1 Proteins
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Pavir.9NG427200.1.p | PAC:37650325 | Panicum virgatum |
75
 |
| Type: | Family | Name: | Glutaredoxin-like protein NrdH |
| 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.NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterised by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH apparently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase []. | Short Name: | GlrX_NrdH |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Pavir.9NG427200.1.p | PAC:37650325 | Panicum virgatum |
75
|
