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PROSITE documentation PDOC00173 [for PROSITE entry PS51354]

Glutaredoxin active site signature and domain profile





Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

GLUTAREDOXIN_2, PS51354; Glutaredoxin domain profile  (MATRIX)

GLUTAREDOXIN_1, PS00195; Glutaredoxin active site  (PATTERN)


References

1AuthorsGleason F.K. Holmgren A.
TitleThioredoxin and related proteins in procaryotes.
SourceFEMS Microbiol. Rev. 4:271-297(1988).
PubMed ID3152490

2AuthorsHolmgren A.
TitleThioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.
SourceBiochem. Soc. Trans. 16:95-96(1988).
PubMed ID3286320

3AuthorsHolmgren A.
TitleThioredoxin and glutaredoxin systems.
SourceJ. Biol. Chem. 264:13963-13966(1989).
PubMed ID2668278

4AuthorsJohnson G.P. Goebel S.J. Perkus M.E. Davis S.W. Winslow J.P. Paoletti E.
TitleVaccinia virus encodes a protein with similarity to glutaredoxins.
SourceVirology 181:378-381(1991).
PubMed ID1994586



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