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MetaCyc Polypeptide: PhnL subunit of methylphosphonate degradation complex

Gene: phnL Accession Numbers: EG10721 (MetaCyc), b4096, ECK4089

Species: Escherichia coli K-12 substr. MG1655

Component of: methylphosphonate degradation complex (summary available)

Summary:
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 [Kamat11].

phnL is part of an operon that is phosphate starvation-inducible and required for use of phosphonate and phosphite as phosphorous sources [Yakovleva98, Metcalf91, Chen90]. 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

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0019700 - organic phosphonate catabolic process Inferred from experiment [Metcalf93]
GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol
GO:0005886 - plasma membrane Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism metabolism of other compounds phosphorous metabolism

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


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)

Summary:
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 [Kamat11].

Credits:
Created in EcoCyc 22-Nov-2011 by Keseler I , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: methylphosphonate degradation complex

EC Number: 2.7.8.37

methylphosphonate + ATP <=> α-D-ribose-1-methylphosphonate-5-triphosphate + adenine

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

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
Citations
methylphosphonate
20.0
[Kamat11]
ATP
56.0
[Kamat11]


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 2 -> 226
[UniProt09]
UniProt: ABC transporter;
Nucleotide-Phosphate-Binding-Region 41 -> 48
[UniProt10]
UniProt: ATP; Non-Experimental Qualifier: potential;

History:
10/20/97 Gene b4096 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10721; confirmed by SwissProt match.


References

Chen90: 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

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Kamat11: Kamat SS, Williams HJ, Raushel FM (2011). "Intermediates in the transformation of phosphonates to phosphate by bacteria." Nature 480(7378);570-3. PMID: 22089136

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

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc12.