|PROSITE documentation PDOC00173 [for PROSITE entry PS51354]|
Glutaredoxin [1,2,3], also known as thioltransferase, is a small protein of approximately one hundred amino-acid residues. It functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Like thioredoxin, which functions in a similar way, glutaredoxin possesses an active center disulfide bond. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulfide bond.
Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed  that vaccinia protein O2L is most probably a glutaredoxin. Finally, it must be noted that phage T4 thioredoxin seems also to be evolutionary related.
The pattern is directed against the 2 cysteines of the redox active bonds. We also developed a profile that covers the whole glutaredoxin domain.Note:
In position 5 of the pattern, all glutaredoxin sequences have Pro while T4 thioredoxin has Val.Last update:
December 2007 / Text revised and profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Gleason F.K. Holmgren A.|
|Title||Thioredoxin and related proteins in procaryotes.|
|Source||FEMS Microbiol. Rev. 4:271-297(1988).|
|Title||Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.|
|Source||Biochem. Soc. Trans. 16:95-96(1988).|
|Title||Thioredoxin and glutaredoxin systems.|
|Source||J. Biol. Chem. 264:13963-13966(1989).|
|4||Authors||Johnson G.P. Goebel S.J. Perkus M.E. Davis S.W. Winslow J.P. Paoletti E.|
|Title||Vaccinia virus encodes a protein with similarity to glutaredoxins.|