|Gene:||phnM||Accession Numbers: EG10722 (MetaCyc), b4095, ECK4088|
Species: Escherichia coli K-12 substr. MG1655
PhnM catalyzes hydrolysis of α-D-ribose-1-methylphosphonate-5-triphosphate, generating α-D-ribose-1-methylphosphonate 5-phosphate and pyrophosphate [Kamat11]. PhnM is a member of the amidohydrolase superfamily [Seibert05].
phnM is part of an operon that is phosphate starvation-inducible and required for use of phosphonate and phosphite as phosphorous sources [Yakovleva98, Metcalf91, Chen90c]. PhnM appeared to be required for carbon-phosphorous lyase activity [Metcalf93].
Locations: cytosol, inner membrane
|Map Position: [4,314,105 <- 4,315,241]|
Molecular Weight of Polypeptide: 42.01 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0013419 , CGSC:34526 , EchoBASE:EB0716 , EcoGene:EG10722 , EcoliWiki:b4095 , ModBase:P16689 , OU-Microarray:b4095 , PortEco:phnM , Protein Model Portal:P16689 , RefSeq:NP_418519 , RegulonDB:EG10722 , SMR:P16689 , String:511145.b4095 , UniProt:P16689
|Biological Process:||GO:0019700 - organic phosphonate catabolic process [GOA01a, Metcalf93]|
|Molecular Function:||GO:0016787 - hydrolase activity
GO:0016810 - hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GOA01a]
|Cellular Component:||GO:0005829 - cytosol
GO:0005886 - plasma membrane
|MultiFun Terms:||cell structure → membrane|
|metabolism → metabolism of other compounds → phosphorous metabolism|
Enzymatic reaction of: RPnTP hydrolase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: methylphosphonate degradation I
10/20/97 Gene b4095 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10722; confirmed by SwissProt match.
Chen90c: Chen CM, Ye QZ, Zhu ZM, Wanner BL, Walsh CT (1990). "Molecular biology of carbon-phosphorus bond cleavage. Cloning and sequencing of the phn (psiD) genes involved in alkylphosphonate uptake and C-P lyase activity in Escherichia coli B." J Biol Chem 265(8);4461-71. PMID: 2155230
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Metcalf91: Metcalf WW, Wanner BL (1991). "Involvement of the Escherichia coli phn (psiD) gene cluster in assimilation of phosphorus in the form of phosphonates, phosphite, Pi esters, and Pi." J Bacteriol 173(2);587-600. PMID: 1846145
Metcalf93: Metcalf WW, Wanner BL (1993). "Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements." J Bacteriol 175(11);3430-42. PMID: 8388873
Yakovleva98: Yakovleva GM, Kim SK, Wanner BL (1998). "Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli." Appl Microbiol Biotechnol 49(5);573-8. PMID: 9650256
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