e-07

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: 50.64  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd11026   248 WALLLLMKYPHIQEKVQEEIDRVIGRNRT----PSLEDRAKMPYTDAVIHEVQRFGdiVPLGVPHAVTRDTKFRGYTIPK 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GD--LLMLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCP 347
Cdd:cd11026   324 GTtvIPNLTS--VLRDPKQWETPEEFNPGHFldEQGKFKKN---EAFMPFSAGKRVCL 376
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 204-321 1.40e-06

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: 49.95  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 204 WASLSNAVPVAFWTLAyvLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAP-GVITRKVVK 282
Cdd:cd11071   238 FGGFSALLPSLLARLG--LAGEELHARLAEEIRSALGSEGGLTLAA----LEKMPLLKSVVYETLRLHPPvPLQYGRARK 311

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370508148 283 PVEILN----YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 321
Cdd:cd11071   312 DFVIEShdasYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDR 354
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 215-350 1.42e-06

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: 49.90  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 215 FWTLAyvlSHPDIHKAIMEGISSVFGKAGKDKIKV-SEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVeIL--NYI 290
Cdd:cd11064   254 FWLLS---KNPRVEEKIREELKSKLPKLTTDESRVpTYEELKKLVYLHAALSESLRLYPPvPFDSKEAVNDD-VLpdGTF 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 291 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWkkanLEKHSFLDC-----FMAFGSGKFQCPARK 350
Cdd:cd11064   330 VKKGTRIVYSIYAMGRMESIWgEDALEFKPERW----LDEDGGLRPespykFPAFNAGPRICLGKD 391
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 54-351 1.68e-06

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: 49.71  E-value: 1.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148  54 MLKGKMGTVNLHQF-TGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLfstnkkkikefhqyfQVYDED 132
Cdd:cd20626    84 KARGLINLSAADWElLTQAIQATLRRWISHATGGCVNLAELVQALTLRVVLVGLFQSDT---------------DALSLP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 133 FEYGSQLPECLLRNWSKSKKWFLEL-FEKNIpdikacksakdnsmtLLQATLDIVETETSKENSPNYGLLLL---WASLS 208
Cdd:cd20626   149 DESLLDLAEAINELWISSKSGPDPPpFSDNI---------------DLQDALRRVFPDLNDIDPFENPLNLIlpaFETMW 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 209 NAVPVAFWTLAY----VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEddlenllLIKwcvlETIRLKAPgviTRKVVK-- 282
Cdd:cd20626   214 RVVLRTFLEIHYlkgsPTLRDPTHPEWREANADFAKSATKDGISAKN-------LVK----EALRLYPP---TRRIYRaf 279

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 283 ------PVEILNYIIPSgdllmlspfwLHRNPKYF-PEPELFKPERWKKANLEKHsflDCFMAFGSGKFQCPARKT 351
Cdd:cd20626   280 qrpgssKPEIIAADIEA----------CHRSESIWgPDALEFNPSRWSKLTPTQK---EAFLPFGSGPFRCPAKPV 342
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 213-347 1.98e-06

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 49.71  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 213 VAFWTLAYVLSHPDIH---KAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILN 288
Cdd:PLN02302  306 LTMWATIFLQEHPEVLqkaKAEQEEIAK---KRPPGQKGLTLKDVRKMEYLSQVIDETLRLiNISLTVFREAKTDVEVNG 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 289 YIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCP 347
Cdd:PLN02302  383 YTIPKGWKVLA---WFrqvHMDPEVYPNPKEFDPSRWDNYTPKAGTFL----PFGLGSRLCP 437
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 266-355 2.39e-06

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 49.35  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 266 ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhsflDCFMAFGSGKF 344
Cdd:PLN03141  323 ETLRMgNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNN----SSFTPFGGGQR 398

                          90
                  ....*....|.
gi 1370508148 345 QCPARKTNRKE 355
Cdd:PLN03141  399 LCPGLDLARLE 409
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 215-346 3.25e-06

