Active Site

4-hydroxybenzoyl-CoA thioesterase, active site (IPR008272)

Short name: HB-CoA_thioesterase_AS

Description

4-hydroxybenzoyl-CoA thioesterase (EC:3.1.2.23) is an enzyme from Pseudomonas CBS-3, a soil-dwelling microbe that survives on 4-chlorobenzoate as its sole carbon source. This enzyme [PMID: 9837940] catalyzes the last of the three steps in the pathway from 4-chlorobenzoate to hydroxybenzoate, the cleavage of the thioester bond of 4-hydroxybenzoyl-CoA to form hydroxybenzoate. 4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA 4-hydroxybenzoyl-CoA thioesterase is a protein of 141 amino-acid residues that assemble as an homotetramer. An aspartate in the N-terminal domain is thought to participate in the catalytic mechanism. This enzyme is evolutionary related to a number of uncharacterised proteins.

This signature spans the sequence which contains the active site aspartate residue.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016787 hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns