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Conserved domains on  [gi|942412537|gb|JAN88198|]
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putative Cytochrome p450 [Daphnia magna]

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 ...
 126-310 6.55e-68

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 cd20628:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 426  Bit Score: 217.78  E-value: 6.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEFElsiETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEI-YLSNVHRFCQIFIERVKRPWLSYKW 284
Cdd:cd20628   81 NENSKILVEKLK---KKAGGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSeYVKAVKRILEIILKRIFSPWLRFDF 157

                        170       180
                 ....*....|....*....|....*.
gi 942412537 285 IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20628  158 IFRLTSLGKEQRKALKVLHDFTNKVI 183
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 126-310 6.55e-68

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: 217.78  E-value: 6.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEFElsiETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEI-YLSNVHRFCQIFIERVKRPWLSYKW 284
Cdd:cd20628   81 NENSKILVEKLK---KKAGGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSeYVKAVKRILEIILKRIFSPWLRFDF 157

                        170       180
                 ....*....|....*....|....*.
gi 942412537 285 IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20628  158 IFRLTSLGKEQRKALKVLHDFTNKVI 183
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 123-310 3.10e-26

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: 107.75  E-value: 3.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  123 KKYGPIYSVWLGPRPFVTLASPELVHTIL-----SSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQN 197
Cdd:pfam00067  31 KKYGPIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  198 YNSFMDIFNEKSSICAAEFELSIETQGdtGIDVSRLLARCTLNIICETVMG-QQTKVEMEKEI-YLSNVHRFCQIFIERV 275
Cdd:pfam00067 111 KLSFEPRVEEEARDLVEKLRKTAGEPG--VIDITDLLFRAALNVICSILFGeRFGSLEDPKFLeLVKAVQELSSLLSSPS 188

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 942412537  276 KRPWLSYKWI-YKMSPLSRESERCINTLHTFTDKVI 310
Cdd:pfam00067 189 PQLLDLFPILkYFPGPHGRKLKRARKKIKDLLDKLI 224
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 124-248 2.51e-11

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: 63.76  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTILSSSKN---NTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNS 200
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTfssDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAA 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 942412537 201 FMDIFNEkssICAAEFElSIETQGdtGIDVSRLLARCTLNIICETVMG 248
Cdd:COG2124  110 LRPRIRE---IADELLD-RLAARG--PVDLVEEFARPLPVIVICELLG 151
PLN02738 PLN02738
carotene beta-ring hydroxylase
 108-246 1.40e-08

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 55.69  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 108 VYNEEFYKVMAiDWVKKYGPIYSVWLGPRPFVTLASPELVHTILsssKNNTKASDYLNLSEWL----GNSILVSSGDHWK 183
Cdd:PLN02738 148 VRGEAFFIPLY-ELFLTYGGIFRLTFGPKSFLIVSDPSIAKHIL---RDNSKAYSKGILAEILefvmGKGLIPADGEIWR 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942412537 184 TRRRILTPGFHFQNYNSFMDIFNEKSS-ICAaefELSIETQGDTGIDVSRLLARCTLNIICETV 246
Cdd:PLN02738 224 VRRRAIVPALHQKYVAAMISLFGQASDrLCQ---KLDAAASDGEDVEMESLFSRLTLDIIGKAV 284
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 126-310 6.55e-68

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: 217.78  E-value: 6.55e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEFElsiETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEI-YLSNVHRFCQIFIERVKRPWLSYKW 284
Cdd:cd20628   81 NENSKILVEKLK---KKAGGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSeYVKAVKRILEIILKRIFSPWLRFDF 157

                        170       180
                 ....*....|....*....|....*.
gi 942412537 285 IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20628  158 IFRLTSLGKEQRKALKVLHDFTNKVI 183
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 126-310 9.87e-60

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: 196.71  E-value: 9.87e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd20660    1 GPIFRIWLGPKPIVVLYSAETVEVILSSSKHIDKSFEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEfelsIETQGDTG-IDVSRLLARCTLNIICETVMGQQTKVEMEKEI-YLSNVHRFCQIFIERVKRPWLSYK 283
Cdd:cd20660   81 NEQSEILVKK----LKKEVGKEeFDIFPYITLCALDIICETAMGKSVNAQQNSDSeYVKAVYRMSELVQKRQKNPWLWPD 156

                        170       180
                 ....*....|....*....|....*..
gi 942412537 284 WIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20660  157 FIYSLTPDGREHKKCLKILHGFTNKVI 183
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 127-310 8.46e-41

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: 147.21  E-value: 8.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 127 PIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIFN 206
Cdd:cd20680   13 PLLKLWIGPVPFVILYHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 207 EKSSICAAEFELSIETQG-DTGIDVSrllaRCTLNIICETVMGQQTKVEMEKEI-YLSNVHRFCQIFIERVKRPWLSYKW 284
Cdd:cd20680   93 EQSNILVEKLEKHVDGEAfNCFFDIT----LCALDIICETAMGKKIGAQSNKDSeYVQAVYRMSDIIQRRQKMPWLWLDL 168

                        170       180
                 ....*....|....*....|....*.
gi 942412537 285 IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20680  169 WYLMFKEGKEHNKNLKILHTFTDNVI 194
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 128-310 1.35e-40

