PROSITE documentation PDOC01031
4-hydroxybenzoyl-CoA thioesterase family active site


4-hydroxybenzoyl-CoA thioesterase (EC is an enzyme from Pseudomonas CBS-3, a soil-dwelling microbe that survives on 4-chlorobenzoate as its sole carbon source. This enzyme [1] 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 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 uncharacterized proteins:

  • Escherichia coli hypothetical protein ybgC.
  • Aquifex aeolicus hypothetical protein AQ_1494.
  • Haemophilus influenzae hypothetical protein HI0386.
  • Helicobacter pylori hypothetical protein HP0496.
  • Synechocystis strain PCC 6803 hypothetical protein slr0204.
  • Synechocystis strain PCC 6803 hypothetical protein sll0410.

We developed a signature pattern based on the region surrounding the potential active site residue.

Last update:

July 1999 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

4HBCOA_THIOESTERASE, PS01328; 4-hydroxybenzoyl-CoA thioesterase family active site  (PATTERN)


1AuthorsBenning M.M. Wesenberg G. Liu R. Taylor K.L. Dunaway-Mariano D. Holden H.M.
TitleThe three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3.
SourceJ. Biol. Chem. 273:33572-33579(1998).
PubMed ID9837940

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