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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 30515: Putative aromatic hydrocarbon hydrolase

There are 2 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
2,6-dioxo-6-phenylhexa-3-enoate hydrolase. [EC: 3.7.1.8]
2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate.
  • Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 by ring-fission at a -CO-C bond.
  • Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
 3 A0A0K6JZD7 A0A0K6KGG6 A0A0T8PUX1
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 A0A0T8PUX1