Accession | TIGR02182 |
Name | GRXB |
Function | glutaredoxin, GrxB family |
Gene Symbol | grxB |
Trusted Cutoff | 186.65 |
Domain Trusted Cutoff | 186.65 |
Noise Cutoff | 134.20 |
Domain Noise Cutoff | 134.20 |
Isology Type | equivalog |
HMM Length | 209 |
Mainrole Category | Energy metabolism |
Subrole Category | Electron transport |
Gene Ontology Term | GO:0006790: sulfur compound metabolic process biological_process |
| GO:0015035: protein disulfide oxidoreductase activity molecular_function |
| GO:0042965: glutaredoxin biosynthetic process biological_process |
| GO:0045454: cell redox homeostasis biological_process |
| GO:0055114: oxidation-reduction process biological_process |
Author | Selengut J |
Entry Date | May 7 2004 12:36PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [1]. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides.
This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase [2], and may have more to do with resistance to redox stress [3]. |
References | RN [1]
RM PMID: 14713336
RT Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.
RA Fernandes AP, Holmgren A.
RL Antioxid Redox Signal. 2004 Feb;6(1):63-74.
RN [2]
RM PMID: 15123823
RT Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.
RA Ortenberg R, Gon S, Porat A, Beckwith J.
RL Proc Natl Acad Sci U S A. 2004 Apr 27 [Epub ahead of print]
RN [3]
RM PMID: 11741965
RT Characterization of Escherichia coli null mutants for glutaredoxin 2.
RA Vlamis-Gardikas A, Potamitou A, Zarivach R, Hochman A, Holmgren A.
RL J Biol Chem. 2002 Mar 29;277(13):10861-8. Epub 2001 Dec 10. |