Accession | TIGR02476 |
Name | BluB |
Function | 5,6-dimethylbenzimidazole synthase |
Gene Symbol | bluB |
Trusted Cutoff | 150.00 |
Domain Trusted Cutoff | 150.00 |
Noise Cutoff | 120.00 |
Domain Noise Cutoff | 120.00 |
Isology Type | equivalog |
EC Number | 1.14.99.40 |
HMM Length | 205 |
Gene Ontology Term | GO:0009236: cobalamin biosynthetic process biological_process |
| GO:0016722: oxidoreductase activity, oxidizing metal ions molecular_function |
Author | Haft DH, Selengut J |
Entry Date | Feb 16 2005 4:18PM |
Last Modified | Feb 10 2012 10:31AM |
Comment | A previously published hypothesis that BluB, involved in cobalamin biosynthesis, is EC 1.16.8.1 (cob(II)yrinic acid a,c-diamide reductase) is now contradicted by newer work ascribing a role in 5,6-dimethylbenzimidazole (DMB) biosynthesis. The BluB protein is related to the nitroreductase family (PF0881). |
References | RN [1]
RM PMID:17301238
RT Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12.
RA Gray MJ, Escalante-Semerena JC
RL Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2921-6.
RN [2]
RM PMID:17377583
RT BluB cannibalizes flavin to form the lower ligand of vitamin B12.
RA Taga ME, Larsen NA, Howard-Jones AR, Walsh CT, Walker GC
RL Nature. 2007 Mar 22;446(7134):449-53.
RN [3]
RM PMID: 12869542
RT Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.
RA Rodionov DA, Vitreschak AG, Mironov AA, Gelfand MS.
RL J Biol Chem. 2003 Oct 17;278(42):41148-59.
RN [4]
RM PMID: 7635831
RT Identification and sequence analysis of genes involved in late steps in cobalamin (vitamin B12) synthesis in Rhodobacter capsulatus.
RA Pollich M, Klug G.
RL J Bacteriol. 1995 Aug;177(15):4481-7. |