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glutaredoxin family protein
These proteins are related to the Pfam:PF00462 family. This entry includes several viral glutaredoxins and many related bacterial and eukaryotic proteins of unknown function. The best characterised member is G4L (Swiss:P68460) from Vaccinia virus (strain Western Reserve/WR) (VACV), which is necessary for virion morphogenesis and replication [1]. This is a cytoplasmic protein which functions as a shuttle in a redox pathway between membrane-associated E10R and L1R or F9L [2]. [1]. 10982364. A glutaredoxin, encoded by the G4L gene of vaccinia virus, is essential for virion morphogenesis. White CL, Weisberg AS, Moss B;. J Virol. 2000;74:9175-9183. [2]. 11752136. Vaccinia virus G4L glutaredoxin is an essential intermediate of a cytoplasmic disulfide bond pathway required for virion assembly. White CL, Senkevich TG, Moss B;. J Virol. 2002;76:467-472. (from Pfam)
glutaredoxin domain-containing protein
GrxA family glutaredoxin
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 E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase [2].
glutaredoxin
glutaredoxin is a glutathione dependent reductase that catalyzes the reduction of disulfides in target proteins such as ribonucleotide reductase
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