HMM Summary Page: TIGR02181

Functionglutaredoxin 3
Gene SymbolgrxC
Trusted Cutoff90.00
Domain Trusted Cutoff90.00
Noise Cutoff82.45
Domain Noise Cutoff82.45
Isology Typeequivalog
HMM Length80
Mainrole CategoryEnergy metabolism
Subrole CategoryElectron transport
Gene Ontology TermGO:0015036: disulfide oxidoreductase activity molecular_function
GO:0055114: oxidation-reduction process biological_process
AuthorSelengut J
Entry DateMay 7 2004 11:19AM
Last ModifiedFeb 14 2011 3:27PM
CommentGlutaredoxins 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 family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides [2].
ReferencesRN [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: 7937896 RT Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. RA Aslund F, Ehn B, Miranda-Vizuete A, Pueyo C, Holmgren A. RL Proc Natl Acad Sci U S A. 1994 Oct 11;91(21):9813-7.