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PROSITE documentation PDOC00173Glutaredoxin active site signature and domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00173
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 [4] 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.
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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). | |
| PubMed ID | 3152490 |
| 2 | Authors | Holmgren A. |
| Title | Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds. | |
| Source | Biochem. Soc. Trans. 16:95-96(1988). | |
| PubMed ID | 3286320 |
| 3 | Authors | Holmgren A. |
| Title | Thioredoxin and glutaredoxin systems. | |
| Source | J. Biol. Chem. 264:13963-13966(1989). | |
| PubMed ID | 2668278 |
| 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. | |
| Source | Virology 181:378-381(1991). | |
| PubMed ID | 1994586 |
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