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Conserved domains on  [gi|530377130|ref|XP_005262777|]
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cytochrome P450 2U1 isoform X2 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
163-327 2.39e-116

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 cd20666:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 426  Bit Score: 342.91  E-value: 2.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20666  262 QEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAP 322
Cdd:cd20666  342 IWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPSMEGRFGLTLAP 421

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20666  422 CPFNI 426
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
61-156 6.81e-08

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 PTZ00404:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 482  Bit Score: 53.57  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  61 PGPTPWPLVGNFGHvllppflrrrswLSSRtraagidpsvigPQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREAL 140
Cdd:PTZ00404  32 KGPIPIPILGNLHQ------------LGNL------------PHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMF 87
                         90
                 ....*....|....*.
gi 530377130 141 VQQAEVFSDRPRVPLI 156
Cdd:PTZ00404  88 VDNFDNFSDRPKIPSI 103
 
Name Accession Description Interval E-value
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
163-327 2.39e-116

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 342.91  E-value: 2.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20666  262 QEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAP 322
Cdd:cd20666  342 IWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPSMEGRFGLTLAP 421

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20666  422 CPFNI 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
164-325 5.24e-62

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: 204.43  E-value: 5.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:pfam00067 296 EKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEV 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAPH 323
Cdd:pfam00067 376 FPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPK 455

                  ..
gi 530377130  324 PF 325
Cdd:pfam00067 456 PY 457
PTZ00404 PTZ00404
cytochrome P450; Provisional
163-332 1.49e-34

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 131.77  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRDP 241
Cdd:PTZ00404 317 QEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLikkeTFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAlPEDSKKPLLTGRFGLTLA 321
Cdd:PTZ00404 397 KYFENPEQFDPSRFLNPDSND----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLK-SIDGKKIDETEEYGLTLK 471
                        170
                 ....*....|.
gi 530377130 322 PHPFNITISRR 332
Cdd:PTZ00404 472 PNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
189-299 4.22e-20

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: 89.95  E-value: 4.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 189 PYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflddqgqliKKETF 268
Cdd:COG2124  268 ELLPAAVEETLRLYPPVP-LLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAH 337
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530377130 269 IPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:COG2124  338 LPFGGGPHRCLGAALARLEARIALATLLRRF 368
PTZ00404 PTZ00404
cytochrome P450; Provisional
61-156 6.81e-08

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.57  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  61 PGPTPWPLVGNFGHvllppflrrrswLSSRtraagidpsvigPQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREAL 140
Cdd:PTZ00404  32 KGPIPIPILGNLHQ------------LGNL------------PHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMF 87
                         90
                 ....*....|....*.
gi 530377130 141 VQQAEVFSDRPRVPLI 156
Cdd:PTZ00404  88 VDNFDNFSDRPKIPSI 103
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
103-161 1.37e-07

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 52.89  E-value: 1.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 103 PQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRPRVPLISIVTK 161
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTN 59
 
Name Accession Description Interval E-value
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
163-327 2.39e-116

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 342.91  E-value: 2.39e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20666  262 QEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAP 322
Cdd:cd20666  342 IWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPSMEGRFGLTLAP 421

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20666  422 CPFNI 426
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
163-327 1.42e-96

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: 292.16  E-value: 1.42e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11026  260 QEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPK 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRF-GLTLA 321
Cdd:cd11026  340 QWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDPDLTPRFsGFTNS 419

                 ....*.
gi 530377130 322 PHPFNI 327
Cdd:cd11026  420 PRPYQL 425
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
164-327 3.97e-79

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 247.52  E-value: 3.97e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20651  260 RKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEY 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAPH 323
Cdd:cd20651  340 WGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDLEGIPGGITLSPK 419

                 ....
gi 530377130 324 PFNI 327
Cdd:cd20651  420 PFRV 423
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
163-327 2.43e-78

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: 245.58  E-value: 2.43e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11027  263 QAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPK 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKK-ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLA 321
Cdd:cd11027  343 EWDDPDEFRPERFLDENGKLVPKpESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPELEGIPGLVLY 422

                 ....*.
gi 530377130 322 PHPFNI 327
Cdd:cd11027  423 PLPYKV 428
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
164-327 3.06e-73

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: 232.10  E-value: 3.06e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20617  258 EKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKY 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGqLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFaLPEDSKKPLLTGRFGLTLAPH 323
Cdd:cd20617  338 FEDPEEFNPERFLENDG-NKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKF-KSSDGLPIDEKEVFGLTLKPK 415

                 ....
gi 530377130 324 PFNI 327
Cdd:cd20617  416 PFKV 419
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
165-325 4.81e-67

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 216.48  E-value: 4.81e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:cd20663  266 RVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVW 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAPHP 324
Cdd:cd20663  346 EKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPAGQPRPSDHGVFAFLVSPSP 425

                 .
gi 530377130 325 F 325
Cdd:cd20663  426 Y 426
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
164-327 3.90e-66

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 214.08  E-value: 3.90e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11028  266 EKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKL 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKK--ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAlPEDSKKPLLTGRFGLTLA 321
Cdd:cd11028  346 WPDPSVFRPERFLDDNGLLDKTkvDKFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFS-VKPGEKLDLTPIYGLTMK 424

                 ....*.
gi 530377130 322 PHPFNI 327
Cdd:cd11028  425 PKPFKV 430
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
163-327 2.10e-62

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 204.26  E-value: 2.10e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20662  259 QEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPK 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDqGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDsKKPLLTGRFGLTLAP 322
Cdd:cd20662  339 EWATPDTFNPGHFLEN-GQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPN-EKLSLKFRMGITLSP 416

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20662  417 VPHRI 421
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
164-325 5.24e-62

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: 204.43  E-value: 5.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:pfam00067 296 EKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEV 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAPH 323
Cdd:pfam00067 376 FPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPK 455

                  ..
gi 530377130  324 PF 325
Cdd:pfam00067 456 PY 457
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
161-327 1.03e-60

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: 199.94  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 161 KEKEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20652  266 KEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMD 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTL 320
Cdd:cd20652  346 PNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIALPDGQPVDSEGGNVGITL 425

                 ....*..
gi 530377130 321 APHPFNI 327
Cdd:cd20652  426 TPPPFKI 432
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
163-327 1.98e-60

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 199.65  E-value: 1.98e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20661  272 QGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEK 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSkKPLLTGRFGLTLAP 322
Cdd:cd20661  352 YWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGL-IPDLKPKLGMTLQP 430

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20661  431 QPYLI 435
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
163-324 1.71e-59

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: 196.57  E-value: 1.71e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRaPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20664  259 QKKVQEEIDRVIGSRQ-PQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKT 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLL--TGRFGLTL 320
Cdd:cd20664  338 EWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPPGVSEDDLdlTPGLGFTL 417

                 ....
gi 530377130 321 APHP 324
Cdd:cd20664  418 NPLP 421
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
163-325 6.45e-58

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 192.92  E-value: 6.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20673  266 QKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEK 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKK--ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTL 320
Cdd:cd20673  346 EWDQPDQFMPERFLDPTGSQLISpsLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGQLPSLEGKFGVVL 425

                 ....*
gi 530377130 321 APHPF 325
Cdd:cd20673  426 QIDPF 430
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
163-309 8.64e-56

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 186.93  E-value: 8.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20668  260 EAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPK 339
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKK 309
Cdd:cd20668  340 FFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPED 406
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
163-332 6.49e-53

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: 179.74  E-value: 6.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20670  260 EAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPK 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFafalpedSKKPLLtgrfgltlap 322
Cdd:cd20670  340 YFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNF-------SLRSLV---------- 402
                        170
                 ....*....|
gi 530377130 323 HPFNITISRR 332
Cdd:cd20670  403 PPADIDITPK 412
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
164-325 8.98e-53

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: 179.19  E-value: 8.98e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20669  261 ARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQ 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAF---ALPED-SKKPLLTgrfGLT 319
Cdd:cd20669  341 FKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLqplGAPEDiDLTPLSS---GLG 417

                 ....*.
gi 530377130 320 LAPHPF 325
Cdd:cd20669  418 NVPRPF 423
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
164-299 1.97e-51

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: 175.53  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20665  261 AKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKE 340
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20665  341 FPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNF 396
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
163-330 2.09e-50

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 172.98  E-value: 2.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20674  260 QDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDET 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGqliKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAP 322
Cdd:cd20674  340 VWEQPHEFRPERFLEPGA---ANRALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALPSLQPVAGINLKV 416

                 ....*...
gi 530377130 323 HPFNITIS 330
Cdd:cd20674  417 QPFQVRLQ 424
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
164-327 4.29e-50