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 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: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 48.89  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 215 FWTLAYVLSHPDIHKAIMEGISSVFGkaGKDkikVSEDDLENLLLIKWCVLETIRLKaPGV--ITRKVVKPVEILNYIIP 292
Cdd:cd20616   245 FFMLLLIAQHPEVEEAILKEIQTVLG--ERD---IQNDDLQKLKVLENFINESMRYQ-PVVdfVMRKALEDDVIDGYPVK 318

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 293 SGDLLMLSPFWLHRNPkYFPEPELFKPErwkkaNLEKHSFLDCFMAFGSGKFQC 346
Cdd:cd20616   319 KGTNIILNIGRMHRLE-FFPKPNEFTLE-----NFEKNVPSRYFQPFGFGPRSC 366
PLN00168 PLN00168
Cytochrome P450; Provisional
 216-322 3.49e-06

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 49.18  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPS 293
Cdd:PLN00168  328 WIMAELVKNPSIQSKLHDEIKA---KTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAhfVLPHKAAEDMEVGGYLIPK 404

                          90       100
                  ....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERW 322
Cdd:PLN00168  405 GATVNFMVAEMGRDEREWERPMEFVPERF 433
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 266-342 3.86e-06

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: 48.36  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 266 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERwkKANleKHsfldcfMAFGS 341
Cdd:cd11032   248 EVLRYRPPvQRTARVTTEDVELGGVTIPAGQLVIA---WLasaNRDERQFEDPDTFDIDR--NPN--PH------LSFGH 314


                  .
gi 1370508148 342 G 342
Cdd:cd11032   315 G 315
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 200-355 4.75e-06

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: 48.46  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 200 LLLLWASLSNAVPVAFWTLAYvLSHPD-------IHKAIMEgissvfgkAGKDKIKVSEDDLEN------LLLIKwcvlE 266
Cdd:cd11066   234 LTMVSAGLDTVPLNLNHLIGH-LSHPPgqeiqekAYEEILE--------AYGNDEDAWEDCAAEekcpyvVALVK----E 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 267 TIR------LKAPgvitRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFmAFG 340
Cdd:cd11066   301 TLRyftvlpLGLP----RKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHF-SFG 375

                         170
                  ....*....|....*
gi 1370508148 341 SGKFQCPARKTNRKE 355
Cdd:cd11066   376 AGSRMCAGSHLANRE 390
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 188-346 4.86e-06

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: 48.41  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 188 TETSkENSPNYGLLLLwaslsnavpvafwtlayvLSHPDIHKAIMEGISSVFGK----AGKDKIKVSEDDlenlllikwC 263
Cdd:cd20665   239 TETT-STTLRYGLLLL------------------LKHPEVTAKVQEEIDRVIGRhrspCMQDRSHMPYTD---------A 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 264 VLETIRLKA---PGVITRKVVKPVEILNYIIPSGD--LLMLSPFwLHrNPKYFPEPELFKPERW--KKANLEKHsflDCF 336
Cdd:cd20665   291 VIHEIQRYIdlvPNNLPHAVTCDTKFRNYLIPKGTtvITSLTSV-LH-DDKEFPNPEKFDPGHFldENGNFKKS---DYF 365

                         170
                  ....*....|
gi 1370508148 337 MAFGSGKFQC 346
Cdd:cd20665   366 MPFSAGKRIC 375
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 266-347 4.94e-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: 48.37  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 266 ETIRLKAPGVIT-RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkANLEKHsfldcfMAFGSGKF 344
Cdd:cd11078   259 ETLRYDSPVQGLrRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PNARKH------LTFGHGIH 329


                  ...
gi 1370508148 345 QCP 347
Cdd:cd11078   330 FCL 332
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 216-342 6.60e-06

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: 48.04  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKikvseDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 294
Cdd:cd20642   256 WTMVLLSQHPDWQERAREEVLQVFGNNKPDF-----EGLNHLKVVTMILYEVLRLYPPVIqLTRAIHKDTKLGDLTLPAG 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 295 DLLMLSPFWLHRNPKYFPE-PELFKPERWK----KANLEKHSFLdcfmAFGSG 342
Cdd:cd20642   331 VQVSLPILLVHRDPELWGDdAKEFNPERFAegisKATKGQVSYF----PFGWG 379
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 216-346 6.80e-06

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 47.92  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 293
Cdd:PLN00110  311 WSLAEMLKNPSILKRAHEEMDQVIGRNRR----LVESDLPKLPYLQAICKESFRKhpSTPLNLPRVSTQACEVNGYYIPK 386

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSFLDC------FMAFGSGKFQC 346
Cdd:PLN00110  387 NTRLSVNIWAIGRDPDVWENPEEFRPERFLS---EKNAKIDPrgndfeLIPFGAGRRIC 442
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 264-349 7.09e-06

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: 47.72  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 264 VLETIRLK--APGVItRKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkaNLEKhsfldcF 336
Cdd:cd20612   244 VLEALRLNpiAPGLY-RRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR----PLES------Y 312

                          90
                  ....*....|...
gi 1370508148 337 MAFGSGKFQCPAR 349
Cdd:cd20612   313 IHFGHGPHQCLGE 325
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 259-347 2.74e-05

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: 45.75  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 259 LIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfm 337
Cdd:cd20629   235 LIPAAIEEGLRWEPPvASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDRKPKPHL---------- 304

                          90
                  ....*....|
gi 1370508148 338 AFGSGKFQCP 347
Cdd:cd20629   305 VFGGGAHRCL 314
PLN02936 PLN02936
epsilon-ring hydroxylase
 252-322 3.93e-05

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 45.55  E-value: 3.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370508148 252 DDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW 322
Cdd:PLN02936  331 EDIKELKYLTRCINESMRLypHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF 403
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 216-322 4.27e-05

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: 45.32  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLaYVLS-HPDIHKAIMEGISSVFG---KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVeilNYII 291
Cdd:cd11051   207 WAF-YLLSkHPEVLAKVRAEHDEVFGpdpSAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGV---GLTD 282

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370508148 292 PSGDLLMLSPF--W-----LHRNPKYFPEPELFKPERW 322
Cdd:cd11051   283 RDGKEYPTDGCivYvchhaIHRDPEYWPRPDEFIPERW 320
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 263-355 4.98e-05

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 45.36  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 263 CVL-ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKaNLEKHSFLDCFMAFG 340
Cdd:PLN02987  334 CVVnETLRVaNIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQS-NSGTTVPSNVFTPFG 412

                          90
                  ....*....|....*
gi 1370508148 341 SGKFQCPARKTNRKE 355
Cdd:PLN02987  413 GGPRLCPGYELARVA 427
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 213-349 8.59e-05

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: 44.37  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 213 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAgkdkikvsedDLENLlliKWCVLETIRL--KAPgVITRKVVKPVEILNYI 290
Cdd:cd20624   210 ALLRALALLAAHPEQAARAREEAAVPPGPL----------ARPYL---RACVLDAVRLwpTTP-AVLRESTEDTVWGGRT 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 291 IPSGD-LLMLSPFWlHRNPKYFPEPELFKPERWKKANLEKHSFLdcfMAFGSGKFQCPAR 349
Cdd:cd20624   276 VPAGTgFLIFAPFF-HRDDEALPFADRFVPEIWLDGRAQPDEGL---VPFSAGPARCPGE 331
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 217-355 9.94e-05

