Phosphonoacetaldehyde hydrolase

Details

Name
Phosphonoacetaldehyde hydrolase
Synonyms
  • 3.11.1.1
  • Phosphonatase
  • Phosphonoacetaldehyde phosphonohydrolase
Gene Name
phnX
Organism
Bacillus cereus
Amino acid sequence
>lcl|BSEQ0006119|Phosphonoacetaldehyde hydrolase
MKIEAVIFDWAGTTVDYGCFAPLEVFMEIFHKRGVAITAEEARKPMGLLKIDHVRALTEM
PRIASEWNRVFRQLPTEADIQEMYEEFEEILFAILPRYASPINGVKEVIASLRERGIKIG
STTGYTREMMDIVAKEAALQGYKPDFLVTPDDVPAGRPYPWMCYKNAMELGVYPMNHMIK
VGDTVSDMKEGRNAGMWTVGVILGSSELGLTEEEVENMDSVELREKIEVVRNRFVENGAH
FTIETMQELESVMEHIEKQELIIS
Number of residues
264
Molecular Weight
30059.425
Theoretical pI
4.5
GO Classification
Functions
magnesium ion binding / phosphonoacetaldehyde hydrolase activity
Processes
organic phosphonate catabolic process
General Function
Phosphonoacetaldehyde hydrolase activity
Specific Function
Involved in phosphonate degradation.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDO31156
UniProtKB Entry NamePHNX_BACCE
General References
  1. Baker AS, Ciocci MJ, Metcalf WW, Kim J, Babbitt PC, Wanner BL, Martin BM, Dunaway-Mariano D: Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis. Biochemistry. 1998 Jun 30;37(26):9305-15. [Article]
  2. Olsen DB, Hepburn TW, Lee SL, Martin BM, Mariano PS, Dunaway-Mariano D: Investigation of the substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase. Arch Biochem Biophys. 1992 Jul;296(1):144-51. [Article]
  3. Morais MC, Baker AS, Dunaway-Mariano D, Allen KN: Crystallization and preliminary crystallographic analysis of phosphonoacetaldehyde hydrolase. Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):206-9. [Article]
  4. Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN: The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry. 2000 Aug 29;39(34):10385-96. [Article]
  5. Morais MC, Zhang G, Zhang W, Olsen DB, Dunaway-Mariano D, Allen KN: X-ray crystallographic and site-directed mutagenesis analysis of the mechanism of Schiff-base formation in phosphonoacetaldehyde hydrolase catalysis. J Biol Chem. 2004 Mar 5;279(10):9353-61. Epub 2003 Dec 10. [Article]
  6. Lahiri SD, Zhang G, Dai J, Dunaway-Mariano D, Allen KN: Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry. 2004 Mar 16;43(10):2812-20. [Article]
  7. Zhang G, Morais MC, Dai J, Zhang W, Dunaway-Mariano D, Allen KN: Investigation of metal ion binding in phosphonoacetaldehyde hydrolase identifies sequence markers for metal-activated enzymes of the HAD enzyme superfamily. Biochemistry. 2004 May 4;43(17):4990-7. [Article]
  8. Lahiri SD, Zhang G, Dunaway-Mariano D, Allen KN: Diversification of function in the haloacid dehalogenase enzyme superfamily: The role of the cap domain in hydrolytic phosphoruscarbon bond cleavage. Bioorg Chem. 2006 Dec;34(6):394-409. Epub 2006 Oct 27. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03635Ethanesulfonic acidexperimentalunknownDetails
DB04359Vinylsulfonic acidexperimentalunknownDetails
DB03174PhosphonoacetaldehydeexperimentalunknownDetails