Description

IPR004480 is a Monothiol glutaredoxin-related.

<p>Glutaredoxins [[cite:PUB00001738], [cite:PUB00000560], [cite:PUB00002504]], 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 [[cite:PUB00014033]].</p> <p>Glutaredoxin functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Like thioredoxin (TRX), which functions in a similar way, glutaredoxin possesses an active centre disulphide bond [[cite:PUB00015562]]. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulphide bond. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH ->GSH reductase ->GSH ->GRX ->protein substrates [[cite:PUB00023503], [cite:PUB00030238], [cite:PUB00080927], [cite:PUB00080925]]. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress.</p> <p>Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity, it has been proposed [[cite:PUB00005575]] that Vaccinia virus protein O2L is most probably a glutaredoxin. Finally, it must be noted that Bacteriophage T4 thioredoxin seems also to be evolutionary related. In position 5 of the pattern T4 thioredoxin has Val instead of Pro.</p> <p>This family groups proteins from different organisms which are related to monothiol glutaredoxins. Monothiol glutaredoxins occur in different subcellular compartments; for instance, yeast Grx3 and Grx4 are nuclear proteins, whereas Grx5 is mitochondrially localized [[cite:PUB00053832]]. They share a common basic structural motif and biochemical mechanism of action, while participating in a diversity of cellular functions as protein redox regulators.</p>

This description is obtained from EB-eye REST.

Associated GO terms

Unable to find any GO terms for the transcript with the identifier.

Associated Lotus transcripts 15

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: