HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "IPR005746",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0015035",
"name": "protein-disulfide reductase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF000077": "Thioredoxin"
},
"ncbifam": {
"TIGR01068": "thioredoxin"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005746",
"name": "Thioredoxin",
"type": "Family",
"children": []
},
"name": {
"name": "Thioredoxin",
"short": "Thioredoxin"
},
"description": [
{
"text": "<p>This entry represents the thioredoxin protein family.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Thioredoxins [[cite:PUB00000038], [cite:PUB00002504], [cite:PUB00005258], [cite:PUB00005259]] are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. In the NADPH-dependent protein disulphide reduction, thioredoxin reductase (TR) catalyses the reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide; reduced thioredoxin then directly reduces the disulphide in the substrate protein [[cite:PUB00000038]].</p>\r\n\r\n<p>Thioredoxin is present in prokaryotes and eukaryotes and the sequence around the redox-active disulphide bond is well conserved. All thioredoxins contain a cis-proline located in a loop preceding β-strand 4, which makes contact with the active site cysteines, and is important for stability and function [[cite:PUB00005250]]. Thioredoxin belongs to a structural family that includes glutaredoxin, glutathione peroxidase, bacterial protein disulphide isomerase DsbA, and the N-terminal domain of glutathione transferase [[cite:PUB00005259]]. Thioredoxins have a β-α unit preceding the motif common to all these proteins.</p>\r\n\r\n<p>A number of eukaryotic proteins contain domains evolutionary related to thioredoxin, most of them are protein disulphide isomerases (PDI). PDI ([ec:5.3.4.1]) [[cite:PUB00000561], [cite:PUB00001495], [cite:PUB00005423]] is an endoplasmic reticulum multi-functional enzyme that catalyses the formation and rearrangement of disulphide bonds during protein folding [[cite:PUB00002862]]. All PDI contains two or three (ERp72) copies of the thioredoxin domain, each of which contributes to disulphide isomerase activity, but which are functionally non-equivalent [[cite:PUB00002883]]. Moreover, PDI exhibits chaperone-like activity towards proteins that contain no disulphide bonds, i.e. behaving independently of its disulphide isomerase activity [[cite:PUB00001458]]. The various forms of PDI which are currently known are:</p>\r\n\r\n\n<ul><li>PDI major isozyme; a multifunctional protein that also function as the beta subunit of prolyl 4-hydroxylase ([ec:1.14.11.2]), as a component of oligosaccharyl transferase ([ec:2.4.1.119]), as thyroxine deiodinase ([ec:3.8.1.4]), as glutathione-insulin transhydrogenase ([ec:1.8.4.2]) and as a thyroid hormone-binding protein</li>\r\n<li>ERp60 (ER-60; 58 Kd microsomal protein). ERp60 was originally thought to be a phosphoinositide-specific phospholipase C isozyme and later to be a protease.</li>\r\n<li>ERp72.</li>\r\n<li>ERp5.</li></ul>\r\n\r\n<p>Bacterial proteins that act as thiol:disulphide interchange proteins that allows disulphide bond formation in some periplasmic proteins also contain a thioredoxin domain. These proteins include:</p>\r\n\r\n\n<ul><li>Escherichia coli DsbA (or PrfA) and its orthologs in Vibrio cholerae (TtcpG) and Haemophilus influenzae (Por).</li>\r\n<li>E. coli DsbC (or XpRA) and its orthologues in Erwinia chrysanthemi and H. influenzae.</li>\r\n<li>E. coli DsbD (or DipZ) and its H. influenzae orthologue.</li>\r\n<li>E. coli DsbE (or CcmG) and orthologues in H. influenzae.</li>\r\n<li>Rhodobacter capsulatus (Rhodopseudomonas capsulata) (HelX), Rhiziobiacae (CycY and TlpA).</li></ul>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000038": {
"PMID": 3896121,
"ISBN": null,
"volume": "54",
"issue": null,
"year": 1985,
"title": "Thioredoxin.",
"URL": null,
"raw_pages": "237-71",
"medline_journal": "Annu Rev Biochem",
"ISO_journal": "Annu. Rev. Biochem.",
"authors": [
"Holmgren A."
],
"DOI_URL": "http://dx.doi.org/10.1146/annurev.bi.54.070185.001321"
},
"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"
},
"PUB00005258": {
"PMID": 7788289,
"ISBN": null,
"volume": "3",
"issue": "3",
"year": 1995,
"title": "Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.",
"URL": null,
"raw_pages": "239-43",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Holmgren A."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00153-8"
},
"PUB00005259": {
"PMID": 7788290,
"ISBN": null,
"volume": "3",
"issue": "3",
"year": 1995,
"title": "Thioredoxin--a fold for all reasons.",
"URL": null,
"raw_pages": "245-50",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Martin JL."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00154-X"
},
"PUB00002862": {
"PMID": 7913469,
"ISBN": null,
"volume": "269",
"issue": "29",
"year": 1994,
"title": "The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.",
"URL": null,
"raw_pages": "19128-35",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Puig A",
"Lyles MM",
"Noiva R",
"Gilbert HF."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/269/29/19128"
},
"PUB00002883": {
"PMID": 7983029,
"ISBN": null,
"volume": "269",
"issue": "49",
"year": 1994,
"title": "Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.",
"URL": null,
"raw_pages": "30946-52",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Lyles MM",
"Gilbert HF."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/269/49/30946.pdf"
},
"PUB00001458": {
"PMID": 7635143,
"ISBN": null,
"volume": "231",
"issue": "2",
"year": 1995,
"title": "Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.",
"URL": null,
"raw_pages": "312-6",
"medline_journal": "Eur J Biochem",
"ISO_journal": "Eur. J. Biochem.",
"authors": [
"Song JL",
"Wang CC."
],
"DOI_URL": "http://dx.doi.org/10.1111/j.1432-1033.1995.tb20702.x"
},
"PUB00005250": {
"PMID": 8590004,
"ISBN": null,
"volume": "3",
"issue": "10",
"year": 1995,
"title": "Crystal structure of thioredoxin-2 from Anabaena.",
"URL": null,
"raw_pages": "1097-108",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Saarinen M",
"Gleason FK",
"Eklund H."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0969-2126(01)00245-3"
},
"PUB00000561": {
"PMID": 3371540,
"ISBN": null,
"volume": "16",
"issue": "2",
"year": 1988,
"title": "Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins.",
"URL": null,
"raw_pages": "96-9",
"medline_journal": "Biochem Soc Trans",
"ISO_journal": "Biochem. Soc. Trans.",
"authors": [
"Freedman RB",
"Hawkins HC",
"Murant SJ",
"Reid L."
],
"DOI_URL": null
},
"PUB00001495": {
"PMID": 2537773,
"ISBN": null,
"volume": "3",
"issue": "5",
"year": 1989,
"title": "Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.",
"URL": null,
"raw_pages": "1609-17",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J.",
"authors": [
"Kivirikko KI",
"Myllyla R",
"Pihlajaniemi T."
],
"DOI_URL": "http://www.fasebj.org/cgi/content/abstract/3/5/1609"
},
"PUB00005423": {
"PMID": 7940678,
"ISBN": null,
"volume": "19",
"issue": "8",
"year": 1994,
"title": "Protein disulphide isomerase: building bridges in protein folding.",
"URL": null,
"raw_pages": "331-6",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Freedman RB",
"Hirst TR",
"Tuite MF."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(94)90072-8"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036249",
"name": "Thioredoxin-like superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 60035,
"pathways": 74,
"proteins": 60021,
"proteomes": 20749,
"sets": 0,
"structural_models": {
"alphafold": 46776,
"bfvd": 6
},
"structures": 267,
"taxa": 39240
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2yn1",
"name": "Crystal Structure of Ancestral Thioredoxin Relative to Last Gamma- Proteobacteria Common Ancestor (LGPCA) from the Precambrian Period"
}
}
}
