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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.

December 2007 / Pattern removed, profile added and text revised.

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

PHOSPHOTRIESTERASE_2, PS51347; Phosphotriesterase family profile  (MATRIX)

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

• Domain architecture view of Swiss-Prot proteins matching PS51347 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51347 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51347 • Scan Swiss-Prot/TrEMBL entries against PS51347 • view ligand binding statistics

Matching PDB structures: 1BF6 1DPM 1EYW 1EZ2 ... [ALL]

PHOSPHOTRIESTERASE_1, PS01322; Phosphotriesterase family signature 1  (PATTERN)

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01322 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01322 • Scan Swiss-Prot/TrEMBL entries against PS01322 • view ligand binding statistics

Matching PDB structures: 1BF6 1DPM 1EYW 1EZ2 ... [ALL]

1	Authors	Scanlan T.S., Reid R.C.
	Title	Evolution in action.
	Source	Chem. Biol. 2:71-75(1995).
	PubMed ID	9383406

2	Authors	Buchbinder J.L., Stephenson R.C., Dresser M.J., Pitera J.W., Scanlan T.S., Fletterick R.J.
	Title	Biochemical characterization and crystallographic structure of an Escherichia coli protein from the phosphotriesterase gene family.
	Source	Biochemistry 37:5096-5106(1998).
	PubMed ID	9548740
	DOI	10.1021/bi971707+

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