EC - α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase

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IntEnz Enzyme Nomenclature


Accepted name:
α-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase
Other name:
phnJ (gene name)
Systematic name:
α-D-ribose-1-methylphosphonate-5-phosphate C-P-lyase (methane forming)




This radical SAM (AdoMet) enzyme is part of the C-P lyase complex, which is responsible for processing phophonates into usable phosphate. Contains an [4Fe-4S] cluster. The enzyme from the bacterium Escherichia coli can act on additional α-D-ribose phosphonate substrates with different substituents attached to the phosphonate phosphorus (e.g. α-D-ribose-1-[N-(phosphonomethyl)glycine]-5-phosphate and α-D-ribose-1-(2-N-acetamidomethylphosphonate)-5-phosphate).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0098848


  1. Kamat, S. S., Williams, H. J., Raushel, F. M.
    Intermediates in the transformation of phosphonates to phosphate by bacteria.
    Nature 480: 570-573 (2011). [PMID: 22089136]
  2. Jochimsen, B., Lolle, S., McSorley, F. R., Nabi, M., Stougaard, J., Zechel, D. L., Hove-Jensen, B.
    Five phosphonate operon gene products as components of a multi-subunit complex of the carbon-phosphorus lyase pathway.
    Proc. Natl. Acad. Sci. U.S.A. 108: 11393-11398 (2011). [PMID: 21705661]
  3. Zhang, Q., van der Donk, W. A.
    Answers to the carbon-phosphorus lyase conundrum.
    Chembiochem 13: 627-629 (2012). [PMID: 22334536]

[EC created 2013, modified 2016]