Protein Domain : Radical-activating enzyme, conserved site IPR001989

Type	Conserved_site
Description	In Escherichia coli and related bacteria, the pflA protein (or act) [ ] is involved () in the activation of pyruvate formate-lyase (gene pflB) under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine. The activity of pflA is iron-dependent. A protein highly similar to pflA and termed pflC [ ] is probably involved in the activation of a second pyruvate format lyase (gene pflD). The pflA/pflC proteins belong to a family that also includes Bacteriophage T4 and E. coli nrdG which are involved [] in the generation of the free radical for the anaerobic ribonucleoside-triphosphate reductase (gene nrdD or sunY). It also includes E. coli hypothetical protein yjjW, Haemophilus influenzae hypothetical protein HI0520 and Methanocaldococcus jannaschii (Methanococcus jannaschii) hypothetical protein MJ0021. All these proteins possess, in their N-terminal section, a highly conserved region which contains three clustered cysteines which are involved in iron-binding.
Short Name	Radical_activat_CS