| Accession | TIGR01422 |
| Name | phosphonatase |
| Function | phosphonoacetaldehyde hydrolase |
| Gene Symbol | phnX |
| Trusted Cutoff | 221.20 |
| Domain Trusted Cutoff | 221.20 |
| Noise Cutoff | 117.40 |
| Domain Noise Cutoff | 117.40 |
| Isology Type | equivalog |
| EC Number | 3.11.1.1 |
| HMM Length | 253 |
| Mainrole Category | Central intermediary metabolism |
| Subrole Category | Other |
| Gene Ontology Term | GO:0009636: response to toxin biological_process |
| | GO:0016827: hydrolase activity, acting on acid carbon-phosphorus bonds molecular_function |
| | GO:0019635: 2-aminoethylphosphonate catabolic process biological_process |
| | GO:0019636: phosphonoacetate metabolic process biological_process |
| | GO:0019700: organic phosphonate catabolic process biological_process |
| Author | Selengut J |
| Entry Date | Jan 28 2002 10:59AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme catalyzes the cleavage of the carbon phosphorous bond of a phosphonate. The mechanism depends on the substrate having a carbonyl one carbon away from the cleavage position.
This enzyme is a member of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases (PF00702), and contains a modified version of the conserved catalytic motifs of that superfamily: the first motif is usually DxDx(T/V), here it is DxAxT, and in the third motif the normal conserved lysine is instead an arginine. Additionally, the enzyme contains a unique conserved catalytic lysine (B. cereus pos. 53) which is involved in the binding and activation of the substrate through the formation of a Schiff base. 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 utilized by microorganisms as a chemical warfare agent. |
| References | RN [1]
RM 10956028
RT The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily.
RA Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN
RL Biochemistry 2000 Aug 29;39(34):10385-96.
DR PFAM; PF00702
DR EXPERIMENTAL; GP|10835405|pdb|1FEZ|A; Bacillus cereus
DR OUTGROUP; EGAD|155362|AA0933; Aquifex aolicus; phosphoglycolate phosphatase (pgp)
DR HAMAP; MF_01375; 42 of 42 |
| Genome Property | GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM) |