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 172.27  E-value: 4.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20672  261 EKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQY 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGR-FGLTLAP 322
Cdd:cd20672  341 FEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVASPVAPEDIDLTPKeSGVGKIP 420

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20672  421 PTYQI 425
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
163-327 5.88e-50

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 171.95  E-value: 5.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20667  259 QEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPE 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTLAP 322
Cdd:cd20667  339 CWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLPEGVQELNLEYVFGGTLQP 418

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20667  419 QPYKI 423
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
163-322 7.39e-49

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 169.04  E-value: 7.39e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20676  271 QKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEK 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKK---ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPeDSKKPLLTGRFGLT 319
Cdd:cd20676  351 LWKDPSSFRPERFLTADGTEINKtesEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVP-PGVKVDMTPEYGLT 429

                 ...
gi 530377130 320 LAP 322
Cdd:cd20676  430 MKH 432
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
165-327 1.22e-48

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 168.74  E-value: 1.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:cd20677  272 KIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLW 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLDDQGQLIKK--ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPlLTGRFGLTLAP 322
Cdd:cd20677  352 KDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKCLGEDVARNEIFVFLTTILQQLKLEKPPGQKLD-LTPVYGLTMKP 430

                 ....*
gi 530377130 323 HPFNI 327
Cdd:cd20677  431 KPYRL 435
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
161-327 2.83e-48

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 167.49  E-value: 2.83e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 161 KEKEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20675  267 DVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHD 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLmFVSLM--QSFAFALPEDSkkPLLTGRF 316
Cdd:cd20675  347 PQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCIGEELSKMQLFL-FTSILahQCNFTANPNEP--LTMDFSY 423
                        170
                 ....*....|.
gi 530377130 317 GLTLAPHPFNI 327
Cdd:cd20675  424 GLTLKPKPFTI 434
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
163-324 1.13e-46

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 163.04  E-value: 1.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20671  257 QKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKT 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFaLPEDSKKPL---LTGRFGLT 319
Cdd:cd20671  336 QWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTF-LPPPGVSPAdldATPAAAFT 414

                 ....*
gi 530377130 320 LAPHP 324
Cdd:cd20671  415 MRPQP 419
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
165-325 5.89e-46

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: 161.21  E-value: 5.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:cd11065  259 KAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVY 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLDDqGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKK--PLLTGRF--G 317
Cdd:cd11065  339 PDPEEFDPERYLDD-PKGTPDPPdppHFAFGFGRRICPGRHLAENSLFIAIARLLWAFDIKKPKDEGGkeIPDEPEFtdG 417

                 ....*...
gi 530377130 318 LTLAPHPF 325
Cdd:cd11065  418 LVSHPLPF 425
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
164-320 5.35e-42

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: 150.78  E-value: 5.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20618  264 RKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPL-LTGRFGLTL 320
Cdd:cd20618  344 WEDPLEFKPERFLESDIDDVKGQDFelLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDWSLPGPKPEDIdMEEKFGLTV 423
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
164-321 4.30e-41

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: 148.45  E-value: 4.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11073  266 AKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSV 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKE-TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPE--DSKKPLLTGRFGLTL 320
Cdd:cd11073  346 WEDPLEFKPERFLGSEIDFKGRDfELIPFGSGRRICPGLPLAERMVHLVLASLLHSFDWKLPDgmKPEDLDMEEKFGLTL 425

                 .
gi 530377130 321 A 321
Cdd:cd11073  426 Q 426
PTZ00404 PTZ00404
cytochrome P450; Provisional
163-332 1.49e-34

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 131.77  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRDP 241
Cdd:PTZ00404 317 QEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLikkeTFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAlPEDSKKPLLTGRFGLTLA 321
Cdd:PTZ00404 397 KYFENPEQFDPSRFLNPDSND----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLK-SIDGKKIDETEEYGLTLK 471
                        170
                 ....*....|.
gi 530377130 322 PHPFNITISRR 332
Cdd:PTZ00404 472 PNKFKVLLEKR 482
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
164-321 1.62e-34

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: 130.66  E-value: 1.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11072  263 KKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKY 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDD----QGQLIKketFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK--KPLLTGRFG 317
Cdd:cd11072  343 WEDPEEFRPERFLDSsidfKGQDFE---LIPFGAGRRICPGITFGLANVELALANLLYHFDWKLPDGMKpeDLDMEEAFG 419

                 ....
gi 530377130 318 LTLA 321
Cdd:cd11072  420 LTVH 423
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
164-327 2.12e-34

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: 130.34  E-value: 2.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGAN-RAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20628  264 EKVYEELDEIFGDDdRRPTLEDLNKMKYLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPE 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAF--ALPEDSKKPlltgRFGLTL 320
Cdd:cd20628  343 YFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVlpVPPGEDLKL----IAEIVL 418

                 ....*...
gi 530377130 321 AP-HPFNI 327
Cdd:cd20628  419 RSkNGIRV 426
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
164-332 4.31e-33

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 126.96  E-value: 4.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20654  276 KKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNV 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQL-IKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPedSKKPL-LTGRFGLT 319
Cdd:cd20654  356 WSDPLEFKPERFLTTHKDIdVRGQNFelIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTP--SNEPVdMTEGPGLT 433
                        170
                 ....*....|....
gi 530377130 320 LAP-HPFNITISRR 332
Cdd:cd20654  434 NPKaTPLEVLLTPR 447
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
164-299 9.51e-33

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: 125.80  E-value: 9.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20653  262 KKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKL 341
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 244 WEKPEDFYPNRFlDDQGQLIKKetFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20653  342 WEDPTKFKPERF-EGEEREGYK--LIPFGLGRRACPGAGLAQRVVGLALGSLIQCF 394
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
164-315 9.74e-33

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: 125.38  E-value: 9.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20620  247 ARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRF 324
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK---KPLLTGR 315
Cdd:cd20620  325 WPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPvepEPLITLR 399
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
164-306 3.13e-32

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: 123.78  E-value: 3.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLtdkAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd00302  237 ERLRAEIDAVLGDGTPEDL---SKLPYLEAVVEETLRLYPPVPL-LPRVATEDVELGGYTIPAGTLVLLSLYAAHRDPEV 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530377130 244 WEKPEDFYPNRFLDDQGqlIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:cd00302  313 FPDPDEFDPERFLPERE--EPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPD 373
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
163-305 3.53e-32

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 124.52  E-value: 3.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20656  264 QEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPA 343
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 243 IWEKPEDFYPNRFLDDQGQlIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPE 305
Cdd:cd20656  344 VWKNPLEFRPERFLEEDVD-IKGHDFrlLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPE 407
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
165-320 7.32e-32

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 123.69  E-value: 7.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:cd20657  264 KAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVW 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLDDQGQLI--KKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGR--FGL 318
Cdd:cd20657  344 ENPLEFKPERFLPGRNAKVdvRGNDFelIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELNMEeaFGL 423

                 ..
gi 530377130 319 TL 320
Cdd:cd20657  424 AL 425
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
164-322 9.92e-32

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: 123.08  E-value: 9.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLtvvVPLAIPHM--TSENTVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11055  261 EKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRL---YPPAFFISreCKEDCTINGVFIPKGVDVVIPVYAIHHDP 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFaLPEDSKKPLLTGRFGLTLA 321
Cdd:cd11055  338 EFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRF-VPCKETEIPLKLVGGATLS 416

                 .
gi 530377130 322 P 322
Cdd:cd11055  417 P 417
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
164-313 5.43e-30

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: 118.62  E-value: 5.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIpHMTSENTVLQG--YTIPKGTLILPNLWSVHRDP 241
Cdd:cd11046  275 AKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLI-RRAVEDDKLPGggVKVPAGTDIFISVYNLHRSP 353
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 242 AIWEKPEDFYPNRFLDDQG----QLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLT 313
Cdd:cd11046  354 ELWEDPEEFDPERFLDPFInppnEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMT 429
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
164-299 1.87e-29

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: 116.86  E-value: 1.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11054  266 EKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAP-GNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEY 344
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd11054  345 FPDPEEFIPERWLRDDSENKNIHPFasLPFGFGPRMCIGRRFAELEMYLLLAKLLQNF 402
PLN02687 PLN02687
flavonoid 3'-monooxygenase
165-320 3.27e-29

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 117.22  E-value: 3.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN02687 333 KAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQW 412
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFL---DDQGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED--SKKPLLTGRFG 317
Cdd:PLN02687 413 PDPLEFRPDRFLpggEHAGVDVKGSDFelIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGqtPDKLNMEEAYG 492

                 ...
gi 530377130 318 LTL 320
Cdd:PLN02687 493 LTL 495
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
164-305 3.86e-29

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: 115.80  E-value: 3.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11075  266 EKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKV 345
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQ--------LIKketFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPE 305
Cdd:cd11075  346 WEDPEEFKPERFLAGGEAadidtgskEIK---MMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVE 412
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
163-323 9.32e-29

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 114.88  E-value: 9.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11074  267 QKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPA 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLT---GRF 316
Cdd:cd11074  347 HWKKPEEFRPERFLEEESKVEANGNdfrYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPPGQSKIDTSekgGQF 426

                 ....*..
gi 530377130 317 GLTLAPH 323
Cdd:cd11074  427 SLHILKH 433
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
165-323 1.83e-28

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 114.83  E-value: 1.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN02394 329 KLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELW 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLDDQGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLT---GRFGL 318
Cdd:PLN02394 409 KNPEEFRPERFLEEEAKVEANGNdfrFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQSKIDVSekgGQFSL 488

                 ....*
gi 530377130 319 TLAPH 323
Cdd:PLN02394 489 HIAKH 493
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
164-308 3.02e-28

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 113.46  E-value: 3.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20655  263 EKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPL-LVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNY 341
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKET------FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:cd20655  342 WEDPLEFKPERFLASSRSGQELDVrgqhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEK 412
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
164-311 3.60e-28

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 113.02  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPsLTDKA--QMPYTEATIMEVQRLTVVVPLAIpHMTSENTVL--QGYTIPKGTLILPNLWSVHR 239
Cdd:cd11056  264 EKLREEIDEVLEKHGGE-LTYEAlqEMKYLDQVVNETLRKYPPLPFLD-RVCTKDYTLpgTDVVIEKGTPVIIPVYALHH 341
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 240 DPAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPL 311
Cdd:cd11056  342 DPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPL 413
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
163-323 6.33e-28

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: 112.29  E-value: 6.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGAnraPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11053  257 LARLLAELDALGGD---PDPEDIAKLPYLDAVIKETLRLYPVAP-LVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPD 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQgqlIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDskKPLLTGRFGLTLAP 322
Cdd:cd11053  333 LYPDPERFRPERFLGRK---PSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDP--RPERPVRRGVTLAP 407

                 .
gi 530377130 323 H 323
Cdd:cd11053  408 S 408
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
164-320 3.50e-27

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 111.10  E-value: 3.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:PLN00110 324 KRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDV 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKE----TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGrFGLT 319
Cdd:PLN00110 404 WENPEEFRPERFLSEKNAKIDPRgndfELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEA-FGLA 482

                 .
gi 530377130 320 L 320
Cdd:PLN00110 483 L 483
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
164-322 4.25e-27

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: 110.30  E-value: 4.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20613  269 KRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEY 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL-PEDSKKPLLTGrfglTLAP 322
Cdd:cd20613  348 FEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELvPGQSFGILEEV----TLRP 423
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
164-314 1.92e-26

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: 108.41  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20659  262 QKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKPITIDGVTLPAGTLIAINIYALHHNPTV 340
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTG 314
Cdd:cd20659  341 WEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPG 411
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
164-287 6.09e-26

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: 106.96  E-value: 6.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGA-NRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20660  267 EKVHEELDRIFGDsDRPATMDDLKEMKYLECVIKEALRLFPSVPM-FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPR 345
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKME 287
Cdd:cd20660  346 QFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALME 390
PLN02183 PLN02183
ferulate 5-hydroxylase
164-322 3.61e-25

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 105.70  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIpHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:PLN02183 339 KRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLL-HETAEDAEVAGYFIPKRSRVMINAWAIGRDKNS 417
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKE--TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPeDSKKPL---LTGRFGL 318
Cdd:PLN02183 418 WEDPDTFKPSRFLKPGVPDFKGShfEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELP-DGMKPSeldMNDVFGL 496

                 ....
gi 530377130 319 TlAP 322
Cdd:PLN02183 497 T-AP 499
PLN02655 PLN02655
ent-kaurene oxidase
161-305 9.67e-25

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 104.05  E-value: 9.67e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 161 KEKEKVHEEIERVIGANRApSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:PLN02655 294 DKQERLYREIREVCGDERV-TEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMD 372
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPE 305
Cdd:PLN02655 373 KKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLRE 437
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
164-292 1.61e-24

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: 103.18  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDKA---QMPYTEATIMEVQRLTVVVPLaIPHMTSENTVL-----QGYTIPKGTLILPNLW 235
Cdd:cd11070  258 DWLREEIDSVLG-DEPDDWDYEEdfpKLPYLLAVIYETLRLYPPVQL-LNRKTTEPVVVitglgQEIVIPKGTYVGYNAY 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 236 SVHRDPAIWEK-PEDFYPNRFLDDQGQLIK-------KETFIPFGIGKRVCMGEQLAKME----LFLMF 292
Cdd:cd11070  336 ATHRDPTIWGPdADEFDPERWGSTSGEIGAatrftpaRGAFIPFSAGPRACLGRKFALVEfvaaLAELF 404
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
164-332 3.08e-24

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: 102.26  E-value: 3.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGAnRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQG-YTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11068  265 AKARAEVDEVLGD-DPPPYEQVAKLRYIRRVLDETLRLWPTAP-AFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPS 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IW-EKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKkplLTGRFGLTLA 321
Cdd:cd11068  343 VWgEDAEEFRPERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDPDYE---LDIKETLTLK 419
                        170
                 ....*....|.
gi 530377130 322 PHPFNITISRR 332
Cdd:cd11068  420 PDGFRLKARPR 430
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
164-324 1.29e-23

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 100.38  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDK-AQMPYTEATIMEVQRLTVVVPLAIPHMT-SENTVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11061  251 EKLRAELDSTFPSDDEIRLGPKlKSLPYLRACIDEALRLSPPVPSGLPRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIK-KETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTL 320
Cdd:cd11061  331 RYFPDPFEFIPERWLSRPEELVRaRSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGEDGEAGEGGFKDAF 410

                 ....
gi 530377130 321 APHP 324
Cdd:cd11061  411 GRGP 414
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
164-306 3.52e-23

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 99.36  E-value: 3.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20658  272 RKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKV 351
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:cd20658  352 WDDPLKFKPERHLNEDSEVTLTEPdlrFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPN 417
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
164-324 9.60e-23

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 97.87  E-value: 9.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIgANRAPSLTDK-AQMPYTEATIMEVQRLtvvVPLA--IPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20650  263 QKLQEEIDAVL-PNKAPPTYDTvMQMEYLDMVVNETLRL---FPIAgrLERVCKKDVEINGVFIPKGTVVMIPTYALHRD 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGRFGLTL 320
Cdd:cd20650  339 PQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLKLSLQGLLQ 418

                 ....
gi 530377130 321 APHP 324
Cdd:cd20650  419 PEKP 422
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
163-308 1.26e-22

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: 97.71  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANraPSLTDK--AQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20621  263 QEKLRQEIKSVVGND--DDITFEdlQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFN 340
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:cd20621  341 PKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPK 408
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
164-316 1.36e-22

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: 97.73  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKA--QMPYTEATIMEVQRLTVVVPLAiPHMTSENTVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11069  270 ERLREEIRAALPDPPDGDLSYDDldRLPYLNAVCRETLRLYPPVPLT-SREATKDTVIKGVPIPKGTVVLIPPAAINRSP 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 242 AIW-EKPEDFYPNRFLDDQGQLIKKE-----TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTGR 315
Cdd:cd11069  349 EIWgPDAEEFNPERWLEPDGAASPGGagsnyALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVERPIGI 428

                 .
gi 530377130 316 F 316
Cdd:cd11069  429 I 429
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
164-301 2.89e-22

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: 96.52  E-value: 2.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIG-ANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11057  262 EKVYEEIMEVFPdDGQFITYEDLQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQLsNGVVIPKGTTIVIDIFNMHRRK 340
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377130 242 AIW-EKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAF 301
Cdd:cd11057  341 DIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
164-288 4.19e-22

unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized fungal cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 95.83  E-value: 4.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIG-ANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSEN-TVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11059  256 EKLREELAGLPGpFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGTIVSTQAYSLHRDP 335
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIK--KETFIPFGIGKRVCMGEQLAKMEL 288
Cdd:cd11059  336 EVFPDPEEFDPERWLDPSGETARemKRAFWPFGSGSRMCIGMNLALMEM 384
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
164-306 7.65e-22

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 95.36  E-value: 7.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAP-SLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11042  247 EALREEQKEVLGDGDDPlTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEgGGYVIPKGHIVLASPAVSHRDP 326
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKE--TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:cd11042  327 EIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDS 393
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
164-299 7.85e-22

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 95.46  E-value: 7.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAP--SLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11066  265 EKAYEEILEAYGNDEDAweDCAAEEKCPYVVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDP 344
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd11066  345 EHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLF 402
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
163-299 1.40e-21

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 94.73  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSEN-TVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd20646  267 QERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVP-GNARVIVEKeVVVGDYLFPKNTLFHLCHYAVSHDE 345
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20646  346 TNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRF 403
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
165-320 1.50e-21

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 94.32  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPL-AIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11076  260 KAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLlSWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHV 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 WEKPEDFYPNRFLDDQGQlikKETFI--------PFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFaLPEDSKKPLLTGR 315
Cdd:cd11076  340 WEDPLEFKPERFVAAEGG---ADVSVlgsdlrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEW-LPDDAKPVDLSEV 415

                 ....*
gi 530377130 316 FGLTL 320
Cdd:cd11076  416 LKLSC 420
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
164-291 1.69e-21

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 94.25  E-value: 1.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11049  255 RRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEV 332
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLM 291
Cdd:cd11049  333 YPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLA 380
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
164-328 3.43e-21

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: 93.54  E-value: 3.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAP-SLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd11083  257 ARVREEVDAVLGGARVPpLLEALDRLPYLEAVARETLRLKPVAPL-LFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAE 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 243 IWEKPEDFYPNRFLDDQGQLIKKE--TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPllTGRFGLTL 320
Cdd:cd11083  336 HFPDPEEFDPERWLDGARAAEPHDpsSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPAV--GEEFAFTM 413

                 ....*...
gi 530377130 321 APHPFNIT 328
Cdd:cd11083  414 SPEGLRVR 421
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
164-308 4.70e-21

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 93.03  E-value: 4.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPS-LTDKA--QMPYTEATIMEVQRLTVVVPLAIP-HMTSENTVLQGYTIPKGTLILPNLWSVHR 239
Cdd:cd11060  257 AKLRAEIDAAVAEGKLSSpITFAEaqKLPYLQAVIKEALRLHPPVGLPLErVVPPGGATICGRFIPGGTIVGVNPWVIHR 336
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 240 DPAIW-EKPEDFYPNRFLDDQGQLIKKE--TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:cd11060  337 DKEVFgEDADVFRPERWLEADEEQRRMMdrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDPEK 408
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
164-296 7.69e-21

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 92.31  E-value: 7.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDK--AQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRD 240
Cdd:cd11082  255 AKVREEQARLRP-NDEPPLTLDllEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQ 332
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 241 PaiWEKPEDFYPNRFLDDQGQLIK-KETFIPFGIGKRVCMGEQLAKMEL--FLMFVSLM 296
Cdd:cd11082  333 G--FPEPDKFDPDRFSPERQEDRKyKKNFLVFGAGPHQCVGQEYAINHLmlFLALFSTL 389
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
163-299 1.03e-20

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 92.18  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAiPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20645  260 QQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFT-SRTLDKDTVLGDYLLPKGTVLMINSQALGSSEE 338
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 243 IWEKPEDFYPNRFLDDQGQlIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20645  339 YFEDGRQFKPERWLQEKHS-INPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKY 394
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
164-306 1.44e-20

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: 91.58  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEiERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTsENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11044  258 EKLRQE-QDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVL-EDFELGGYQIPKGWLVYYSIRDTHRDPEL 335
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKE-TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:cd11044  336 YPDPERFDPERFSPARSEDKKKPfSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLPN 399
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
164-309 1.47e-20

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 91.55  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVI-GANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENT-VLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:cd11062  259 ERLREELKTAMpDPDSPPSLAELEKLPYLTAVIKEGLRLSYGVPTRLPRVVPDEGlYYKGWVIPPGTPVSMSSYFVHHDE 338
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKK 309
Cdd:cd11062  339 EIFPDPHEFRPERWLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEE 406
PLN02971 PLN02971
tryptophan N-hydroxylase
165-309 1.72e-20

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 92.02  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN02971 363 KAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVW 442
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 245 EKPEDFYPNRFLDDQGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKK 309
Cdd:PLN02971 443 SDPLSFKPERHLNECSEVTLTENdlrFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETR 510
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
165-306 3.66e-20

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 91.04  E-value: 3.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN03112 332 KIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIW 411
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 245 EKPEDFYPNRFLDDQG---QLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:PLN03112 412 DDVEEFRPERHWPAEGsrvEISHGPDFkiLPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDG 478
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
189-299 4.22e-20

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: 89.95  E-value: 4.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 189 PYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflddqgqliKKETF 268
Cdd:COG2124  268 ELLPAAVEETLRLYPPVP-LLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAH 337
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530377130 269 IPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:COG2124  338 LPFGGGPHRCLGAALARLEARIALATLLRRF 368
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
167-292 4.24e-20

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 89.93  E-value: 4.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 167 HEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEK 246
Cdd:cd11043  251 HEEIAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVP-GVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPD 329
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530377130 247 PEDFYPNRFldDQGQLIKKETFIPFGIGKRVCMGEQLAKMELfLMF 292
Cdd:cd11043  330 PLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELAKLEI-LVF 372
PLN02936 PLN02936
epsilon-ring hydroxylase
165-314 4.26e-20

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 90.62  E-value: 4.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN02936 314 KAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVW 392
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530377130 245 EKPEDFYPNRFLDDQGQLIKKET---FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPLLTG 314
Cdd:PLN02936 393 ERAEEFVPERFDLDGPVPNETNTdfrYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQDIVMTTG 465
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
168-332 7.05e-20

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 89.66  E-value: 7.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 168 EEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQ-GYTIPKGTLILPNLWSVHRDPAIWEK 246
Cdd:cd11041  266 EEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSdGLTLPKGTRIAVPAHAIHRDPDIYPD 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 247 PEDFYPNRF--LDDQGQLIKK-------ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPlLTGRFG 317
Cdd:cd11041  346 PETFDGFRFyrLREQPGQEKKhqfvstsPDFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERP-KNIWFG 424
                        170
                 ....*....|....*.
gi 530377130 318 LTLAPHPFN-ITISRR 332
Cdd:cd11041  425 EFIMPDPNAkVLVRRR 440
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
164-322 9.25e-20

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 89.75  E-value: 9.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:PLN03234 323 KKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAA 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 W-EKPEDFYPNRFLDD-QGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL-----PEDSKKPLLTG 314
Cdd:PLN03234 403 WgDNPNEFIPERFMKEhKGVDFKGQDFelLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLpkgikPEDIKMDVMTG 482
                        170
                 ....*....|...
gi 530377130 315 -----RFGLTLAP 322
Cdd:PLN03234 483 lamhkKEHLVLAP 495
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
164-312 9.67e-20

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 89.29  E-value: 9.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAP----SLTDKAQMPYTEATIMEVQRLtvVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHR 239
Cdd:cd20635  245 KKVMEEISSVLGKAGKDkikiSEDDLKKMPYIKRCVLEAIRL--RSPGAITRKVVKPIKIKNYTIPAGDMLMLSPYWAHR 322
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 240 DPAIWEKPEDFYPNRFLD-DQGQLIKKETFIPFGIGKRVCMGEQLAKMELFlMFVSLM-QSFAFAL----PEDSKKPLL 312
Cdd:cd20635  323 NPKYFPDPELFKPERWKKaDLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQ-MFVAMFlYKYDFTLldpvPKPSPLHLV 400
PLN02966 PLN02966
cytochrome P450 83A1
184-308 2.95e-19

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 88.27  E-value: 2.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 184 DKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW-EKPEDFYPNRFLDDQGQL 262
Cdd:PLN02966 346 DVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDF 425
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530377130 263 IKKE-TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:PLN02966 426 KGTDyEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMK 472
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
164-322 5.49e-19

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 86.84  E-value: 5.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPL----AIphmtsENTVL---------QGYTIPKGTLI 230
Cdd:cd11063  251 AKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLnsrvAV-----RDTTLprgggpdgkSPIFVPKGTRV 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 231 LPNLWSVHRDPAIW-EKPEDFYPNRFLDDQGqliKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKK 309
Cdd:cd11063  326 LYSVYAMHRRKDIWgPDAEEFRPERWEDLKR---PGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVRP 402
                        170
                 ....*....|...
gi 530377130 310 PllTGRFGLTLAP 322
Cdd:cd11063  403 P--EERLTLTLSN 413
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
155-303 5.78e-19

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: 87.01  E-value: 5.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 155 LISIVTKEKEKVHEEIERVIGANRAPSltDK-AQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPN 233
Cdd:cd11052  258 LLAIHPEWQEKAREEVLEVCGKDKPPS--DSlSKLKTVSMVINESLRLYPPAVF-LTRKAKEDIKLGGLVIPKGTSIWIP 334
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 234 LWSVHRDPAIW-EKPEDFYPNRFLDDQGQLIK-KETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:cd11052  335 VLALHHDEEIWgEDANEFNPERFADGVAKAAKhPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTL 406
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
186-308 2.26e-18

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 85.33  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 186 AQMPYTEATIMEVQRLTVVVPLAIPHMT-SENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQLI- 263
Cdd:cd11058  274 AQLPYLNAVIQEALRLYPPVPAGLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFd 353
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530377130 264 --KKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:cd11058  354 ndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESE 400
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
163-299 2.31e-18

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 85.36  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:cd20647  271 QQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLP-GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEE 349
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 243 IWEKPEDFYPNRFLDdQGQLIKKETF--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20647  350 NFPRAEEFRPERWLR-KDALDRVDNFgsIPFGYGIRSCIGRRIAELEIHLALIQLLQNF 407
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
165-299 1.10e-17

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: 83.27  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIG-ANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGT--LILPnlWSVHRDP 241
Cdd:cd20680  279 KVHKELDEVFGkSDRPVTMEDLKKLRYLECVIKESLRLFPSVPL-FARSLCEDCEIRGFKVPKGVnaVIIP--YALHRDP 355
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 242 AIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20680  356 RYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF 413
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
164-288 1.12e-17

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: 83.09  E-value: 1.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd20678  274 QRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAV 353
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530377130 244 WEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMEL 288
Cdd:cd20678  354 WPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEM 398
PLN02738 PLN02738
carotene beta-ring hydroxylase
165-303 1.19e-17

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 83.81  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIpHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN02738 427 KLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLYPQPPVLI-RRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHW 504
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 245 EKPEDFYPNRF-LD--DQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:PLN02738 505 DDAEKFNPERWpLDgpNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQL 566
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
166-299 1.56e-17

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 82.88  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 166 VHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWE 245
Cdd:cd20648  271 LHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFP 350
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530377130 246 KPEDFYPNRFLdDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20648  351 DPNSFRPERWL-GKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHF 403
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
164-296 3.39e-17

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 81.64  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVI----GANRAPSLTDK-AQMPYTEATIMEVQRLTVVvPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVH 238
Cdd:cd11040  258 ERIREEIEPAVtpdsGTNAILDLTDLlTSCPLLDSTYLETLRLHSS-STSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLH 336
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 239 RDPAIWEK-PEDFYPNRFLDDQGQLI---KKETFIPFGIGKRVCMGEQLAKMELfLMFVSLM 296
Cdd:cd11040  337 MDPEIWGPdPEEFDPERFLKKDGDKKgrgLPGAFRPFGGGASLCPGRHFAKNEI-LAFVALL 397
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
164-299 2.44e-16

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 79.28  E-value: 2.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVigANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:cd11045  246 ERLREESLAL--GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEY 322
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 244 WEKPEDFYPNRFLDDQG-QLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd11045  323 WPNPERFDPERFSPERAeDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRF 379
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
167-308 4.07e-16

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 78.87  E-value: 4.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 167 HEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEK 246
Cdd:PLN02987 308 HEKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKD 386
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530377130 247 PEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:PLN02987 387 ARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAEQDK 448
PLN02302 PLN02302
ent-kaurenoic acid oxidase
164-290 1.48e-15

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 77.06  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIgANRAP-----SLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSeNTVLQGYTIPKGTLILPNLWSVH 238
Cdd:PLN02302 322 QKAKAEQEEIA-KKRPPgqkglTLKDVRKMEYLSQVIDETLRLINISLTVFREAKT-DVEVNGYTIPKGWKVLAWFRQVH 399
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530377130 239 RDPAIWEKPEDFYPNRFlddQGQLIKKETFIPFGIGKRVCMGEQLAKMELFL 290
Cdd:PLN02302 400 MDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISI 448
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
163-311 1.86e-15

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: 76.80  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLtvvVPLA--IPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20649  295 QKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRM---YPPAfrFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHD 371
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKPL 311
Cdd:cd20649  372 PEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPL 442
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
164-320 3.44e-15

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: 75.70  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVI-----GANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVH 238
Cdd:cd11064  265 EKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMG 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 239 RDPAIW-EKPEDFYPNRFLDDQGQLIKKET--FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAlPEDSKKPllTGR 315
Cdd:cd11064  345 RMESIWgEDALEFKPERWLDEDGGLRPESPykFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFK-VVPGHKV--EPK 421

                 ....*
gi 530377130 316 FGLTL 320
Cdd:cd11064  422 MSLTL 426
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
165-322 4.77e-15

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 75.52  E-value: 4.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQM----PYTEATIMEVQRLTVVVpLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20643  266 NVQEMLRAEVLAARQEAQGDMVKMlksvPLLKAAIKETLRLHPVA-VSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRD 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 241 PAIWEKPEDFYPNRFLDDQGQLIKKetfIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFalpEDSKKPLLTGRFGLTL 320
Cdd:cd20643  345 PTVFPKPEKYDPERWLSKDITHFRN---LGFGFGPRQCLGRRIAETEMQLFLIHMLENFKI---ETQRLVEVKTTFDLIL 418

                 ..
gi 530377130 321 AP 322
Cdd:cd20643  419 VP 420
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
147-318 5.39e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 75.36  E-value: 5.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 147 FSDRPRVplISIVTKEKEKVHEEIERviganrAPSLT--DKAQMPYTEATIMEVQRLTVVVPLAIPHMTsENTVLQGYTI 224
Cdd:PLN02196 291 LAENPSV--LEAVTEEQMAIRKDKEE------GESLTweDTKKMPLTSRVIQETLRVASILSFTFREAV-EDVEYEGYLI 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 225 PKGTLILPNLWSVHRDPAIWEKPEDFYPNRFlddqGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALP 304
Cdd:PLN02196 362 PKGWKVLPLFRNIHHSADIFSDPGKFDPSRF----EVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIV 437
                        170
                 ....*....|....
gi 530377130 305 EDSkKPLLTGRFGL 318
Cdd:PLN02196 438 GTS-NGIQYGPFAL 450
PLN00168 PLN00168
Cytochrome P450; Provisional
163-299 7.06e-15

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 75.37  E-value: 7.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGAN-RAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDP 241
Cdd:PLN00168 340 QSKLHDEIKAKTGDDqEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDE 419
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530377130 242 AIWEKPEDFYPNRFL---DDQGQLI---KKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:PLN00168 420 REWERPMEFVPERFLaggDGEGVDVtgsREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREF 483
PLN03018 PLN03018
homomethionine N-hydroxylase
165-306 7.58e-15

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 75.05  E-value: 7.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW 244
Cdd:PLN03018 350 KALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIW 429
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 245 EKPEDFYPNRFLddQGQLIKKET--------FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:PLN03018 430 KDPLVYEPERHL--QGDGITKEVtlvetemrFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQD 497
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
184-310 2.20e-14

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: 73.57  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 184 DKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVL-QGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQL 262
Cdd:cd20679  301 DLAQLPFLTMCIKESLRLHPPVT-AISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQG 379
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530377130 263 IKKETFIPFGIGKRVCMGEQLAKMElflMFVSLMQSFA-FALPEDSKKP 310
Cdd:cd20679  380 RSPLAFIPFSAGPRNCIGQTFAMAE---MKVVLALTLLrFRVLPDDKEP 425
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
163-303 4.79e-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: 72.48  E-value: 4.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLtvvVP--LAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRD 240
Cdd:cd20639  266 QERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRL---YPpaVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHD 342
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 241 PAIW-EKPEDFYPNRFLDDQGQLIKKE-TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:cd20639  343 AELWgNDAAEFNPARFADGVARAAKHPlAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
190-331 4.96e-14

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 72.18  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 190 YTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQLikkETFI 269
Cdd:cd11067  264 YAEAFVQEVRRFYPFFPF-VGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDP---FDFI 339
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 270 PFGIGKRV----CMGEQLAkmelflmfVSLMQSFAfalpedskkPLLTGRFGLTLAPHPFNITISR 331
Cdd:cd11067  340 PQGGGDHAtghrCPGEWIT--------IALMKEAL---------RLLARRDYYDVPPQDLSIDLNR 388
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
168-316 5.81e-14

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 72.09  E-value: 5.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 168 EEIERVIGANRAPSltDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKP 247
Cdd:cd20614  247 DEAAAAGDVPRTPA--ELRRFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDP 323
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 248 EDFYPNRFLDDQGQLIKKETfIPFGIGKRVCMGEQLAKMELFLMFVSLmqsfAFALPEDSKKPLLTGRF 316
Cdd:cd20614  324 DRFRPERWLGRDRAPNPVEL-LQFGGGPHFCLGYHVACVELVQFIVAL----ARELGAAGIRPLLVGVL 387
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
164-302 1.14e-13

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: 71.13  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAPSLTDKA-------QMPYTEATIMEVQRLtvvVPLA------IPHMTSenTVLQGYTIP-KGTL 229
Cdd:cd11051  220 AKVRAEHDEVFGPDPSAAAELLRegpellnQLPYTTAVIKETLRL---FPPAgtarrgPPGVGL--TDRDGKEYPtDGCI 294
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 230 ILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQL--IKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFA 302
Cdd:cd11051  295 VYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHElyPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
188-322 1.33e-13

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 71.03  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 188 MPYTEATIMEVQRLtVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQlikKET 267
Cdd:cd20644  291 LPLLKAALKETLRL-YPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGS---GRN 366
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530377130 268 F--IPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFalpEDSKKPLLTGRFGLTLAP 322
Cdd:cd20644  367 FkhLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLV---ETLSQEDIKTVYSFILRP 420
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
155-318 2.27e-13

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: 70.56  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 155 LISIVTKEKEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNL 234
Cdd:cd20641  261 LLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVIN-IARRASEDMKLGGLEIPKGTTIIIPI 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 235 WSVHRDPAIW-EKPEDFYPNRFLDDQGQLIKK-ETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL-PEDSKKPL 311
Cdd:cd20641  340 AKLHRDKEVWgSDADEFNPLRFANGVSRAATHpNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLsPEYVHAPA 419
                        170
                 ....*....|.
gi 530377130 312 ----LTGRFGL 318
Cdd:cd20641  420 dhltLQPQYGL 430
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
163-264 7.69e-13

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 68.83  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQ----GYTIPKGTLILPNLWSVH 238
Cdd:cd11071  260 HARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL-QYGRARKDFVIEshdaSYKIKKGELLVGYQPLAT 338
                         90       100
                 ....*....|....*....|....*.
gi 530377130 239 RDPAIWEKPEDFYPNRFLDDQGQLIK 264
Cdd:cd11071  339 RDPKVFDNPDEFVPDRFMGEEGKLLK 364
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
162-293 1.70e-12

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: 67.70  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 162 EKEKVHEEIERVIgANRAPSLTDK--AQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSV-H 238
Cdd:cd20615  248 VQEKLREEISAAR-EQSGYPMEDYilSTDTLLAYCVLESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALnI 326
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 239 RDPAIWEKPEDFYPNRFLD-DQGQLIKKetFIPFGIGKRVCMGEQLAK--MELFLMFV 293
Cdd:cd20615  327 NNPFWGPDGEAYRPERFLGiSPTDLRYN--FWRFGFGPRKCLGQHVADviLKALLAHL 382
PLN02500 PLN02500
cytochrome P450 90B1
184-308 2.05e-12

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 67.58  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 184 DKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDD----- 258
Cdd:PLN02500 339 DYKKMEFTQCVINETLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNnnrgg 417
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530377130 259 --QGQLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:PLN02500 418 ssGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEADQ 469
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
164-299 2.78e-12

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 67.00  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHmTSENTVLQGYTIPKGTLILPNLWSVHRDPaI 243
Cdd:cd20616  259 EAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRK-ALEDDVIDGYPVKKGTNIILNIGRMHRLE-F 335
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 244 WEKPEDFYPNRFLDDqgqlIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSF 299
Cdd:cd20616  336 FPKPNEFTLENFEKN----VPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRF 387
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
166-327 8.86e-12

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 65.48  E-value: 8.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 166 VHEEIERVIG-ANRAPSLTDK---------AQMPYTEATIMEVQRLTVVvPLAIpHMTSENTVL-----QGYTIPKGTLI 230
Cdd:cd20631  264 ATKEVKRTLEkTGQKVSDGGNpivltreqlDDMPVLGSIIKEALRLSSA-SLNI-RVAKEDFTLhldsgESYAIRKDDII 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 231 --LPNLwsVHRDPAIWEKPEDFYPNRFLDDQGQliKKETF-----------IPFGIGKRVCMGEQLAKMELfLMFVSLMQ 297
Cdd:cd20631  342 alYPQL--LHLDPEIYEDPLTFKYDRYLDENGK--EKTTFykngrklkyyyMPFGSGTSKCPGRFFAINEI-KQFLSLML 416
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530377130 298 S-FAFALPEDSKK--PLLTGRFGLTLAPHPFNI 327
Cdd:cd20631  417 CyFDMELLDGNAKcpPLDQSRAGLGILPPTHDV 449
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
164-303 1.23e-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: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGaNRAPSLTDKAQMPYTEATIMEVQRLTVVVPLAIPHmTSENTVLQGYTIPKGTLI-LPNLWsVHRDPA 242
Cdd:cd20642  269 ERAREEVLQVFG-NNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRA-IHKDTKLGDLTLPAGVQVsLPILL-VHRDPE 345
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530377130 243 IW-EKPEDFYPNRFLDDQGQLIKKE-TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:cd20642  346 LWgDDAKEFNPERFAEGISKATKGQvSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFEL 408
PLN02290 PLN02290
cytokinin trans-hydroxylase
163-306 1.38e-11

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 65.22  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGANrAPSLTDKAQMPYTEATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPA 242
Cdd:PLN02290 350 QDKVRAEVAEVCGGE-TPSVDHLSKLTLLNMVINESLRLYPPATL-LPRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEE 427
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 243 IWEK-PEDFYPNRFLDDQgqLIKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPED 306
Cdd:PLN02290 428 LWGKdANEFNPDRFAGRP--FAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDN 490
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
195-303 1.67e-11

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: 64.74  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 195 IMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW-EKPEDFYPNRFLDDQGQLIKK-ETFIPFG 272
Cdd:cd20640  295 IQETLRLYPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPpHSYMPFG 373
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530377130 273 IGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:cd20640  374 AGARTCLGQNFAMAELKVLVSLILSKFSFTL 404
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
207-288 2.40e-11

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 63.86  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 207 LAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLIkketfipFGIGKRVCMGEQLAKM 286
Cdd:cd20629  251 ASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--KPKPHLV-------FGGGAHRCLGEHLARV 321

                 ..
gi 530377130 287 EL 288
Cdd:cd20629  322 EL 323
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
187-298 3.02e-11

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 64.06  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 187 QMPYTEATIMEVQRLTVVVPLAIpHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQLIKKE 266
Cdd:cd20638  294 QLKYTGCVIKETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRF 372
                         90       100       110
                 ....*....|....*....|....*....|..
gi 530377130 267 TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQS 298
Cdd:cd20638  373 SFIPFGGGSRSCVGKEFAKVLLKIFTVELARH 404
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
183-307 1.06e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 62.45  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 183 TDKAQMPYTEATIMEVQRLTVVVpLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFlddQGQL 262
Cdd:PLN03141 309 TDYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRW---QEKD 384
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530377130 263 IKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDS 307
Cdd:PLN03141 385 MNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRWVAEEDT 429
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
177-306 2.16e-10

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 61.55  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 177 NRAPSLTDKAQM--PYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLIL-----PNLWSvhrdPAI------ 243
Cdd:cd20622  314 GRLPTAQEIAQAriPYLDAVIEEILRCANTAP-ILSREATVDTQVLGYSIPKGTNVFllnngPSYLS----PPIeidesr 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 --------------WEKP--EDFYPNRFLDDQGQLIKKE------TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAF 301
Cdd:cd20622  389 rssssaakgkkagvWDSKdiADFDPERWLVTDEETGETVfdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFEL 468

                 ....*.
gi 530377130 302 -ALPED 306
Cdd:cd20622  469 lPLPEA 474
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
181-298 9.61e-10

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 59.46  E-value: 9.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 181 SLTDKAQMPYTEATIMEVQRLtvVVPLAIPHMTSENTV-LQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRF--LD 257
Cdd:cd20636  285 SLEKLSRLRYLDCVVKEVLRL--LPPVSGGYRTALQTFeLDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgvER 362
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530377130 258 DQGQLiKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQS 298
Cdd:cd20636  363 EESKS-GRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTT 402
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
192-288 1.45e-09

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 58.64  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 192 EATIMEVQRLTVVVPLaIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDqgqLIKKETFIP- 270
Cdd:cd11080  238 PRAIAETLRYHPPVQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHR--ED---LGIRSAFSGa 311
                         90       100
                 ....*....|....*....|...
gi 530377130 271 -----FGIGKRVCMGEQLAKMEL 288
Cdd:cd11080  312 adhlaFGSGRHFCVGAALAKREI 334
PLN02774 PLN02774
brassinosteroid-6-oxidase
148-288 1.20e-08