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: 146.16  E-value: 1.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 128 IYSVWLGP-RPFVTLASPELVHTILSSSknNTKASDYLN-LSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd20659    3 AYVFWLGPfRPILVLNHPDTIKAVLKTS--EPKDRDSYRfLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEFELSieTQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKE--IYLSNVHRFCQIFIERVKRPWLSYK 283
Cdd:cd20659   81 NECTDILLEKWSKL--AETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKnhPYVAAVHELSRLVMERFLNPLLHFD 158

                        170       180
                 ....*....|....*....|....*..
gi 942412537 284 WIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20659  159 WIYYLTPEGRRFKKACDYVHKFAEEII 185
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 126-310 9.74e-37

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: 135.81  E-value: 9.74e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLseWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIF 205
Cdd:cd11057    1 GSPFRAWLGPRPFVITSDPEIVQVVLNSPHCLNKSFFYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKSSICAAEFElsiETQGDTGIDVSRLLARCTLNIICETVMGQQTKVE-MEKEIYLSNVHRFCQIFIERVKRPWLSYKW 284
Cdd:cd11057   79 NEEAQKLVQRLD---TYVGGGEFDILPDLSRCTLEMICQTTLGSDVNDEsDGNEEYLESYERLFELIAKRVLNPWLHPEF 155

                        170       180
                 ....*....|....*....|....*.
gi 942412537 285 IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11057  156 IYRLTGDYKEEQKARKILRAFSEKII 181
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 123-310 3.10e-26

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: 107.75  E-value: 3.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  123 KKYGPIYSVWLGPRPFVTLASPELVHTIL-----SSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQN 197
Cdd:pfam00067  31 KKYGPIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  198 YNSFMDIFNEKSSICAAEFELSIETQGdtGIDVSRLLARCTLNIICETVMG-QQTKVEMEKEI-YLSNVHRFCQIFIERV 275
Cdd:pfam00067 111 KLSFEPRVEEEARDLVEKLRKTAGEPG--VIDITDLLFRAALNVICSILFGeRFGSLEDPKFLeLVKAVQELSSLLSSPS 188

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 942412537  276 KRPWLSYKWI-YKMSPLSRESERCINTLHTFTDKVI 310
Cdd:pfam00067 189 PQLLDLFPILkYFPGPHGRKLKRARKKIKDLLDKLI 224
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 122-310 1.64e-22

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: 97.07  E-value: 1.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 122 VKKYGPIYSVWLGP-RPFVTLASPELVHTILSSSKNNTKASD--YLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNY 198
Cdd:cd20679    8 VATYPQGCLWWLGPfYPIIRLFHPDYIRPVLLASAAVAPKDElfYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAFHFNIL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 199 NSFMDIFNEKSSICAAEFELsIETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEIYLSNVHRFCQIFIERVKRP 278
Cdd:cd20679   88 KPYVKIFNQSTNIMHAKWRR-LASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVVKRQQQL 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 942412537 279 WLSYKWIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20679  167 LLHLDFLYYLTADGRRFRRACRLVHDFTDAVI 198
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 121-310 1.02e-21

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: 94.65  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGP-RPFVTLASPELVHTILSSSknNTKASD-YLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNY 198
Cdd:cd20678    7 WVEKYPYAFPLWFGGfKAFLNIYDPDYAKVVLSRS--DPKAQGvYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYDIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 199 NSFMDIFNEKSSICAAEFElSIETQGDTgIDVSRLLARCTLNIICETVMGQQTKVEMEK--EIYLSNVHRFCQIFIERVK 276
Cdd:cd20678   85 KPYVKLMADSVRVMLDKWE-KLATQDSS-LEIFQHVSLMTLDTIMKCAFSHQGSCQLDGrsNSYIQAVSDLSNLIFQRLR 162

                        170       180       190
                 ....*....|....*....|....*....|....
gi 942412537 277 RPWLSYKWIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd20678  163 NFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVI 196
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 119-310 2.42e-21

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: 93.35  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 119 IDWVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSkNNTKASDYLNL------SEWLGNSiLVSSGDH--WKTRRRILT 190
Cdd:cd20613    5 LEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITL-NLPKPPRVYSRlaflfgERFLGNG-LVTEVDHekWKKRRAILN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 191 PGFHFQNYNSFMDIFNEkssiCAAEF--ELSIETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEIYLSNVHRFC 268
Cdd:cd20613   83 PAFHRKYLKNLMDEFNE----SADLLveKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFPKAISLV 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 942412537 269 -QIFIERVKRPWLSY---KWIYKmsplsRESERCINTLHTFTDKVI 310
Cdd:cd20613  159 lEGIQESFRNPLLKYnpsKRKYR-----REVREAIKFLRETGRECI 199
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 126-310 6.97e-19

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: 86.03  E-value: 6.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDY--LNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMD 203
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPglPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 204 IFNEkssiCAAEFELSIETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKeiylsnVHRFCQIFIERVKRPWLSYK 283
Cdd:cd00302   81 VIRE----IARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEE------LAELLEALLKLLGPRLLRPL 150

