| Accession | TIGR02495 |
| Name | NrdG2 |
| Function | anaerobic ribonucleoside-triphosphate reductase activating protein |
| Trusted Cutoff | 131.15 |
| Domain Trusted Cutoff | 131.15 |
| Noise Cutoff | 101.50 |
| Domain Noise Cutoff | 101.50 |
| Isology Type | equivalog |
| EC Number | 1.97.-.- |
| HMM Length | 193 |
| Author | Selengut J |
| Entry Date | Feb 28 2005 11:08AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme is a member of the radical-SAM family (PF04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG [1,2] which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. |
| References | RN [1]
RM PMID: 11389585
RT Activation of class III ribonucleotide reductase from E. coli. The electron transfer from the iron-sulfur center to S-adenosylmethionine.
RA Padovani D, Thomas F, Trautwein AX, Mulliez E, Fontecave M.
RL Biochemistry. 2001 Jun 12;40(23):6713-9.
RN [2]
RM PMID: 11297442
RT Activation of class III ribonucleotide reductase by flavodoxin: a protein radical-driven electron transfer to the iron-sulfur center.
RA Mulliez E, Padovani D, Atta M, Alcouffe C, Fontecave M.
RL Biochemistry. 2001 Mar 27;40(12):3730-6. |
| Genome Property | GenProp0291: class III (anaerobic) ribonucleotide reductase (HMM) |