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 55.94  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 148 SDRPRVplisivTKEKEKVHEEIERVIGANRAPSLTDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKG 227
Cdd:PLN02774 292 HDHPKA------LQELRKEHLAIRERKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVN-GVLRKTTQDMELNGYVIPKG 364
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530377130 228 TLILPNLWSVHRDPAIWEKPEDFYPNRFLDDqgQLIKKETFIPFGIGKRVCMGEQLAKMEL 288
Cdd:PLN02774 365 WRIYVYTREINYDPFLYPDPMTFNPWRWLDK--SLESHNYFFLFGGGTRLCPGKELGIVEI 423
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
164-303 3.73e-08

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 54.47  E-value: 3.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIE---------RVIGANRAPSLtdkAQMPYTEATIMEVQRLtvVVPLAIPHMTSENTV-LQGYTIPKGTLILPN 233
Cdd:cd20637  261 EKLREELRsngilhngcLCEGTLRLDTI---SSLKYLDCVIKEVLRL--FTPVSGGYRTALQTFeLDGFQIPKGWSVLYS 335
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530377130 234 LWSVHRDPAIWEKPEDFYPNRFLDDQGQliKKE---TFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFAL 303
Cdd:cd20637  336 IRDTHDTAPVFKDVDAFDPDRFGQERSE--DKDgrfHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFEL 406
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
165-319 5.08e-08

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 54.31  E-value: 5.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 165 KVHEEIERVIGANRAPSLTDK-AQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAI 243
Cdd:PLN02426 329 AIREEADRVMGPNQEAASFEEmKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERI 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 244 W-EKPEDFYPNRFLDDQgqlikkeTFIP--------FGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSKKpllTG 314
Cdd:PLN02426 409 WgPDCLEFKPERWLKNG-------VFVPenpfkypvFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGRSNR---AP 478

                 ....*..
gi 530377130 315 RF--GLT 319
Cdd:PLN02426 479 RFapGLT 485
PTZ00404 PTZ00404
cytochrome P450; Provisional
61-156 6.81e-08

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.57  E-value: 6.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  61 PGPTPWPLVGNFGHvllppflrrrswLSSRtraagidpsvigPQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREAL 140
Cdd:PTZ00404  32 KGPIPIPILGNLHQ------------LGNL------------PHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMF 87
                         90
                 ....*....|....*.
gi 530377130 141 VQQAEVFSDRPRVPLI 156
Cdd:PTZ00404  88 VDNFDNFSDRPKIPSI 103
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
103-161 1.37e-07

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 52.89  E-value: 1.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530377130 103 PQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRPRVPLISIVTK 161
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTN 59
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
163-258 1.91e-07

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 52.13  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 163 KEKVHEEIERVIGanRAPSLTDK-AQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQgYTIPKGTLILPNLWSVHRDP 241
Cdd:cd20627  236 QKKLYKEVDQVLG--KGPITLEKiEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQ-HIIPKETLVLYALGVVLQDN 312
                         90
                 ....*....|....*..
gi 530377130 242 AIWEKPEDFYPNRFLDD 258
Cdd:cd20627  313 TTWPLPYRFDPDRFDDE 329
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
167-300 3.03e-07

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 51.66  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 167 HEEIERVIGANraPSLTDKAqmpyteatIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEK 246
Cdd:cd20630  233 HPEALRKVKAE--PELLRNA--------LEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSD 302
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530377130 247 PEDFYPNRflddqgqliKKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFA 300
Cdd:cd20630  303 PDRFDVRR---------DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFP 347
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
192-307 6.44e-07

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 50.43  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 192 EATIMEVQRLTVvvPL-AIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQgqlikketfIP 270
Cdd:cd11079  228 PAAIDEILRLDD--PFvANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDRHAADN---------LV 296
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530377130 271 FGIGKRVCMGEQLAKMEL-FLMFVSLMQSFAFALPEDS 307
Cdd:cd11079  297 YGRGIHVCPGAPLARLELrILLEELLAQTEAITLAAGG 334
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
197-288 7.45e-07

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 50.22  E-value: 7.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 197 EVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLikketfiPFGIGKR 276
Cdd:cd11029  261 ELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--DANGHL-------AFGHGIH 331
                         90
                 ....*....|..
gi 530377130 277 VCMGEQLAKMEL 288
Cdd:cd11029  332 YCLGAPLARLEA 343
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
168-315 1.23e-06

unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 49.77  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 168 EEIERVIGANRAPSltDKAQMPYTEATIMEVQRLTVVVPlAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKP 247
Cdd:cd20624  223 EQAARAREEAAVPP--GPLARPYLRACVLDAVRLWPTTP-AVLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEALPFA 299
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 248 EDFYPNRFLDDQGQLikKETFIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALpeDSKKPLLTGR 315
Cdd:cd20624  300 DRFVPEIWLDGRAQP--DEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDP--LESPRSGPGE 363
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
209-292 1.37e-06

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. 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: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 49.45  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 209 IPHM---TSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDF----YPNRFLddqgqlikketfiPFGIGKRVCMGE 281
Cdd:cd11033  267 VIHFrrtATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFditrSPNPHL-------------AFGGGPHFCLGA 333
                         90
                 ....*....|.
gi 530377130 282 QLAKMELFLMF 292
Cdd:cd11033  334 HLARLELRVLF 344
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
114-160 1.59e-06

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 49.24  E-value: 1.59e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 530377130 114 YGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRPRVPLISIVT 160
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLS 47
PLN02648 PLN02648
allene oxide synthase
164-261 2.94e-06

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 48.78  E-value: 2.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRApSLTDKA--QMPYTEATIMEVQRLTVVVPLAIPHmTSENTVLQ----GYTIPKGTLILPNLWSV 237
Cdd:PLN02648 308 ARLAEEVRSAVKAGGG-GVTFAAleKMPLVKSVVYEALRIEPPVPFQYGR-AREDFVIEshdaAFEIKKGEMLFGYQPLV 385
                         90       100
                 ....*....|....*....|....
gi 530377130 238 HRDPAIWEKPEDFYPNRFLDDQGQ 261
Cdd:PLN02648 386 TRDPKVFDRPEEFVPDRFMGEEGE 409
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
209-316 3.55e-06

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. 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: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 48.33  E-value: 3.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 209 IPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLIkketfipFGIGKRVCMGEQLAKMEL 288
Cdd:cd11031  269 FPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR--EPNPHLA-------FGHGPHHCLGAPLARLEL 339
                         90       100       110
                 ....*....|....*....|....*....|....
gi 530377130 289 FLMFVSLMQSF---AFALPEDS---KKPLLTGRF 316
Cdd:cd11031  340 QVALGALLRRLpglRLAVPEEElrwREGLLTRGP 373
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
164-296 4.18e-06

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 48.06  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVI---GANRAPS----LT--DKAQMPYTEATIMEVQRLTVVVplAIPHMTSENTVLQ-----GYTIPKGTL 229
Cdd:cd20632  250 AAVRDEIDHVLqstGQELGPDfdihLTreQLDSLVYLESAINESLRLSSAS--MNIRVVQEDFTLKlesdgSVNLRKGDI 327
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530377130 230 ILPNLWSVHRDPAIWEKPEDFYPNRFLDDqGQliKKETF-----------IPFGIGKRVCMGEQLAKMELfLMFVSLM 296
Cdd:cd20632  328 VALYPQSLHMDPEIYEDPEVFKFDRFVED-GK--KKTTFykrgqklkyylMPFGSGSSKCPGRFFAVNEI-KQFLSLL 401
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
164-317 8.85e-06

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 46.98  E-value: 8.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANR-----APSLTDKA-----QMPYTEATIMEVQRLTVVvPLAIpHMTSENTVL-----QGYTIPKGT 228
Cdd:cd20633  259 KAVREEVEQVLKETGqevkpGGPLINLTrdmllKTPVLDSAVEETLRLTAA-PVLI-RAVVQDMTLkmangREYALRKGD 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 229 LIL--PNLwSVHRDPAIWEKPEDFYPNRFLDDQGQLiKKETF----------IPFGIGKRVCMGEQLAKMELfLMFVSLM 296
Cdd:cd20633  337 RLAlfPYL-AVQMDPEIHPEPHTFKYDRFLNPDGGK-KKDFYkngkklkyynMPWGAGVSICPGRFFAVNEM-KQFVFLM 413
                        170       180
                 ....*....|....*....|....
gi 530377130 297 QS-FAFAL--PEDSKKPLLTGRFG 317
Cdd:cd20633  414 LTyFDLELvnPDEEIPSIDPSRWG 437
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
211-288 1.01e-05

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 46.78  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 211 HMTS----ENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLikketfiPFGIGKRVCMGEQLAKM 286
Cdd:cd20625  260 QLTArvalEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR--APNRHL-------AFGAGIHFCLGAPLARL 330

