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Conserved domains on  [gi|725824127|gb|AIY33890|]
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cytochrome P450 family 11 subfamily a, partial [Rattus norvegicus]

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 ...
 80-198 7.98e-67

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 cd20643:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 425  Bit Score: 210.73  E-value: 7.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  80 FQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAP 159
Cdd:cd20643    1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 725824127 160 DSIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISD 198
Cdd:cd20643   81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSN 119
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 80-198 7.98e-67

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: 210.73  E-value: 7.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  80 FQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAP 159
Cdd:cd20643    1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 725824127 160 DSIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISD 198
Cdd:cd20643   81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSN 119
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 50-187 9.67e-28

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: 108.14  E-value: 9.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127   50 PSPGDNGWINLYHFLREnGTHRIHYHHMQNFQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQ 129
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLG-RKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 725824127  130 YYQRPIGVLFKSSDAWRKDRIVLNQEVMAPdSIKNFVPLLEGVAQDFIKVLHRRIKQQ 187
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGEP 136
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 80-198 7.98e-67

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: 210.73  E-value: 7.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  80 FQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAP 159
Cdd:cd20643    1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 725824127 160 DSIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISD 198
Cdd:cd20643   81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSN 119
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 80-197 5.96e-34

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: 124.95  E-value: 5.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  80 FQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAP 159
Cdd:cd20644    1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 725824127 160 DSIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDIS 197
Cdd:cd20644   81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQ 118
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 80-190 1.25e-31

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: 118.40  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  80 FQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAP 159
Cdd:cd11054    1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 725824127 160 DSIKNFVPLLEGVAQDFIKVLHRRIKQQNSG 190
Cdd:cd11054   81 KSVASYLPAINEVADDFVERIRRLRDEDGEE 111
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 50-187 9.67e-28

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: 108.14  E-value: 9.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127   50 PSPGDNGWINLYHFLREnGTHRIHYHHMQNFQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQ 129
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLG-RKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 725824127  130 YYQRPIGVLFKSSDAWRKDRIVLNQEVMAPdSIKNFVPLLEGVAQDFIKVLHRRIKQQ 187
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGEP 136
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 81-198 9.78e-15

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: 71.32  E-value: 9.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  81 QKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPD 160
Cdd:cd20648    3 AKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKPK 82

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 725824127 161 SIKNFVPLLEGVAQDFIKVLhRRIKQQNSGKFSGDISD 198
Cdd:cd20648   83 AVEAYAGVLNAVVTDLIRRL-RRQRSRSSPGVVKDIAG 119
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 81-178 2.01e-13

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: 67.52  E-value: 2.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  81 QKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPD 160
Cdd:cd20645    2 KKFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKPK 81

                         90
                 ....*....|....*...
gi 725824127 161 SIKNFVPLLEGVAQDFIK 178
Cdd:cd20645   82 EVMKLDGKINEVLADFMG 99
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 81-198 3.77e-11

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: 61.21  E-value: 3.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  81 QKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPD 160
Cdd:cd20646    2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKPK 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 725824127 161 SIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISD 198
Cdd:cd20646   82 EVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLAN 119
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 81-198 2.15e-09

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: 56.08  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  81 QKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNPERYLVPPWVAYHQYYQRPIGVLFKSSDAWRKDRIVLNQEVMAPD 160
Cdd:cd20647    2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPR 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 725824127 161 SIKNFVPLLEGVAQDFIKVLHRRIKQQNSGKFSGDISD 198
Cdd:cd20647   82 DVAVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVND 119
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 73-196 6.79e-04

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: 39.70  E-value: 6.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 725824127  73 HYHHMQnfQKYGPIYREKLGNMESVYILDPKDAATLFSCEGPNperyLVPPwvAYHQYYQRPI---GVLFKSSDAWRKDR 149
Cdd:cd20640    3 YFDKWR--KQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLD----LGKP--SYLKKTLKPLfggGILTSNGPHWAHQR 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 725824127 150 IVLNQEVMaPDSIKNFVPLLEGVAQDFIKVLHRRIKQqnSGKFSGDI 196
Cdd:cd20640   75 KIIAPEFF-LDKVKGMVDLMVDSAQPLLSSWEERIDR--AGGMAADI 118
 
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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