{PDOC01031}
{PS01328; 4HBCOA_THIOESTERASE}
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* 4-hydroxybenzoyl-CoA thioesterase family active site *
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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 [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.

-Consensus pattern: [QR]-[IV]-x(4)-[TC]-D-x(2)-G-[IV]-V-x-[HF]-x(2)-[FY]
                    [D is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: July 1999 / First entry.

[ 1] Benning M.M., Wesenberg G., Liu R., Taylor K.L., Dunaway-Mariano D.,
     Holden H.M.
     "The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase
     from Pseudomonas sp. Strain CBS-3."
     J. Biol. Chem. 273:33572-33579(1998).
     PubMed=9837940;

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