| Type: | Domain | Name: | Glutaredoxin domain |
| Description: | Glutaredoxins [, , ], also known as thioltransferases (disulphide reductases, are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system []. Glutaredoxin 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 centre disulphide bond []. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulphide bond.Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed [] that Vaccinia virusprotein O2L is most probably a glutaredoxin. Finally, it must be noted that Bacteriophage T4thioredoxin seems also to be evolutionary related. In position 5 of the pattern T4 thioredoxin has Val instead of Pro.This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain. | Short Name: | Glutaredoxin_dom |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Brdisv1pangenome1006473m.p | PAC:33599069 | Brachypodium distachyon Pangenome |
85
 |
|
| Brdisv1BdTR11A1041316m.p | PAC:35690870 | Brachypodium distachyon BdTR11a |
85
|
