Conserved Site

Formate C-acetyltransferase glycine radical, conserved site (IPR019777)

Short name: Form_AcTrfase_GR_CS


Synonym(s):Pyruvate formate-lyase

Protein radicals are components of several biologically important reactions. Glycyl radical enzymes are involved in a great variety of functions, for example, nucleotide, pyruvate and toluene metabolism [PMID: 10574800]. These enzymes are post-translationally interconverted, under anaerobic conditions, from an inactive to an active form that carries a stable radical localised to a specific glycine at the C-terminal region of the polypeptidic chain. Extreme sensitivity towards destruction by oxygen, leading to polypeptide cleavage between the N-C alpha-bond of the Gly residue, is a conspicuous property of all protein-based glycyl radicals, thus confining their existence to strictly anaerobic conditions.

Some proteins known to contain a glycyl radical are listed below:

  • Escherichia coli pyruvate formate-lyase (EC:, genes pflB, pflD and pflF), a key enzyme of anaerobic glucose metabolism, it converts pyruvate and CoA into acetyl-CoA and pyruvate [PMID: 1310545].
  • E. coli (gene nrdD) and Bacteriophage T4 (gene nrdD or sunY) anaerobic ribonucleoside-triphosphate reductase (EC: [PMID: 8421692, PMID: 8051113].
  • E. coli and Bacteriophage T4 autonomous glycyl radical cofactor (gene grcA) [PMID: 11444864].

The signature pattern in this entry is based on a conserved region centred on the glycine which, in Pfl, is known to bear the free radical.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns