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{
"metadata": {
"accession": "IPR011902",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0009055",
"name": "electron transfer activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0015035",
"name": "protein-disulfide reductase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0045454",
"name": "cell redox homeostasis",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"ncbifam": {
"TIGR02183": "glutaredoxin, GrxA family"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR011902",
"name": "Glutaredoxin, GrxA",
"type": "Family",
"children": []
},
"name": {
"name": "Glutaredoxin, GrxA",
"short": "GRXA"
},
"description": [
{
"text": "<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>\n\n<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>\n\n<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>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entry includes the Escherichia coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase [[cite:PUB00015499]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00015562": {
"PMID": 14962389,
"ISBN": null,
"volume": "12",
"issue": "2",
"year": 2004,
"title": "The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues.",
"URL": null,
"raw_pages": "289-300",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Foloppe N",
"Nilsson L."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(04)00021-8"
},
"PUB00015499": {
"PMID": 15123823,
"ISBN": null,
"volume": "101",
"issue": "19",
"year": 2004,
"title": "Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.",
"URL": null,
"raw_pages": "7439-44",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Ortenberg R",
"Gon S",
"Porat A",
"Beckwith J."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.0401965101"
},
"PUB00000560": {
"PMID": 3286320,
"ISBN": null,
"volume": "16",
"issue": "2",
"year": 1988,
"title": "Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.",
"URL": null,
"raw_pages": "95-6",
"medline_journal": "Biochem Soc Trans",
"ISO_journal": "Biochem. Soc. Trans.",
"authors": [
"Holmgren A."
],
"DOI_URL": null
},
"PUB00005575": {
"PMID": 1994586,
"ISBN": null,
"volume": "181",
"issue": "1",
"year": 1991,
"title": "Vaccinia virus encodes a protein with similarity to glutaredoxins.",
"URL": null,
"raw_pages": "378-81",
"medline_journal": "Virology",
"ISO_journal": "Virology",
"authors": [
"Johnson GP",
"Goebel SJ",
"Perkus ME",
"Davis SW",
"Winslow JP",
"Paoletti E."
],
"DOI_URL": "http://dx.doi.org/10.1016/0042-6822(91)90508-9"
},
"PUB00030238": {
"PMID": 10493864,
"ISBN": null,
"volume": "292",
"issue": "1",
"year": 1999,
"title": "Binding specificity and mechanistic insight into glutaredoxin-catalyzed protein disulfide reduction.",
"URL": null,
"raw_pages": "151-61",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Berardi MJ",
"Bushweller JH."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1999.3067"
},
"PUB00023503": {
"PMID": 9860827,
"ISBN": null,
"volume": "37",
"issue": "49",
"year": 1998,
"title": "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.",
"URL": null,
"raw_pages": "17145-56",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Yang Y",
"Jao S",
"Nanduri S",
"Starke DW",
"Mieyal JJ",
"Qin J."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi9806504"
},
"PUB00014033": {
"PMID": 14713336,
"ISBN": null,
"volume": "6",
"issue": "1",
"year": 2004,
"title": "Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.",
"URL": null,
"raw_pages": "63-74",
"medline_journal": "Antioxid Redox Signal",
"ISO_journal": "Antioxid. Redox Signal.",
"authors": [
"Fernandes AP",
"Holmgren A."
],
"DOI_URL": "http://dx.doi.org/10.1089/152308604771978354"
},
"PUB00001738": {
"PMID": 3152490,
"ISBN": null,
"volume": "4",
"issue": "4",
"year": 1988,
"title": "Thioredoxin and related proteins in procaryotes.",
"URL": null,
"raw_pages": "271-97",
"medline_journal": "FEMS Microbiol Rev",
"ISO_journal": "FEMS Microbiol. Rev.",
"authors": [
"Gleason FK",
"Holmgren A."
],
"DOI_URL": null
},
"PUB00080925": {
"PMID": 15706083,
"ISBN": null,
"volume": "7",
"issue": "3-4",
"year": 2005,
"title": "Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation.",
"URL": null,
"raw_pages": "348-66",
"medline_journal": "Antioxid Redox Signal",
"ISO_journal": "Antioxid. Redox Signal.",
"authors": [
"Shelton MD",
"Chock PB",
"Mieyal JJ."
],
"DOI_URL": "http://dx.doi.org/10.1089/ars.2005.7.348"
},
"PUB00080927": {
"PMID": 15814611,
"ISBN": null,
"volume": "280",
"issue": "22",
"year": 2005,
"title": "Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities.",
"URL": null,
"raw_pages": "21099-106",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Xiao R",
"Lundstrom-Ljung J",
"Holmgren A",
"Gilbert HF."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M411476200"
},
"PUB00002504": {
"PMID": 2668278,
"ISBN": null,
"volume": "264",
"issue": "24",
"year": 1989,
"title": "Thioredoxin and glutaredoxin systems.",
"URL": null,
"raw_pages": "13963-6",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Holmgren A."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/264/24/13963.pdf"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036249",
"name": "Thioredoxin-like superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1903,
"pathways": 0,
"proteins": 1903,
"proteomes": 1191,
"sets": 0,
"structural_models": {
"alphafold": 1513,
"bfvd": 0
},
"structures": 4,
"taxa": 2095
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
