cytochrome P450 3A5 isoform 2 [Homo sapiens]
Protein Classification
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 ... |
67-106 | 5.28e-23 | ||
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 cd20650: Pssm-ID: 477761 [Multi-domain] Cd Length: 426 Bit Score: 92.86 E-value: 5.28e-23
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| Name | Accession | Description | Interval | E-value | ||
| CYP3A | cd20650 | cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ... |
67-106 | 5.28e-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: 92.86 E-value: 5.28e-23
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| p450 | pfam00067 | Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ... |
39-100 | 1.85e-12 | ||
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: 63.07 E-value: 1.85e-12
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| PTZ00404 | PTZ00404 | cytochrome P450; Provisional |
33-105 | 3.27e-07 | ||
cytochrome P450; Provisional Pssm-ID: 173595 [Multi-domain] Cd Length: 482 Bit Score: 47.80 E-value: 3.27e-07
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| Name | Accession | Description | Interval | E-value | ||
| CYP3A | cd20650 | cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ... |
67-106 | 5.28e-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: 92.86 E-value: 5.28e-23
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| p450 | pfam00067 | Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ... |
39-100 | 1.85e-12 | ||
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: 63.07 E-value: 1.85e-12
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| CYP3A-like | cd11055 | cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ... |
67-107 | 2.62e-12 | ||
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: 62.60 E-value: 2.62e-12
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| PTZ00404 | PTZ00404 | cytochrome P450; Provisional |
33-105 | 3.27e-07 | ||
cytochrome P450; Provisional Pssm-ID: 173595 [Multi-domain] Cd Length: 482 Bit Score: 47.80 E-value: 3.27e-07
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| CYP5A1 | cd20649 | cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ... |
67-105 | 7.58e-06 | ||
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: 44.06 E-value: 7.58e-06
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| PLN03112 | PLN03112 | cytochrome P450 family protein; Provisional |
39-105 | 8.57e-05 | ||
cytochrome P450 family protein; Provisional Pssm-ID: 215583 [Multi-domain] Cd Length: 514 Bit Score: 40.96 E-value: 8.57e-05
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| PLN02183 | PLN02183 | ferulate 5-hydroxylase |
39-105 | 1.23e-04 | ||
ferulate 5-hydroxylase Pssm-ID: 165828 [Multi-domain] Cd Length: 516 Bit Score: 40.60 E-value: 1.23e-04
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| CYP6-like | cd11056 | cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ... |
73-107 | 2.38e-04 | ||
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: 39.44 E-value: 2.38e-04
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