HMM Summary Page: TIGR02183

Functionglutaredoxin, GrxA family
Gene SymbolgrxA
Trusted Cutoff106.50
Domain Trusted Cutoff106.50
Noise Cutoff68.25
Domain Noise Cutoff68.25
Isology Typeequivalog
HMM Length86
AuthorSelengut J
Entry DateMay 7 2004 12:49PM
Last ModifiedMar 1 2011 11:50AM
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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase [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: 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]