| Type: | Active_site | Name: | Glutaredoxin active site |
| 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 entry represents the Glutaredoxin active site. | Short Name: | GLR_AS |
| DB identifier | Type | Name |
|---|---|---|
| IPR012336 | Domain | Thioredoxin-like fold |
| IPR011899 | Domain | Glutaredoxin, eukaryotic/virial |
| IPR002109 | Domain | Glutaredoxin |
| IPR011900 | Family | Glutaredoxin, GrxC |
| IPR011906 | Domain | Glutaredoxin domain |
| IPR011901 | Family | Glutaredoxin, GrxB |
| IPR004502 | Family | Thioredoxins/glutaredoxin |
| IPR011902 | Family | Glutaredoxin, GrxA |
