Phosphonoacetaldehyde hydrolase (IPR006323)

Short name: Phosphonoacetald_hydro

Overlapping homologous superfamilies

Family relationships


Phosphonoacetaldehyde hydrolase or phosphonatase catalyses the cleavage of the carbon-phosphorous bond of a phosphonate.

This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases, and contains a modified version of the conserved catalytic motifs of that superfamily [PMID: 7966317]. The first motif is usually DxDx(T/V); here it is DxAxT. In the third motif the normally conserved lysine is instead an arginine. Additionally, the enzyme from Bacillus cereus contains a unique conserved catalytic lysine which is involved in the binding and activation of the substrate through the formation of a Schiff base [PMID: 10956028].

The substrate of this enzyme is the product of 2-aminoethylphosphonate (AEP) transaminase, phosphonoacetaldehyde. This degradation pathway for AEP may be related to its toxic properties which are utilised by microorganisms as a chemical warfare agent.

GO terms

Biological Process

GO:0019700 organic phosphonate catabolic process

Molecular Function

GO:0050194 phosphonoacetaldehyde hydrolase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.