UniProt functional annotation for P0A434



	UniProt functional annotation for P0A434

UniProt codes: P0A434, P16648.

Organism: Brevundimonas diminuta (Pseudomonas diminuta).

Taxonomy: Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Brevundimonas.

Function: Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.

Catalytic activity: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1;

Cofactor: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;

Subunit: Homodimer.

Subcellular location: Cell membrane; Peripheral membrane protein.

Ptm: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Biotechnology: 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.

Similarity: Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.

Sequence caution: Sequence=AAA98299.1; Type=Frameshift; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Brevundimonas diminuta (Pseudomonas diminuta).
Taxonomy:		Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales; Caulobacteraceae; Brevundimonas.



Function:		Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.


Catalytic activity:		Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1;
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
Subunit:		Homodimer.
Subcellular location:		Cell membrane; Peripheral membrane protein.
Ptm:		Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Biotechnology:		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.
Similarity:		Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family. {ECO:0000255\|PROSITE-ProRule:PRU00679}.
Sequence caution:		Sequence=AAA98299.1; Type=Frameshift; Evidence={ECO:0000305};