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CATH Superfamily 3.40.50.1820

Alpha/Beta hydrolase fold, catalytic domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.

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 114777: Abhydrolase domain-containing protein 4

There are 4 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
1-acylglycerol-3-phosphate O-acyltransferase. [EC: 2.3.1.51]
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
  • Acyl-[acyl-carrier-protein] can also act as acyl donor.
  • The animal enzyme is specific for the transfer of unsaturated fatty acyl groups.
 8 A0A061I5L9 A0A061I6E7 A0A0S2Z5D6 Q5EE05 Q5RBI4 Q6QA69 Q8WTS1 Q9DBL9
Carboxylesterase. [EC: 3.1.1.1]
A carboxylic ester + H(2)O = an alcohol + a carboxylate.
  • Wide specificity; also hydrolyzes vitamin A esters.
  • The enzymes from microsomes also catalyze the reactions of EC 3.1.1.2, EC 3.1.1.5, EC 3.1.1.6, EC 3.1.1.23, EC 3.1.1.28, EC 3.1.2.2, EC 3.5.1.4, and EC 3.5.1.13.
  • Formerly EC 3.1.1.12.
 3 A0A0J9R7I3 Q5U191 Q7JQU9
Soluble epoxide hydrolase. [EC: 3.3.2.10]
An epoxide + H(2)O = a glycol.
  • Catalyzes the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism.
  • It is involved in the metabolism of arachidonic epoxides (epoxyeicosatrienoic acids; EETs) and linoleic acid epoxides.
  • The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76.
  • Like EC 3.3.2.9, it is probable that the reaction involves the formation of an hydroxyalkyl-enzyme intermediate.
  • The enzyme can also use leukotriene A(4), the substrate of EC 3.3.2.6, but it forms 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than leukotriene B(4) as the product.
  • Formerly EC 3.3.2.3, EC 4.2.1.63 and EC 4.2.1.64.
 3 A0A0J9R7I3 Q5U191 Q7JQU9
Prolyl aminopeptidase. [EC: 3.4.11.5]
Release of N-terminal proline from a peptide.
  • Present in the cytosol of mammalian and microbial cells.
  • In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide.
  • The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1.
  • Belongs to peptidase family S33.
  • Formerly EC 3.4.1.4.
 1 B7PSU1