HMM Summary Page: TIGR01422

AccessionTIGR01422
Namephosphonatase
Functionphosphonoacetaldehyde hydrolase
Gene SymbolphnX
Trusted Cutoff221.20
Domain Trusted Cutoff221.20
Noise Cutoff117.40
Domain Noise Cutoff117.40
Isology Typeequivalog
EC Number3.11.1.1
HMM Length253
Mainrole CategoryCentral intermediary metabolism
Subrole CategoryOther
Gene Ontology TermGO:0009636: response to toxin biological_process
GO:0009636: response to toxin biological_process
GO:0009636: response to toxin biological_process
GO:0016827: hydrolase activity, acting on acid carbon-phosphorus bonds molecular_function
GO:0016827: hydrolase activity, acting on acid carbon-phosphorus bonds molecular_function
GO:0016827: hydrolase activity, acting on acid carbon-phosphorus bonds molecular_function
GO:0019635: 2-aminoethylphosphonate catabolic process biological_process
GO:0019635: 2-aminoethylphosphonate catabolic process biological_process
GO:0019635: 2-aminoethylphosphonate catabolic process biological_process
GO:0019636: phosphonoacetate metabolic process biological_process
GO:0019636: phosphonoacetate metabolic process biological_process
GO:0019636: phosphonoacetate metabolic process biological_process
GO:0019700: organic phosphonate catabolic process biological_process
GO:0019700: organic phosphonate catabolic process biological_process
GO:0019700: organic phosphonate catabolic process biological_process
AuthorSelengut J
Entry DateJan 28 2002 10:59AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis 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.
ReferencesRN [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 PropertyGenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)
GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)
GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)
GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)
GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)
GenProp0238: 2-aminoethylphosphonate catabolism to acetaldehyde (HMM)