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CATH Superfamily 1.10.630.10

Cytochrome P450

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Cytochrome P450
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 18: Cytochrome P450 monooxygenase

There are 9 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Cholest-4-en-3-one 26-monooxygenase ((25R)-3-oxocholest-4-en-26-oate forming). [EC: 1.14.15.28]
Cholest-4-en-3-one + 6 reduced [2Fe-2S] ferredoxin + 3 O(2) = (25R)-3- oxocholest-4-en-26-oate + 6 oxidized [2Fe-2S] ferredoxin + 4 H(2)O.
  • This cytochrome P450 (heme-thiolate) enzyme, found in several bacterial pathogens, is involved in degradation of the host cholesterol.
  • It catalyzes the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol.
  • The products are exclusively in the (25R) conformation.
  • The enzyme also accepts cholesterol as a substrate.
  • cf. 1.14.15.29.
  • The enzyme can receive electrons from ferredoxin reductase in vitro, its natural electron donor is not known yet.
  • Formerly EC 1.14.13.221.
 26 A0A045KDZ0 A0A045KDZ0 A0A045KDZ0 A0A045KDZ0 A0A045KDZ0 A5U8J2 A5U8J2 A5U8J2 A5U8J2 A5U8J2
(16 more...)
Biflaviolin synthase. [EC: 1.14.19.69]
(1) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,3'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O. (2) 2 flaviolin + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 3,8'-biflaviolin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O.
  • This cytochrome-P450 (heme-thiolate) enzyme, from the soil-dwelling bacterium Streptomyces coelicolor A3(2), catalyzes a phenol oxidation C-C coupling reaction, which results in the polymerization of flaviolin to form biflaviolin or triflaviolin without the incorporation of oxygen into the product.
  • The products are highly conjugated pigments that protect the bacterium from the deleterious effects of UV irradiation.
  • Formerly EC 1.14.21.7.
 10 A0A2P7ZZN8 A0A2P7ZZN8 A0A2P7ZZN8 D6ESE9 D6ESE9 D6ESE9 Q9FCA6 Q9FCA6 Q9FCA6 Q9KZF5
Pimeloyl-[acyl-carrier protein] synthase. [EC: 1.14.14.46]
A long-chain acyl-[acyl-carrier protein] + 2 reduced flavodoxin + 3 O(2) = pimeloyl-[acyl-carrier protein] + an n-alkanal + 2 oxidized flavodoxin + 3 H(2)O.
  • Catalyzes an oxidative C-C bond cleavage of long-chain acyl-[acyl- carrier protein]s of various lengths to generate pimeloyl-[acyl- carrier protein], an intermediate in the biosynthesis of biotin.
  • The preferred substrate of the enzyme from the bacterium Bacillus subtilis is palmitoyl-[acyl-carrier protein] which then gives heptanal as the alkanal.
  • The mechanism is similar to EC 1.14.15.6, followed by a hydroxylation step, which may occur spontaneously.
  • Formerly EC 1.14.15.12.
 4 L8AQN1 L8AQN1 P53554 P53554
6-deoxyerythronolide B hydroxylase. [EC: 1.14.15.35]
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
  • A cytochrome P450 (heme-thiolate) protein isolated from the bacterium Saccharopolyspora erythraea.
  • The enzyme is involved in the biosynthesis of the antibiotic erythromycin.
  • Formerly EC 1.14.13.188.
 4 A0A2A9J0V3 A0A2A9J0V3 Q00441 Q00441
Pentalenolactone synthase. [EC: 1.14.19.8]
Pentalenolactone F + O(2) + 2 reduced ferredoxin + 2 H(+) = pentalenolactone + 2 oxidized ferredoxin + 2 H(2)O.
  • Isolated from the bacteria Streptomyces exfoliatus and Streptomyces arenae.
  • Formerly EC 1.3.7.10.
 2 E3VWI3 E3VWJ9
2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase. [EC: 1.14.15.31]
2-hydroxy-5-methyl-1-naphthoate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 2,7-dihydroxy-5-methyl-1-naphthoate + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
  • A cytochrome P450 (heme-thiolate) protein involved in the synthesis of neocarzinostatin in the bacterium Streptomyces carzinostaticus.
  • Formerly EC 1.14.99.49.
 1 Q84HB6
20-oxo-5-O-mycaminosyltylactone 23-monooxygenase. [EC: 1.14.15.34]
20-oxo-5-O-beta-mycaminosyltylactone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = 5-O-beta-mycaminosyltylonolide + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
  • A cytochrome P450 (heme-thiolate) protein involved in the biosynthetic pathway of the macrolide antibiotic tylosin, which is produced by several species of Streptomyces bacteria.
  • Formerly EC 1.14.13.186.
 1 Q9ZHQ1
Vitamin D 1,25-hydroxylase. [EC: 1.14.15.22]
(1) Calciol + O(2) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) = calcidiol + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O. (2) Calcidiol + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = calcitriol + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O.
  • An enzyme found in the bacterium Streptomyces griseolus.
  • Cf. EC 1.14.14.24 and EC 1.14.15.18.
 1 P18326
Pentalenic acid synthase. [EC: 1.14.15.11]
1-deoxypentalenate + reduced ferredoxin + O(2) = pentalenate + oxidized ferredoxin + H(2)O.
  • Isolated from the bacterium Streptomyces avermitilis.
  • The product, pentalenate, is a co-metabolite from pentalenolactone biosynthesis.
 1 Q825I8