Accession | TIGR02493 |
Name | PFLA |
Function | pyruvate formate-lyase 1-activating enzyme |
Gene Symbol | pflA |
Trusted Cutoff | 231.75 |
Domain Trusted Cutoff | 231.75 |
Noise Cutoff | 203.45 |
Domain Noise Cutoff | 203.45 |
Isology Type | equivalog |
EC Number | 1.97.1.4 |
HMM Length | 235 |
Mainrole Category | Energy metabolism |
Subrole Category | Anaerobic |
Gene Ontology Term | GO:0018307: enzyme active site formation biological_process |
| GO:0043365: [formate-C-acetyltransferase]-activating enzyme activity molecular_function |
Author | Selengut J |
Entry Date | Feb 25 2005 3:34PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | An iron-sulfur protein with a radical-SAM domain (PF04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue [1]. |
References | RN [1]
RM PMID: 8175649
RT Adenosylmethionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. Studies of [2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site.
RA Frey M, Rothe M, Wagner AF, Knappe J.
RL J Biol Chem. 1994 Apr 29;269(17):12432-7. |
Genome Property | GenProp0943: pyruvate formate-lyase system (HMM) |