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: 44.14  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAY----VLSHPDIHKAIMEGISSVFGK----AGKDKIKVSEDDLenlllikwCVLETIRLK--APGVITRKVVKPVEI 286
Cdd:cd20670   245 TLRYgfllLMKYPEVEAKIHEEINQVIGPhrlpSVDDRVKMPYTDA--------VIHEIQRLTdiVPLGVPHNVIRDTQF 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370508148 287 LNYIIPSG-DLLMLSPFWLhRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd20670   317 RGYLLPKGtDVFPLLGSVL-KDPKYFRYPEAFYPQHFldEQGRFKKN---EAFVPFSSGKRVCLGEAMARME 384
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 279-333 1.03e-04

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: 44.06  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370508148 279 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFL 333
Cdd:cd11067   285 RARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDFI 339
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 216-346 1.50e-04

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: 43.84  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 293
Cdd:cd20675   257 WILLLLVRYPDVQARLQEELDRV---VGRDRLP-CIEDQPNLPYVMAFLYEAMRFSSfvPVTIPHATTADTSILGYHIPK 332

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLD-----CFMAFGSGKFQC 346
Cdd:cd20675   333 DTVVFVNQWSVNHDPQKWPNPEVFDPTRF----LDENGFLNkdlasSVMIFSVGKRRC 386
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 216-355 2.60e-04

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: 42.88  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikvSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 293
Cdd:cd20661   260 WAILFMALYPNIQGQVQKEIDLVVGPNGMP----SFEDKCKMPYTEAVLHEVLRFcnIVPLGIFHATSKDAVVRGYSIPK 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370508148 294 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN--LEKHsflDCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd20661   336 GTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNgqFAKK---EAFVPFSLGRRHCLGEQLARME 396
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 216-346 2.72e-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: 42.66  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDdleNLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 293
Cdd:cd20615   237 WNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILS---TDTLLAYCVLESLRLRplLAFSVPESSPTDKIIGGYRIPA 313

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370508148 294 GDLLMLSPFWL-HRNPKYFPEPELFKPERW---KKANLEKHsfldcFMAFGSGKFQC 346
Cdd:cd20615   314 NTPVVVDTYALnINNPFWGPDGEAYRPERFlgiSPTDLRYN-----FWRFGFGPRKC 365
PLN02500 PLN02500
cytochrome P450 90B1
 248-346 5.58e-04

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 42.16  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 248 KVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN 326
Cdd:PLN02500  334 ELNWEDYKKMEFTQCVINETLRLgNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNN 413

                          90       100
                  ....*....|....*....|....*.
gi 1370508148 327 LEKHS------FLDCFMAFGSGKFQC 346
Cdd:PLN02500  414 NRGGSsgsssaTTNNFMPFGGGPRLC 439
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 217-346 6.62e-04

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: 41.71  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 217 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 290
Cdd:cd20668   245 TLRYgfllLMKHPEVEAKVHEEIDRVIGRNRQPKF----EDRAKMPYTEAVIHEIQRFGdvIPMGLARRVTKDTKFRDFF 320

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 291 IPSGDLL--MLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQC 346
Cdd:cd20668   321 LPKGTEVfpMLGS--VLKDPKFFSNPKDFNPQHFldDKGQFKKS---DAFVPFSIGKRYC 375
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 216-346 6.86e-04

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: 41.54  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 216 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIR------LKAPGVITRKVvkpveILN- 288
Cdd:cd20676   259 WSLMYLVTYPEIQKKIQEELDEVIGRERRPRLS----DRPQLPYLEAFILETFRhssfvpFTIPHCTTRDT-----SLNg 329

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 289 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--FMAFGSGKFQC 346
Cdd:cd20676   330 YYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTESekVMLFGLGKRRC 389
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 266-347 1.04e-03

P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Agrobacterium tumefaciens P450-pinF2, whose expression is induced by the presence of wounded plant tissue and by plant phenolic compounds such as acetosyringone. P450-pinF2 may be involved in the detoxification of plant protective agents at the site of wounding. 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: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 266 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKF 344
Cdd:cd11039   252 EGLRWISPiGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFRPKSPHV----------SFGAGPH 321


