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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 2: Cytochrome P450 1A1

There are 5 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
17-alpha-hydroxyprogesterone deacetylase. [EC: 1.14.14.32]
(1) 17-alpha-hydroxyprogesterone + [reduced NADPH--hemoprotein reductase] + O(2) = androstenedione + acetate + [oxidized NADPH--hemoprotein reductase] + H(2)O. (2) 17-alpha-hydroxypregnenolone + [reduced NADPH--hemoprotein reductase] + O(2) = 3-beta-hydroxyandrost-5-en-17-one + acetate + [oxidized NADPH- -hemoprotein reductase] + H(2)O.
  • A microsomal protein that catalyzes two independent reactions at the same active site - the 17-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis (EC 1.14.14.19), and the conversion of the 17-hydroxylated products via a 17,20-lyase reaction to form androstenedione and 3-beta- hydroxyandrost-5-en-17-one, leading to sex hormone biosynthesis.
  • The activity of this reaction is dependent on the allosteric interaction of the enzyme with cytochrome b5 without any transfer of electrons from the cytochrome.
  • The enzymes from different organisms differ in their substrate specificity; while the enzymes from pig, hamster, and rat accept both 17-alpha-hydroxyprogesterone and 17-alpha-hydroxypregnenolone, the enzymes from human, bovine, sheep, goat, and bison do not accept the former, and the enzyme from guinea pig does not accept the latter.
  • Formerly EC 4.1.2.30.
 62 A0A1U7Q8W9 A0A1U7Q8W9 A0A2J8PCW1 A0A2J8PCW1 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A480MAR4
(52 more...)
Steroid 17-alpha-monooxygenase. [EC: 1.14.14.19]
A C(21)-steroid + [reduced NADPH--hemoprotein reductase] + O(2) = a 17-alpha-hydroxy-C(21)-steroid + [oxidized NADPH--hemoprotein reductase] + H(2)O.
  • Requires NADPH and EC 1.6.2.4.
  • Catalyzes two independent reactions at the same active site - the 17-alpha-hydroxylation of pregnenolone and progesterone, which is part of glucocorticoid hormones biosynthesis, and the conversion of the 17-alpha-hydroxylated products via a 17,20-lyase reaction to form androstenedione and dehydroepiandrosterone, leading to sex hormone biosynthesis (EC 1.14.14.32).
  • The ratio of the 17-alpha-hydroxylase and 17,20-lyase activities is an important factor in determining the directions of steroid hormone biosynthesis toward biosynthesis of glucocorticoid or sex hormones.
  • Formerly EC 1.14.1.7, EC 1.14.99.9 and EC 1.99.1.9.
 62 A0A1U7Q8W9 A0A1U7Q8W9 A0A2J8PCW1 A0A2J8PCW1 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A2K6DJ66 A0A480MAR4
(52 more...)
Unspecific monooxygenase. [EC: 1.14.14.1]
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O.
  • Acts on a wide range of substrates including many xenobiotics, steroids, fatty acids, vitamins and prostaglandins; reactions catalyzed include hydroxylation, epoxidation, N-oxidation, sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, and reduction of azo, nitro and N-oxide groups.
  • Together with EC 1.6.2.4, it forms a system in which two reducing equivalents are supplied by NADPH.
  • Some of the reactions attributed to EC 1.14.15.3 belong here.
  • Formerly EC 1.14.1.1, EC 1.14.14.2, EC 1.14.99.8 and EC 1.99.1.1.
 30 A0A1U7Q236 A0A1U7Q236 A0A384BDJ0 A0A384BDJ0 B6VGH4 B6VGH4 O77809 O77810 P00186 P00186
(20 more...)
Hydroperoxy icosatetraenoate dehydratase. [EC: 4.2.1.152]
A hydroperoxy icosatetraenoate = an oxoicosatetraenoate + H(2)O.
  • The mammalian enzymes accept a range of hydroperoxy icosatetraenoates (HPETE).
  • The human enzyme has highest activity with (12R)-HPETE, followed by (12S)-HPETE and (15R)-HPETE with much lower efficiency.
  • The murine enzyme has highest activity with (8R)-HPETE followed by (8S)-HPETE. All HPETE isoforms are converted to the corresponding oxoicosatetraenoate forms (KETE).
  • The enzymes also catalyze the reaction of EC 5.4.4.7.
 21 A0N0X8 A0N0X8 G7P943 G7P943 P00184 P00184 P00185 P04798 P04798 P05176
(11 more...)
Methyl farnesoate epoxidase. [EC: 1.14.14.127]
Methyl (2E,6E)-farnesoate + [reduced NADPH--hemoprotein reductase] + O(2) = juvenile hormone III + [oxidized NADPH--hemoprotein reductase] + H(2)O.
  • A cytochrome P450 (heme-thiolate) protein.
  • The enzyme, found in insects except for Lepidoptera (moths and butterflies) is specific for methyl farnesoate (cf. EC 1.14.14.128).
  • Formerly EC 1.14.13.202.
 1 Q6R7M4