|Gene:||phnL||Accession Numbers: EG10721 (MetaCyc), b4096, ECK4089|
Species: Escherichia coli K-12 substr. MG1655
Component of: methylphosphonate degradation complex (summary available)
PhnL, in a mixture together with PhnG, PhnH and PhnI, catalyzes the nucleophilic attack of methylphosphonate on the anomeric carbon of ATP to form adenine and α-D-ribose-1-methylphosphonate-5-triphosphate [Kamat11b].
phnL is part of an operon that is phosphate starvation-inducible and required for use of phosphonate and phosphite as phosphorous sources [Yakovleva98, Metcalf91, Chen90a]. PhnL appears to be required for carbon-phosphorous lyase activity [Metcalf93]. A phnL mutant accumulates presumed intermediates of the C-P lyase pathway of phosphonate degradation [HoveJensen10].
Locations: inner membrane, cytosol
|Map Position: [4,315,238 <- 4,315,918]|
Molecular Weight of Polypeptide: 24.705 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0013421 , CGSC:34529 , EchoBASE:EB0715 , EcoGene:EG10721 , EcoliWiki:b4096 , ModBase:P16679 , OU-Microarray:b4096 , PortEco:phnL , PR:PRO_000023537 , Pride:P16679 , Protein Model Portal:P16679 , RefSeq:NP_418520 , RegulonDB:EG10721 , SMR:P16679 , String:511145.b4096 , UniProt:P16679
Relationship Links: InterPro:IN-FAMILY:IPR003439 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR012701 , InterPro:IN-FAMILY:IPR017871 , InterPro:IN-FAMILY:IPR027417 , Pfam:IN-FAMILY:PF00005 , Prosite:IN-FAMILY:PS00211 , Prosite:IN-FAMILY:PS50893 , Smart:IN-FAMILY:SM00382
|Biological Process:||GO:0019700 - organic phosphonate catabolic process
GO:0006200 - ATP catabolic process [GOA01a]
|Molecular Function:||GO:0000166 - nucleotide binding
GO:0005524 - ATP binding [UniProtGOA11a, GOA01a]
GO:0016740 - transferase activity [UniProtGOA11a]
GO:0016887 - ATPase activity [GOA01a]
|Cellular Component:||GO:0005829 - cytosol
GO:0005886 - plasma membrane [DiazMejia09]
|MultiFun Terms:||metabolism → metabolism of other compounds → phosphorous metabolism|
Subunit of: methylphosphonate degradation complex
Species: Escherichia coli K-12 substr. MG1655
Subunit composition of
methylphosphonate degradation complex = [PhnL][PhnH][PhnG][PhnI]
PhnL subunit of methylphosphonate degradation complex = PhnL (summary available)
PhnH subunit of methylphosphonate degradation complex = PhnH (summary available)
PhnG subunit of methylphosphonate degradation complex = PhnG (summary available)
PhnI subunit of methylphosphonate degradation complex = PhnI (summary available)
A mixture of the purified PhnI, PhnG, PhnH and PhnL polypeptides catalyzes the nucleophilic attack of methylphosphonate on the anomeric carbon of ATP to form adenine and α-D-ribose-1-methylphosphonate-5-triphosphate. The subunit stoichiometry of this complex is unknown [Kamat11b].
Enzymatic reaction of: methylphosphonate degradation complex
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
|Conserved-Region||2 -> 226|
|Nucleotide-Phosphate-Binding-Region||41 -> 48|
10/20/97 Gene b4096 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10721; confirmed by SwissProt match.
Chen90a: 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
HoveJensen10: Hove-Jensen B, Rosenkrantz TJ, Zechel DL, Willemoes M (2010). "Accumulation of intermediates of the carbon-phosphorus lyase pathway for phosphonate degradation in phn mutants of Escherichia coli." J Bacteriol 192(1);370-4. PMID: 19854894
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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