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
- Functionsmagnesium ion binding / phosphonoacetaldehyde hydrolase activityProcessesorganic phosphonate catabolic process
- General Function
- Phosphonoacetaldehyde hydrolase activity
- Specific Function
- Involved in phosphonate degradation.
- Pfam Domain Function
- HAD_2 (PF13419)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID O31156 UniProtKB Entry Name PHNX_BACCE - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]