Enzyme

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     3. Hydrolases
        3.11 Acting on carbon-phosphorus bonds
            3.11.1 Acting on carbon-phosphorus bonds (only sub-subclass identified to date)
ID:3.11.1.2
Description:Phosphonoacetate hydrolase.
Cath: 3.30.1360.110; 3.40.720.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.11.1.2
BRENDA Enzyme Link: BRENDA 3.11.1.2
KEGG Enzyme Link: KEGG3.11.1.2
BioCyc Enzyme Link: BioCyc 3.11.1.2
ExPASy Enzyme Link: ExPASy3.11.1.2
EC2PDB Enzyme Link: EC2PDB 3.11.1.2
ExplorEnz Enzyme Link: ExplorEnz 3.11.1.2
PRIAM enzyme-specific profiles Link: PRIAM 3.11.1.2
IntEnz Enzyme Link: IntEnz 3.11.1.2
MEDLINE Enzyme Link: MEDLINE 3.11.1.2
MSA:

3.11.1.2;

Phylogenetic Tree:

3.11.1.2;

Uniprot:
M-CSA:
RHEA:16749 H2O + phosphonoacetate = acetate + H(+) + phosphate
RULE(radius=1) [*:1]-[CH2;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[CH3;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning of the phosphonoacetate hydrolase gene from Pseudomonas fluorescens 23F encoding a new type of carbon-phosphorus bond cleaving enzyme and its expression in Escherichia coli and Pseudomonas putida.Kulakova AN, Kulakov LA, Quinn JP1997 Aug 119300819
The purification and properties of phosphonoacetate hydrolase, a novel carbon-phosphorus bond-cleavage enzyme from Pseudomonas fluorescens 23F.McGrath JW, Wisdom GB, McMullan G, Larkin MJ, Quinn JP1995 Nov 158529644
In vitro characterization of a phosphate starvation-independent carbon-phosphorus bond cleavage activity in Pseudomonas fluorescens 23F.McMullan G, Quinn JP1994 Jan8288524
Phosphonoacetate hydrolase from Penicillium oxalicum: purification and properties, phosphate starvation-independent expression, and partial sequencing.Klimek-Ochab M, Raucci G, Lejczak B, Forlani G2006 Mar16129582
A metal-independent hydrolase from a Penicillium oxalicum strain able to use phosphonoacetic acid as the only phosphorus source.Klimek-Ochab M, Lejczak B, Forlani G2003 May 2812770709