                        170       180
                 ....*....|....*....|....*..
gi 942412537 284 WiykmSPLSRESERCINTLHTFTDKVI 310
Cdd:cd00302  151 P----SPRLRRLRRARARLRDYLEELI 173
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 126-310 3.24e-18

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: 84.17  E-value: 3.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTIL-SSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDI 204
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLvTNARNYVKGGVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 205 FNEkssiCAAEFELSIETQGDTG-IDVSRLLARCTLNIICETVMGQQTKVEMEKeiylsnVHRFCQIFIERVKRPWLSYK 283
Cdd:cd20620   81 MVE----ATAALLDRWEAGARRGpVDVHAEMMRLTLRIVAKTLFGTDVEGEADE------IGDALDVALEYAARRMLSPF 150

                        170       180
                 ....*....|....*....|....*....
gi 942412537 284 WIYKM--SPLSRESERCINTLHTFTDKVI 310
Cdd:cd20620  151 LLPLWlpTPANRRFRRARRRLDEVIYRLI 179
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 121-248 2.01e-15

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: 76.23  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLN-LSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYN 199
Cdd:cd11052    7 WIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPgLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLK 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 942412537 200 SFMDIFNEKSSICAAEFElSIETQGDTGIDVSRLLARCTLNIICETVMG 248
Cdd:cd11052   87 GMVPAMVESVSDMLERWK-KQMGEEGEEVDVFEEFKALTADIISRTAFG 134
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 125-310 1.15e-14

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: 73.84  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGP---IYSVWLGPRPFVTlaSPELVHTILSSSKNNTKASD--YLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYN 199
Cdd:cd11069    1 YGGlirYRGLFGSERLLVT--DPKALKHILVTNSYDFEKPPafRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 200 SFMDIFNEKSSICAAEFELSIETQGD--TGIDVSRLLARCTLNIICETVMGQQTKVEMEKEIYLSNVHR---------FC 268
Cdd:cd11069   79 ELYPIFWSKAEELVDKLEEEIEESGDesISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRrlfeptllgSL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 942412537 269 QIFIERVKRPWLSYKWiykMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11069  159 LFILLLFLPRWLVRIL---PWKANREIRRAKDVLRRLAREII 197
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 120-310 1.15e-14

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: 73.94  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 120 DWVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNN--TKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQN 197
Cdd:cd11046    5 KWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSydKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 198 YNSFMDIFNEKSSICAAEFELSIETQgdTGIDVSRLLARCTLNIICETVMGQQ-TKVEME----KEIYLSNVHrfcqifi 272
Cdd:cd11046   85 LEMMVRVFGRCSERLMEKLDAAAETG--ESVDMEEEFSSLTLDIIGLAVFNYDfGSVTEEspviKAVYLPLVE------- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 942412537 273 ERVKRPWLSYKW----IYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11046  156 AEHRSVWEPPYWdipaALFIVPRQRKFLRDLKLLNDTLDDLI 197
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 121-248 4.95e-14

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 72.10  E-value: 4.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVS-SGDHWKTRRRILTPGFHFQNYN 199
Cdd:cd20639    7 WRKIYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPLVRQLEGDGLVSlRGEKWAHHRRVITPAFHMENLK 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 942412537 200 SFMDIFNEKSSICAAEFELSIETQGDTGIDVSRLLARCTLNIICETVMG 248
Cdd:cd20639   87 RLVPHVVKSVADMLDKWEAMAEAGGEGEVDVAEWFQNLTEDVISRTAFG 135
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 121-230 1.11e-12

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 67.82  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYL--NLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNY 198
Cdd:cd20640    7 WRKQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLDLGKPSYLkkTLKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKV 86

                         90       100       110
                 ....*....|....*....|....*....|..
gi 942412537 199 NSFMDIFNEKSSICAAEFELSIETQGDTGIDV 230
Cdd:cd20640   87 KGMVDLMVDSAQPLLSSWEERIDRAGGMAADI 118
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 126-310 1.60e-12

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: 67.62  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILssSKNNTKASD-YLNLS-EWL--GNSILVSSGDHWKTRRRILTPGF-HFQNYNS 200
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAF--VKNGDNFSDrPLLPSfEIIsgGKGILFSNGDYWKELRRFALSSLtKTKLKKK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 201 FMDIFNEKSSICAAEFELSIETqgDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEIyLSNVHRFCQIFiERVKRPWL 280
Cdd:cd20617   79 MEELIEEEVNKLIESLKKHSKS--GEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEF-LKLVKPIEEIF-KELGSGNP 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 942412537 281 S-YKWIYKMSPLSR--ESERCINTLHTFTDKVI 310
Cdd:cd20617  155 SdFIPILLPFYFLYlkKLKKSYDKIKDFIEKII 187
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 124-249 9.48e-12

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: 65.04  E-value: 9.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYsVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYN-SFM 202
Cdd:cd11070    1 KLGAVK-ILFVSRWNILVTKPEYLTQIFRRRDDFPKPGNQYKIPAFYGPNVISSEGEDWKRYRKIVAPAFNERNNAlVWE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 942412537 203 DIFNEKSSICAAEFElSIETQGDTGIDVSRLLARCTLNIICETVMGQ 249
Cdd:cd11070   80 ESIRQAQRLIRYLLE-EQPSAKGGGVDVRDLLQRLALNVIGEVGFGF 125
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 120-248 1.18e-11

