Protein Domain : IPR001989

Type:  Conserved_site Name:  Radical-activating enzyme, conserved site
Description:  In Escherichia coliand 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 T4and 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 influenzaehypothetical 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 could be involved in iron-binding. Short Name:  Radical_activat_CS

0 Child Features

0 Contains

1 Cross References

Identifier
PS01087

4 Found Ins

DB identifier Type Name
IPR007197 Domain Radical SAM
IPR012839 Family Glycyl radical enzyme activase
IPR012838 Family Pyruvate formate-lyase activating enzyme
IPR012837 Family Ribonucleoside-triphosphate reductase activating, anaerobic

3 GO Annotations

GO Term Gene Name
GO:0016491 IPR001989
GO:0051539 IPR001989
GO:0055114 IPR001989

3 Ontology Annotations

GO Term Gene Name
GO:0016491 IPR001989
GO:0051539 IPR001989
GO:0055114 IPR001989

0 Parent Features

0 Proteins

3 Publications

First Author Title Year Journal Volume Pages PubMed ID
            3053170
            7852304
            7773398