HMM Summary Page: TIGR02180

Trusted Cutoff87.25
Domain Trusted Cutoff87.25
Noise Cutoff79.95
Domain Noise Cutoff79.95
Isology Typeequivalog
HMM Length84
AuthorSelengut J
Entry DateMay 7 2004 10:31AM
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 represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
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.