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: 64.99  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 120 DWVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKAsDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYN 199
Cdd:cd20642    6 HTVKTYGKNSFTWFGPIPRVIIMDPELIKEVLNKVYDFQKP-KTNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEKLK 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 942412537 200 SFMDIFNEKSSICAAEFELSIETQGDTGIDVSRLLARCTLNIICETVMG 248
Cdd:cd20642   85 NMLPAFYLSCSEMISKWEKLVSSKGSCELDVWPELQNLTSDVISRTAFG 133
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 124-248 2.51e-11

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: 63.76  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTILSSSKN---NTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNS 200
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTfssDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAA 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 942412537 201 FMDIFNEkssICAAEFElSIETQGdtGIDVSRLLARCTLNIICETVMG 248
Cdd:COG2124  110 LRPRIRE---IADELLD-RLAARG--PVDLVEEFARPLPVIVICELLG 151
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 124-251 3.42e-11

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: 63.37  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTILSSSKNN-TKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFM 202
Cdd:cd11055    1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNfTNRPLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 942412537 203 DIFNEkssiCAAEFELSIETQGDTG--IDVSRLLARCTLNIICETVMGQQT 251
Cdd:cd11055   81 PIIND----CCDELVEKLEKAAETGkpVDMKDLFQGFTLDVILSTAFGIDV 127
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 120-248 3.93e-10

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: 60.29  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 120 DWVKKYGPIYSVWL-GPRPFVTLASPELVHTILSSSKNN---TKASDylNLSEWLG-NSILVSSGDHWKTRRRILTPGFH 194
Cdd:cd11053    6 RLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFTADPDVlhpGEGNS--LLEPLLGpNSLLLLDGDRHRRRRKLLMPAFH 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 942412537 195 ---FQNYNSFMdifnekssicAAEFELSIET-QGDTGIDVSRLLARCTLNIICETVMG 248
Cdd:cd11053   84 gerLRAYGELI----------AEITEREIDRwPPGQPFDLRELMQEITLEVILRVVFG 131
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 132-310 1.01e-09

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: 59.14  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 132 WLGPRPFVTLASPELVHTILSssknnTKASDYL-------NLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFM-D 203
Cdd:cd11064    7 WPGGPDGIVTADPANVEHILK-----TNFDNYPkgpefrdLFFDLLGDGIFNVDGELWKFQRKTASHEFSSRALREFMeS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 204 IFNEKSS-------ICAAEFELSIETQgdtgidvsRLLARCTLNIICETVMGqqtkVEMEKEIYLSNVHRFCQ------- 269
Cdd:cd11064   82 VVREKVEkllvpllDHAAESGKVVDLQ--------DVLQRFTFDVICKIAFG----VDPGSLSPSLPEVPFAKafddase 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 942412537 270 IFIERVKRPwlsyKWIYK-MSPLSRESER----CINTLHTFTDKVI 310
Cdd:cd11064  150 AVAKRFIVP----PWLWKlKRWLNIGSEKklreAIRVIDDFVYEVI 191
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 126-304 1.37e-09

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: 58.45  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDyLN----LSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSF 201
Cdd:cd20615    1 GPIYRIWSGPTPEIVLTTPEHVKEFYRDSNKHHKAPN-NNsgwlFGQLLGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 202 MDIFnekSSICAAEFELSIETQGDTG---IDVSRLLARCTLNIICETVMGQQTkvEMEKEIYLSNVHRFCQIFIERVKRP 278
Cdd:cd20615   80 IPQF---SREARKWVQNLPTNSGDGRrfvIDPAQALKFLPFRVIAEILYGELS--PEEKEELWDLAPLREELFKYVIKGG 154

                        170       180
                 ....*....|....*....|....*.
gi 942412537 279 WLSYKWIYKmspLSRESERCINTLHT 304
Cdd:cd20615  155 LYRFKISRY---LPTAANRRLREFQT 177
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 125-250 1.90e-09

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: 57.96  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWL--GNSILVSSGDHWKTRRR--ILTpgfhFQNY-- 198
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVtkGYGVVFSNGERWKQLRRfsLTT----LRNFgm 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 942412537 199 --NSFMDIFNEKSSICAAEFElsiETQGDTgIDVSRLLARCTLNIICETVMGQQ 250
Cdd:cd11026   77 gkRSIEERIQEEAKFLVEAFR---KTKGKP-FDPTFLLSNAVSNVICSIVFGSR 126
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 121-262 4.50e-09

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 57.07  E-value: 4.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSS-----SKNNTKASdYLNLsewLGNSILVSSGDHWKTRRRILTPGFHF 195
Cdd:cd20641    7 WKSQYGETFLYWQGTTPRICISDHELAKQVLSDkfgffGKSKARPE-ILKL---SGKGLVFVNGDDWVRHRRVLNPAFSM 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 942412537 196 QNYNSFMDIFNEkssiCAAEFELSIETQGDTG------IDVSRLLARCTLNIICETVMGqqTKVEMEKEIYLS 262
Cdd:cd20641   83 DKLKSMTQVMAD----CTERMFQEWRKQRNNSeterieVEVSREFQDLTADIIATTAFG--SSYAEGIEVFLS 149
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 125-256 7.65e-09

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: 56.45  E-value: 7.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILSSSKN------NTKASDYLNLSewlGNSILVSS-GDHWKTRRRILTPGFHfqN 197
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSAdfagrpKLFTFDLFSRG---GKDIAFGDySPTWKLHRKLAHSALR--L 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942412537 198 YNSFMDIFNEKssIC--AAEFELSIETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEME 256
Cdd:cd11027   76 YASGGPRLEEK--IAeeAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDP 134
PLN02738 PLN02738
carotene beta-ring hydroxylase
 108-246 1.40e-08

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 55.69  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 108 VYNEEFYKVMAiDWVKKYGPIYSVWLGPRPFVTLASPELVHTILsssKNNTKASDYLNLSEWL----GNSILVSSGDHWK 183
Cdd:PLN02738 148 VRGEAFFIPLY-ELFLTYGGIFRLTFGPKSFLIVSDPSIAKHIL---RDNSKAYSKGILAEILefvmGKGLIPADGEIWR 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 942412537 184 TRRRILTPGFHFQNYNSFMDIFNEKSS-ICAaefELSIETQGDTGIDVSRLLARCTLNIICETV 246
Cdd:PLN02738 224 VRRRAIVPALHQKYVAAMISLFGQASDrLCQ---KLDAAASDGEDVEMESLFSRLTLDIIGKAV 284
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 125-279 1.83e-08

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: 55.32  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSE--WLGNSILVSSGDHWKTRRRI-LTPGFHF-QNYNS 200
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIErnFQGHGVALANGERWRILRRFsLTILRNFgMGKRS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942412537 201 FMDIFNEKSSICAAEFElsiETQGdTGIDVSRLLARCTLNIICETVMGqqTKVEMEKEIYLSNVHRFCQIFIErVKRPW 279
Cdd:cd20670   81 IEERIQEEAGYLLEEFR---KTKG-APIDPTFFLSRTVSNVISSVVFG--SRFDYEDKQFLSLLRMINESFIE-MSTPW 152
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 124-310 3.23e-08

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: 54.39  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTILS------SSKNNTKASDYLnlseWLGNSILVSS--GDHWKTRRRI-----LT 190
Cdd:cd11072    1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKthdlvfASRPKLLAARIL----SYGGKDIAFApyGEYWRQMRKIcvlelLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 191 PgfhfQNYNSFMDIFNEKSSICAAEFELSIETQgdTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEiylsnvhrfcqi 270
Cdd:cd11072   77 A----KRVQSFRSIREEEVSLLVKKIRESASSS--SPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDK------------ 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 942412537 271 FIERVKR--------------PWLsyKWIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11072  139 FKELVKEalellggfsvgdyfPSL--GWIDLLTGLDRKLEKVFKELDAFLEKII 190
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 124-293 3.53e-08

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: 54.46  E-value: 3.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNL-SEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFM 202
Cdd:cd20649    1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLiTKPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 203 DIFNEKSSICAAEFELSIETqGDTgIDVSRLLARCTLNIICETVMGqqTKVEMEK---EIYLSNVHRFCQIFIER-VKRP 278
Cdd:cd20649   81 PLINQACDVLLRNLKSYAES-GNA-FNIQRCYGCFTMDVVASVAFG--TQVDSQKnpdDPFVKNCKRFFEFSFFRpILIL 156

                        170
                 ....*....|....*
gi 942412537 279 WLSYKWIykMSPLSR 293
Cdd:cd20649  157 FLAFPFI--MIPLAR 169
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 126-310 5.16e-08

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: 53.86  E-value: 5.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSS-KNNTKASDYLNLSEWLG-NSILVSSGDHWKTRRRILTPGFhfqNYNSFMD 203
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRpDEFRRISSLESVFREMGiNGVFSAEGDAWRRQRRLVMPAF---SPKHLRY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 204 IFNEKSSIcAAEFELSIETQGDTG--IDVSRLLARCTLNIICETVMGQQTK-VEMEKEIYLSNVHRFCQIFIERVKRPwL 280
Cdd:cd11083   78 FFPTLRQI-TERLRERWERAAAEGeaVDVHKDLMRYTVDVTTSLAFGYDLNtLERGGDPLQEHLERVFPMLNRRVNAP-F 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 942412537 281 SYkWIYKMSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11083  156 PY-WRYLRLPADRALDRALVEVRALVLDII 184
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 133-207 1.09e-07

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: 52.64  E-value: 1.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942412537 133 LGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMDIFNE 207
Cdd:cd20621   10 LGSKPLISLVDPEYIKEFLQNHHYYKKKFGPLGIDRLFGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINE 84
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 125-250 1.45e-07

