{PDOC01026}
{PS01322; PHOSPHOTRIESTERASE_1}
{PS51347; PHOSPHOTRIESTERASE_2}
{BEGIN}
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* Phosphotriesterase family signature and profile *
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Bacteria  such  as Pseudomonas diminuta harbor a plasmid that carries the gene
for  the enzyme phosphotriesterase (EC 3.1.8.1) (PTE) (also known as parathion
hydrolase). This enzyme has attracted interest because of its potential use in
the  detoxification  of  chemical  waste and warfare agents and its ability to
degrade  agricultural  pesticides  such  as  parathion. It act specifically on
synthetic organophosphate triesters and phosphorofluoridates. It does not seem
to  have  a natural occuring substrate and may thus have optimally evolved for
utilizing paraoxon.

PTE belongs  to  a family [1,2] of enzymes that possess a binuclear zinc metal
center at  their  active site. This family so far includes, in addition to the
parathion hydrolase, the following proteins:

 - Escherichia coli protein php. The substrate of php is not yet known.
 - Mycobacterium tuberculosis phosphotriesterase homology protein Rv0230C.
 - Mammalian phosphotriesterase related protein (PTER) (RPR-1).

The  two  zinc  ions  are coordinated by six different residues, four of which
being  histidines.  We  have  developed a signature pattern for this family of
enzymes, which corresponds to a region located in the N-terminal section. That
contains  two  histidines  that  bind  the first of the two zinc ions. We also
developed  a  profile  that  covers the entire phosphotriesterase and has been
manually adapted to detect each of the six zinc-binding residues.

-Consensus pattern: G-x-T-L-x-H-E-H-[LIV]
                    [The 2 H's are zinc ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2007 / Pattern removed, profile added and text revised.

[ 1] Scanlan T.S., Reid R.C.
     "Evolution in action."
     Chem. Biol. 2:71-75(1995).
     PubMed=9383406
[ 2] Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W.,
     Scanlan T.S., Fletterick R.J.
     "Biochemical characterization and crystallographic structure of an
     Escherichia coli protein from the phosphotriesterase gene family."
     Biochemistry 37:5096-5106(1998).
     PubMed=9548740; DOI=10.1021/bi971707+

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