                  ...
gi 1370508148 345 QCP 347
Cdd:cd11039   322 FCA 324
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 255-355 1.33e-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: 40.42  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 255 ENLLLIKWCVLETIRLKAPGVITRKVVK-PVEILNYIIPSGDLLMLSpfWL--HRNPKYFPEPELFKPERWKKANLekhs 331
Cdd:cd11079   222 ANPALLPAAIDEILRLDDPFVANRRITTrDVELGGRTIPAGSRVTLN--WAsaNRDERVFGDPDEFDPDRHAADNL---- 295

                          90       100
                  ....*....|....*....|....
gi 1370508148 332 fldcfmAFGSGKFQCPARKTNRKE 355
Cdd:cd11079   296 ------VYGRGIHVCPGAPLARLE 313
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 277-355 1.71e-03

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: 40.10  E-value: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370508148 277 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKFQCPARKTNRKE 355
Cdd:cd20630   266 ARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNANI----------AFGYGPHFCIGAALARLE 334
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 224-346 3.55e-03

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: 39.41  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 224 HPDIHKAIMEGISS--VFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVitRKVVKPVEILNYIIPSGDLLM 298
Cdd:cd20638   260 HPEVLQKVRKELQEkgLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPPvpgGF--RVALKTFELNGYQIPKGWNVI 337

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370508148 299 LSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcFMAFGSGKFQC 346
Cdd:cd20638   338 YSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFS-FIPFGGGSRSC 384
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 202-346 3.78e-03

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: 39.43  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 202 LLWASLSNAVPVAFWTLAYVLSHPD-IHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVi 276
Cdd:cd20636   235 LIFAAFSTTASASTSLVLLLLQHPSaIEKIRQELVSHGLIDQcQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPvsgGY- 313

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 277 tRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQC 346
Cdd:cd20636   314 -RTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSC 382
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 266-349 7.08e-03

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. 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: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 38.34  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 266 ETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLsPFWLH-RNPKYFPEPELFKPERwkKANleKHsfldcfMAFGSGKF 344
Cdd:cd11035   240 ELLRRYPLVNVARIVTRDVEFHGVQLKAGDMVLL-PLALAnRDPREFPDPDTVDFDR--KPN--RH------LAFGAGPH 308


                  ....*....
gi 1370508148 345 QCP----AR 349
Cdd:cd11035   309 RCLgshlAR 317
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 148-355 8.31e-03

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: 38.20  E-value: 8.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 148 SKSKKWFLELFEKNIP-DIKAC---KSAKD--------NSMTLLQATLDIV--ETETSKeNSPNYGLLLLwaslsnavpv 213
Cdd:cd20669   185 AESVREHQESLDPNSPrDFIDCfltKMAEEkqdplshfNMETLVMTTHNLLfgGTETVS-TTLRYGFLIL---------- 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 214 afwtlayvLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYII 291
Cdd:cd20669   254 --------MKYPKVAARVQEEIDRVVGRNRLPTL----EDRARMPYTDAVIHEIQRFADiiPMSLPHAVTRDTNFRGFLI 321

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370508148 292 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlekHSFL--DCFMAFGSGKFQCPARKTNRKE 355
Cdd:cd20669   322 PKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDN---GSFKknDAFMPFSAGKRICLGESLARME 384
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 264-346 9.88e-03

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: 37.92  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370508148 264 VLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfwL----HRNPKYFPEPELFKPERwkKANleKHsfldcfMA 338
Cdd:cd20625   249 VEELLRYDSPvQLTARVALEDVEIGGQTIPAGDRVLL----LlgaaNRDPAVFPDPDRFDITR--APN--RH------LA 314


                  ....*...
gi 1370508148 339 FGSGKFQC 346
Cdd:cd20625   315 FGAGIHFC 322
 
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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