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Conserved domains on  [gi|15218908|ref|NP_176777|]
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cytochrome P450, family 96, subfamily A, polypeptide 14 pseudogene [Arabidopsis thaliana]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 1-166 1.18e-46

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 PLN02169:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 500  Bit Score: 158.63  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908    1 MALIGLIEAFIAFVCFLIF---YYFLIKKPYSYILIKisqsglwNWPVLGMSPGALMRLPRIYDFSVDLLENSNLTFHFK 77
Cdd:PLN02169   1 MAMLGLLEFFVAFIFFLVClftCFFIHKKPHGQPILK-------NWPFLGMLPGMLHQIPRIYDWTVEVLEASNLTFYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908   78 GPWFAGIDILATADSVNINHI-------YYRGPELREIFGPFGDGIINSDSELWRNLKKATQVIFNHQKYQKFSTSTTRS 150
Cdd:PLN02169  74 GPWLSGTDMLFTADPKNIHHIlssnfgnYPKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFHNQDFIELSLSSNKS 153

                        170
                 ....*....|....*...
gi 15218908  151 KLKLGLVPLFND--HENL 166
Cdd:PLN02169 154 KLKEGLVPFLDNaaHENI 171
 
Name Accession Description Interval E-value
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 1-166 1.18e-46

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 158.63  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908    1 MALIGLIEAFIAFVCFLIF---YYFLIKKPYSYILIKisqsglwNWPVLGMSPGALMRLPRIYDFSVDLLENSNLTFHFK 77
Cdd:PLN02169   1 MAMLGLLEFFVAFIFFLVClftCFFIHKKPHGQPILK-------NWPFLGMLPGMLHQIPRIYDWTVEVLEASNLTFYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908   78 GPWFAGIDILATADSVNINHI-------YYRGPELREIFGPFGDGIINSDSELWRNLKKATQVIFNHQKYQKFSTSTTRS 150
Cdd:PLN02169  74 GPWLSGTDMLFTADPKNIHHIlssnfgnYPKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFHNQDFIELSLSSNKS 153

                        170
                 ....*....|....*...
gi 15218908  151 KLKLGLVPLFND--HENL 166
Cdd:PLN02169 154 KLKEGLVPFLDNaaHENI 171
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 74-159 1.03e-19

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: 84.56  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908  74 FHFKGPWFAGIDILATADSVNINHI-------YYRGPELREIFGP-FGDGIINSDSELWRNLKKATQVIFNHQKYQKFST 145
Cdd:cd11064   1 FTFRGPWPGGPDGIVTADPANVEHIlktnfdnYPKGPEFRDLFFDlLGDGIFNVDGELWKFQRKTASHEFSSRALREFME 80

                        90
                ....*....|....
gi 15218908 146 STTRSKLKLGLVPL 159
Cdd:cd11064  81 SVVREKVEKLLVPL 94
 
Name Accession Description Interval E-value
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 1-166 1.18e-46

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 158.63  E-value: 1.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908    1 MALIGLIEAFIAFVCFLIF---YYFLIKKPYSYILIKisqsglwNWPVLGMSPGALMRLPRIYDFSVDLLENSNLTFHFK 77
Cdd:PLN02169   1 MAMLGLLEFFVAFIFFLVClftCFFIHKKPHGQPILK-------NWPFLGMLPGMLHQIPRIYDWTVEVLEASNLTFYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908   78 GPWFAGIDILATADSVNINHI-------YYRGPELREIFGPFGDGIINSDSELWRNLKKATQVIFNHQKYQKFSTSTTRS 150
Cdd:PLN02169  74 GPWLSGTDMLFTADPKNIHHIlssnfgnYPKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFHNQDFIELSLSSNKS 153

                        170
                 ....*....|....*...
gi 15218908  151 KLKLGLVPLFND--HENL 166
Cdd:PLN02169 154 KLKEGLVPFLDNaaHENI 171
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 74-159 1.03e-19

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: 84.56  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908  74 FHFKGPWFAGIDILATADSVNINHI-------YYRGPELREIFGP-FGDGIINSDSELWRNLKKATQVIFNHQKYQKFST 145
Cdd:cd11064   1 FTFRGPWPGGPDGIVTADPANVEHIlktnfdnYPKGPEFRDLFFDlLGDGIFNVDGELWKFQRKTASHEFSSRALREFME 80

                        90
                ....*....|....
gi 15218908 146 STTRSKLKLGLVPL 159
Cdd:cd11064  81 SVVREKVEKLLVPL 94
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 37-155 2.14e-11

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 60.95  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218908   37 QSGLWNWPVLGMSPGALMRLPRIYDFSVDLLENSnLTFHFKGPwfaGIDILATADSVNINHI-------YYRGPELREIF 109
Cdd:PLN03195  32 RKGPKSWPIIGAALEQLKNYDRMHDWLVEYLSKD-RTVVVKMP---FTTYTYIADPVNVEHVlktnfanYPKGEVYHSYM 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15218908  110 GPF-GDGIINSDSELWRNLKKATQVIFNHQKYQKFSTSTTRS-KLKLG 155
Cdd:PLN03195 108 EVLlGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVFREySLKLS 155
 
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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