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 52.46  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTIL-SSSKNNTKASDY---LNLSEwlGNSILVSSGDHWKTRRRiltpgFHFQNYNS 200
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALvDQAEEFSGRGDYpvfFNFTK--GNGIAFSNGERWKILRR-----FALQTLRN 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 942412537 201 F-------MDIFNEKSSICAAEFElsiETQGdTGIDVSRLLARCTLNIICETVMGQQ 250
Cdd:cd20669   74 FgmgkrsiEERILEEAQFLLEELR---KTKG-APFDPTFLLSRAVSNIICSVVFGSR 126
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 124-190 1.55e-07

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: 52.25  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVH--------------------TILSSSKNNTKASDYlnlsewlgnsilvssGDHWK 183
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRELAHealvqkgssfasrppanplrVLFSSNKHMVNSSPY---------------GPLWR 65


                 ....*..
gi 942412537 184 TRRRILT 190
Cdd:cd11075   66 TLRRNLV 72
PLN02290 PLN02290
cytokinin trans-hydroxylase
 121-268 1.75e-07

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 52.12  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASdylnlseWL---------GNSILVSSGDHWKTRRRILTP 191
Cdd:PLN02290  89 WSKQYGKRFIYWNGTEPRLCLTETELIKELLTKYNTVTGKS-------WLqqqgtkhfiGRGLLMANGADWYHQRHIAAP 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942412537 192 GFHFQNYNSFMDIFNEKSSICAAEFELSIEtQGDTGIDVSRLLARCTLNIICETVMGqqTKVEMEKEIY--LSNVHRFC 268
Cdd:PLN02290 162 AFMGDRLKGYAGHMVECTKQMLQSLQKAVE-SGQTEVEIGEYMTRLTADIISRTEFD--SSYEKGKQIFhlLTVLQRLC 237
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 123-310 2.18e-07

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: 51.90  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 123 KKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLG-NSILVSSGDHWKTRRRILTPGFHFQNYNSF 201
Cdd:cd11044   19 QKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLGeNSLSLQDGEEHRRRRKLLAPAFSREALESY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 202 MDIFNekssicaAEFELSIETQGDTG-IDVSRLLARCTLNIICETVMGQQTKVEMEKeiylsnvhrFCQIFiERVKRPWL 280
Cdd:cd11044   99 VPTIQ-------AIVQSYLRKWLKAGeVALYPELRRLTFDVAARLLLGLDPEVEAEA---------LSQDF-ETWTDGLF 161

                        170       180       190
                 ....*....|....*....|....*....|
gi 942412537 281 SYKWIYKMSPLSReSERCINTLHTFTDKVI 310
Cdd:cd11044  162 SLPVPLPFTPFGR-AIRARNKLLARLEQAI 190
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 126-250 6.42e-07

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: 50.25  E-value: 6.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILS------SSKNNTKASDYLNLSewlGNSILVSS-GDHWKTRRRILTpgfhfqny 198
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKtqdavfASRPRTAAGKIFSYN---GQDIVFAPyGPHWRHLRKICT-------- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942412537 199 nsfMDIFNEK-----SSICAAEFELSIET-----QGDTGIDVSRLLARCTLNIICETVMGQQ 250
Cdd:cd20618   70 ---LELFSAKrlesfQGVRKEELSHLVKSlleesESGKPVNLREHLSDLTLNNITRMLFGKR 128
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 125-252 7.19e-07

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: 50.27  E-value: 7.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILssSKNNTKASD------YLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNY 198
Cdd:cd11065    1 YGPIISLKVGGQTIIVLNSPKAAKDLL--EKRSAIYSSrprmpmAGELMGWGMRLLLMPYGPRWRLHRRLFHQLLNPSAV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 942412537 199 NSFMDIFNEKSSICAAEFELSIEtqgdtgiDVSRLLARCTLNIICETVMGQQTK 252
Cdd:cd11065   79 RKYRPLQELESKQLLRDLLESPD-------DFLDHIRRYAASIILRLAYGYRVP 125
PLN02936 PLN02936
epsilon-ring hydroxylase
 121-242 7.88e-07

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 50.18  E-value: 7.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 121 WVKKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWL-GNSILVSSGDHWKTRRRILTPGFHfQNYN 199
Cdd:PLN02936  45 WMNEYGPVYRLAAGPRNFVVVSDPAIAKHVLRNYGSKYAKGLVAEVSEFLfGSGFAIAEGELWTARRRAVVPSLH-RRYL 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 942412537 200 SFM--DIFNEkssiCAAEFELSIETQGDTG--IDVSRLLARCTLNII 242
Cdd:PLN02936 124 SVMvdRVFCK----CAERLVEKLEPVALSGeaVNMEAKFSQLTLDVI 166
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 125-250 2.04e-06

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: 48.79  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTIL-SSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTPGFHFQNYNSFMD 203
Cdd:cd11049   12 HGDLVRIRLGPRPAYVVTSPELVRQVLvNDRVFDKGGPLFDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAE 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 942412537 204 IFNEkssicAAEFELSIETQGDTgIDVSRLLARCTLNIICETVMGQQ 250
Cdd:cd11049   92 VMRE-----EAEALAGSWRPGRV-VDVDAEMHRLTLRVVARTLFSTD 132
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 124-248 6.21e-06