                 ..
gi 530377130 287 EL 288
Cdd:cd20625  331 EA 332
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
48-152 1.03e-05

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 47.12  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  48 WSWLRRRRARGIPPGPTPWPLVGNfghvllppfLRRRSWLSSRTraagidpsvigpqvlLAHLARVYGSIFSFFIGHYLV 127
Cdd:PLN03112  22 WLNASMRKSLRLPPGPPRWPIVGN---------LLQLGPLPHRD---------------LASLCKKYGPLVYLRLGSVDA 77
                         90       100
                 ....*....|....*....|....*
gi 530377130 128 VVLSDFHSVREALVQQAEVFSDRPR 152
Cdd:PLN03112  78 ITTDDPELIREILLRQDDVFASRPR 102
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
184-308 1.36e-05

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 46.54  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 184 DKAQMPYTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW-EKPEDFYPNRFLDDQGQL 262
Cdd:PLN02169 350 DLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGL 429
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 530377130 263 IKKET--FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPEDSK 308
Cdd:PLN02169 430 RHEPSykFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIEGHK 477
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
195-285 1.53e-05

C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; This family contains Gaeumannomyces graminis linoleate diol synthase (LDS) and similar proteins including Ssp1 from the phytopathogenic basidiomycete Ustilago maydis. LDS, also called linoleate (8R)-dioxygenase, catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and the isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate. Ssp1 is expressed in mature teliospores, which are produced by U. maydis only after infection of its host plant, maize. Ssp1 is localized on lipid bodies in germinating teliospores, suggesting a role in the mobilization of storage lipids. LDS and Ssp1 contain an N-terminal dioxygenase domain related to animal heme peroxidases, and a C-terminal cytochrome P450 domain. The LDS-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 46.18  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 195 IMEVQRLTVVVPLAIPHMTSENTVLQG----YTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflddqgqliKKETFIP 270
Cdd:cd20612  244 VLEALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR---------PLESYIH 314
                         90
                 ....*....|....*
gi 530377130 271 FGIGKRVCMGEQLAK 285
Cdd:cd20612  315 FGHGPHQCLGEEIAR 329
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
213-288 1.54e-05

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 46.04  E-value: 1.54e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 213 TSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLikketfiPFGIGKRVCMGEQLAKMEL 288
Cdd:cd11037  267 TTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGHV-------GFGHGVHACVGQHLARLEG 333
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
114-161 1.74e-05

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: 46.29  E-value: 1.74e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530377130 114 YGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRPRVPLISIVTK 161
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTK 48
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
190-305 4.08e-05

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 45.16  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 190 YTEATIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIW-EKPEDFYPNRFLDDQG-QLIKKET 267
Cdd:PLN03195 373 YLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVfQNASPFK 452
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530377130 268 FIPFGIGKRVCMGEQLAKMELFLMFVSLMQSFAFALPE 305
Cdd:PLN03195 453 FTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVP 490
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
114-151 5.32e-05

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 44.62  E-value: 5.32e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530377130 114 YGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRP 151
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRP 38
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
213-288 6.93e-05

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 44.13  E-value: 6.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530377130 213 TSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLIKketfipFGIGKRVCMGEQLAKMEL 288
Cdd:cd11078  274 ATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNARKHLT------FGHGIHFCLGAALARMEA 341
PLN02966 PLN02966
cytochrome P450 83A1
59-151 8.49e-05

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 43.97  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  59 IPPGPTPWPLVGNFghvllppflrrrswlssrtraagIDPSVIGPQVLLAHLARVYGSIFSFFIGHYLVVVLSDFHSVRE 138
Cdd:PLN02966  30 LPPGPSPLPVIGNL-----------------------LQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKE 86
                         90
                 ....*....|...
gi 530377130 139 ALVQQAEVFSDRP 151
Cdd:PLN02966  87 LLKTQDVNFADRP 99
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
213-287 8.57e-05

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 43.74  E-value: 8.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530377130 213 TSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQGQLikketfiPFGIGKRVCMGEQLAKME 287
Cdd:cd11032  263 TTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR--NPNPHL-------SFGHGIHFCLGAPLARLE 328
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
180-288 1.30e-04

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-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: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 43.28  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 180 PSLTDKAqmpyteatIMEVQRLTVVVPLAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRflDDQ 259
Cdd:cd11030  249 PSLVPGA--------VEELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--PAR 318
                         90       100
                 ....*....|....*....|....*....
gi 530377130 260 GQLikketfiPFGIGKRVCMGEQLAKMEL 288
Cdd:cd11030  319 RHL-------AFGHGVHQCLGQNLARLEL 340
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
207-292 2.03e-04

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 42.71  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 207 LAIPHMTSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPE----DFYPNRFLddqgqlikketfiPFGIGKRVCMGEQ 282
Cdd:cd11034  249 AGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDridiDRTPNRHL-------------AFGSGVHRCLGSH 315
                         90
                 ....*....|
gi 530377130 283 LAKMELFLMF 292
Cdd:cd11034  316 LARVEARVAL 325
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
164-320 2.13e-04

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 42.82  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 164 EKVHEEIERVIGANRAP--SLTDKAQ-----MPYTEATIMEVQRLTvvvplAIPHMTSE---NTVL-----QGYTIPKG- 227
Cdd:cd20634  256 AAVRGEIQRIKHQRGQPvsQTLTINQelldnTPVFDSVLSETLRLT-----AAPFITREvlqDMKLrladgQEYNLRRGd 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 228 TLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQlIKKETF----------IPFGIGKRVCMGEQLA----KMELFLMFV 293
Cdd:cd20634  331 RLCLFPFLSPQMDPEIHQEPEVFKYDRFLNADGT-EKKDFYkngkrlkyynMPWGAGDNVCIGRHFAvnsiKQFVFLILT 409
                        170       180
                 ....*....|....*....|....*..
gi 530377130 294 SLmqSFAFALPEDSKKPLLTGRFGLTL 320
Cdd:cd20634  410 HF--DVELKDPEAEIPEFDPSRYGFGL 434
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
114-151 2.63e-04

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 42.30  E-value: 2.63e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530377130 114 YGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRP 151
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRP 38
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
51-160 3.07e-04

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 42.41  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  51 LRRRRARgIPPGPTPWPLVGNfghvllppflrrrsWLSsrtraAGIDPSvigpQVLLAHLARVYGSIFSFFIGHYLVVVL 130
Cdd:PLN02394  24 LRGKKLK-LPPGPAAVPIFGN--------------WLQ-----VGDDLN----HRNLAEMAKKYGDVFLLRMGQRNLVVV 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 530377130 131 SDFHSVREALVQQAEVFSDRPRVPLISIVT 160
Cdd:PLN02394  80 SSPELAKEVLHTQGVEFGSRTRNVVFDIFT 109
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
114-151 6.08e-04

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 41.23  E-value: 6.08e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530377130 114 YGSIFSFFIGHYLVVVLSDFHSVREALVQQAEVFSDRP 151
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRP 38
PLN00168 PLN00168
Cytochrome P450; Provisional
52-154 1.50e-03

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 40.32  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130  52 RRRRARGIPPGPTPWPLVGNFghvllppflrrrSWLssRTRAAGIDPsvigpqvLLAHLARVYGSIFSFFIGHYLVVVLS 131
Cdd:PLN00168  29 GGKKGRRLPPGPPAVPLLGSL------------VWL--TNSSADVEP-------LLRRLIARYGPVVSLRVGSRLSVFVA 87
                         90       100
                 ....*....|....*....|...
gi 530377130 132 DFHSVREALVQQAEVFSDRPRVP 154
Cdd:PLN00168  88 DRRLAHAALVERGAALADRPAVA 110
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
198-285 6.21e-03

cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial metabolism of the military explosive, hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX). XplA has an unusual structural organization comprising a heme domain that is fused to its flavodoxin redox partner. XplA, along with its partner reductase XplB, are plasmid encoded and the xplA gene has now been found in divergent genera across the globe with near sequence identity. It has only been detected at explosive-contaminated sites, suggesting rapid dissemination of this novel catabolic activity, possibly within a 50-year period since the introduction of RDX into the environment. XplA 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: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 38.18  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530377130 198 VQRLTVVVPLAIPHM--TSENTVLQGYTIPKGTLILPNLWSVHRDPAIWEKPEDFYPNRFLDDQGQLIkketfipFGIGK 275
Cdd:cd20619  238 INEMVRMDPPQLSFLrfPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPAASRNLS-------FGLGP 310
                         90
                 ....*....|
gi 530377130 276 RVCMGEQLAK 285
Cdd:cd20619  311 HSCAGQIISR 320
 
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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