| Accession | TIGR02491 |
| Name | NrdG |
| Function | anaerobic ribonucleoside-triphosphate reductase activating protein |
| Gene Symbol | nrdG |
| Trusted Cutoff | 126.10 |
| Domain Trusted Cutoff | 126.10 |
| Noise Cutoff | 114.40 |
| Domain Noise Cutoff | 114.40 |
| Isology Type | equivalog |
| EC Number | 1.97.1.- |
| HMM Length | 154 |
| Mainrole Category | Purines, pyrimidines, nucleosides, and nucleotides |
| Subrole Category | 2'-Deoxyribonucleotide metabolism |
| Gene Ontology Term | GO:0005506: iron ion binding molecular_function |
| | GO:0008998: ribonucleoside-triphosphate reductase activity molecular_function |
| | GO:0009265: 2'-deoxyribonucleotide biosynthetic process biological_process |
| | GO:0043365: [formate-C-acetyltransferase]-activating enzyme activity molecular_function |
| Author | Selengut J |
| Entry Date | Feb 25 2005 10:42AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This enzyme [1] is a member of the radical-SAM family (PF04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin [2]) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. |
| 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) |