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: 47.15  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 124 KYGPIYSVWLGPRPFVTLASPELVHTIL----SSSKNNTKASDYLNLSewLGNSILVSSGDHWKTRRRILTPGFhfqnyN 199
Cdd:cd11056    1 GGEPFVGIYLFRRPALLVRDPELIKQILvkdfAHFHDRGLYSDEKDDP--LSANLFSLDGEKWKELRQKLTPAF-----T 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 942412537 200 S----FM-DIFNEkssiCAAEFELSIETQGDTG--IDVSRLLARCTLNIICETVMG 248
Cdd:cd11056   74 SgklkNMfPLMVE----VGDELVDYLKKQAEKGkeLEIKDLMARYTTDVIASCAFG 125
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 126-256 1.29e-05

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: 46.44  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELV------HTILSSSKNNTKASDYLNlsewLGNSILVSS--GDHWKTRRRILTpgfhfqn 197
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSAAeecftkNDIVLANRPRFLTGKHIG----YNYTTVGSApyGDHWRNLRRITT------- 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 942412537 198 ynsfMDIFnekSSICAAEFeLSIETQgdtgiDVSRLLARctlniICETVMGQQTKVEME 256
Cdd:cd20653   70 ----LEIF---SSHRLNSF-SSIRRD-----EIRRLLKR-----LARDSKGGFAKVELK 110
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 137-302 1.31e-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: 46.09  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 137 PFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSS-GDHWKTRRRILTPGFHFQNYNSFMDIFNEKSSICAAE 215
Cdd:cd11051   11 PLLVVTDPELAEQITQVTNLPKPPPLRKFLTPLTGGSSLISMeGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 216 FELSIETqGDTgIDVSRLLARCTLNIICETVMG-----QQTKVEMEKEIYLSNVHRFCQIFIervkRPWLSYKWIYKMSP 290
Cdd:cd11051   91 LRELAES-GEV-FSLEELTTNLTFDVIGRVTLDidlhaQTGDNSLLTALRLLLALYRSLLNP----FKRLNPLRPLRRWR 164

                        170
                 ....*....|..
gi 942412537 291 LSRESERCINTL 302
Cdd:cd11051  165 NGRRLDRYLKPE 176
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 133-310 1.74e-05

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: 46.01  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 133 LGPRPFVTlASPELVHTILSssknnTKASDY-------LNLSEWLGNSILVSSGDHWKTRRRILTPGFhFQNYNSFMDIF 205
Cdd:cd11063   10 LGTRVIFT-IEPENIKAVLA-----TQFKDFglgerrrDAFKPLLGDGIFTSDGEEWKHSRALLRPQF-SRDQISDLELF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 206 NEKssicAAEFELSIETQGDTGiDVSRLLARCTLNIICETVMGQQTKVeMEKEIYLSNVHRFCQIF-------IERVKrp 278
Cdd:cd11063   83 ERH----VQNLIKLLPRDGSTV-DLQDLFFRLTLDSATEFLFGESVDS-LKPGGDSPPAARFAEAFdyaqkylAKRLR-- 154

                        170       180       190
                 ....*....|....*....|....*....|..
gi 942412537 279 WLSYKWIYkmspLSRESERCINTLHTFTDKVI 310
Cdd:cd11063  155 LGKLLWLL----RDKKFREACKVVHRFVDPYV 182
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 126-264 1.92e-05

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: 45.86  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 126 GPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKTRRRILTP---GFHFQNYNSFM 202
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTFRRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDwlrQFGMTKFGNGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 942412537 203 DIFNEKSSICAAEFELSIETQGDTGIDVSRLLARCTLNIICETVMGQQTKVEMEKEIYLSNV 264
Cdd:cd20652   81 AKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFL 142
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 125-302 5.46e-05

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 44.41  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWL--GNSILVSSGDHWKTRRRiltpgFHFQNYNSF- 201
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFnkGYGILFSNGENWKEMRR-----FTLTTLRDFg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 202 ------MDIFNEKSSICAAEFelsiETQGDTGIDVSRLLARCTLNIICETVMGQQTkvemekEIYLSNVHRFCQIFIERV 275
Cdd:cd20664   76 mgkktsEDKILEEIPYLIEVF----EKHKGKPFETTLSMNVAVSNIIASIVLGHRF------EYTDPTLLRMVDRINENM 145

                        170       180
                 ....*....|....*....|....*..
gi 942412537 276 KRPWLSYKWIYKMSPLSRESERCINTL 302
Cdd:cd20664  146 KLTGSPSVQLYNMFPWLGPFPGDINKL 172
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 123-190 9.23e-05

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: 43.67  E-value: 9.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942412537 123 KKYGPIYSVWLGPRPFVTLASP----ELVHT---ILSSSK--NNTKASDYLNLSEWlgnsiLVSSGDHWKTRRRILT 190
Cdd:cd11073    2 KKYGPIMSLKLGSKTTVVVSSPeaarEVLKThdrVLSGRDvpDAVRALGHHKSSIV-----WPPYGPRWRMLRKICT 73
PLN02966 PLN02966
cytochrome P450 83A1
 68-271 6.10e-04

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 41.27  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  68 LPAIAVFYYWKWSQSRTVKLMnaiPGRKPLPLLGNLLHLDVYN-EEFYKvmaiDWVKKYGPIYSVWLGPRPFVTLASPEL 146
Cdd:PLN02966  11 LAAVLLFFLYQKPKTKRYKLP---PGPSPLPVIGNLLQLQKLNpQRFFA----GWAKKYGPILSYRIGSRTMVVISSAEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 147 VHTILSSSKNNTKASDYLNLSEWLGNSILVSSGDHWKT-RRRILTPGFHFQNYNSFMDIFNEKSSICAAEFELSIETQGD 225
Cdd:PLN02966  84 AKELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPyYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAAD 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 942412537 226 TG--IDVSRLLARCTLNIICETVMGQQTKVEMEKeiylsnVHRFCQIF 271
Cdd:PLN02966 164 KSevVDISELMLTFTNSVVCRQAFGKKYNEDGEE------MKRFIKIL 205
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 70-250 6.74e-04

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 40.96  E-value: 6.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537  70 AIAVFYYWKWSQSRTVKLMNAIPGRKPLPLLGNLLHLdvyNEEFYKVMAiDWVKKYGPIYSVWLGPRPFVTLASPELVHT 149
Cdd:PLN03112  13 LIFNVLIWRWLNASMRKSLRLPPGPPRWPIVGNLLQL---GPLPHRDLA-SLCKKYGPLVYLRLGSVDAITTDDPELIRE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 150 ILS------SSKNNTKASDYLNLSewLGNSILVSSGDHWKTRRRI-----LTPgfhfQNYNSFMDIFNEKSSiCAAEFEL 218
Cdd:PLN03112  89 ILLrqddvfASRPRTLAAVHLAYG--CGDVALAPLGPHWKRMRRIcmehlLTT----KRLESFAKHRAEEAR-HLIQDVW 161

                        170       180       190
                 ....*....|....*....|....*....|..
gi 942412537 219 SIETQGDTgIDVSRLLARCTLNIICETVMGQQ 250
Cdd:PLN03112 162 EAAQTGKP-VNLREVLGAFSMNNVTRMLLGKQ 192
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 122-242 9.93e-04

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: 40.63  E-value: 9.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 122 VKKYGPIYSVWLGPRPFVTLASPELVhTILSSSKNNTKA--SDYLNLSEWLGNSILVSSGD--HWKTRRRILTPGF---H 194
Cdd:cd11068    9 ADELGPIFKLTLPGRRVVVVSSHDLI-AELCDESRFDKKvsGPLEELRDFAGDGLFTAYTHepNWGKAHRILMPAFgplA 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 942412537 195 FQNYNSFM-DIfnekssicAAEFELSIETQG-DTGIDVSRLLARCTLNII 242
Cdd:cd11068   88 MRGYFPMMlDI--------AEQLVLKWERLGpDEPIDVPDDMTRLTLDTI 129
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 123-310 1.16e-03

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: 40.20  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 123 KKYGPIYSVWLGPRPFVTLASPELVHTIL-SSSKN----NTKASDYLNLS--EWLGnsILVSSGDHWKTRRRILTPGF-H 194
Cdd:cd11054    2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFrNEGKYpirpSLEPLEKYRKKrgKPLG--LLNSNGEEWHRLRSAVQKPLlR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 195 FQNYNSFMDIFNEkssiCAAEF----ELSIETQGDTGIDVSRLLARCTLNIICETVMGQ-----QTKVEMEKEIYLSNVH 265
Cdd:cd11054   80 PKSVASYLPAINE----VADDFveriRRLRDEDGEEVPDLEDELYKWSLESIGTVLFGKrlgclDDNPDSDAQKLIEAVK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 942412537 266 RFCQIFIERVKRPWLsYKWIYkmSPLSRESERCINTLHTFTDKVI 310
Cdd:cd11054  156 DIFESSAKLMFGPPL-WKYFP--TPAWKKFVKAWDTIFDIASKYV 197
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 123-197 4.84e-03

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 38.56  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942412537 123 KKYGPIYSVWLGPRPFVTLASPELVHTILSS------SKNNTKASDYLNlsewlGNS---ILVSSGDHWKTRRRILTPGF 193
Cdd:PLN02394  61 KKYGDVFLLRMGQRNLVVVSSPELAKEVLHTqgvefgSRTRNVVFDIFT-----GKGqdmVFTVYGDHWRKMRRIMTVPF 135


                 ....
gi 942412537 194 hFQN 197
Cdd:PLN02394 136 -FTN 138
PTZ00404 PTZ00404
cytochrome P450; Provisional
 123-189 7.60e-03

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 37.78  E-value: 7.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942412537 123 KKYGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEW--LGNSILVSSGDHWKTRRRIL 189
Cdd:PTZ00404  59 KKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHgtFYHGIVTSSGEYWKRNREIV 127
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 125-187 8.73e-03

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: 37.63  E-value: 8.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 942412537 125 YGPIYSVWLGPRPFVTLASPELVHTILSSSKNNTKASDYLNLSEWL--GNSILVSSGDHWKTRRR 187
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVnkGLGIVFSNGERWKETRR 65
 
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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