"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"IPR005746"	"{'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}"	"{}"	"[{'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}]"	""	"[{'identifier': 'GO:0015035', 'name': 'protein-disulfide reductase activity', 'category': {'code': 'F', 'name': 'molecular_function'}}]"	"{'accession': 'IPR005746', 'name': 'Thioredoxin', 'type': 'Family', 'children': []}"	""	False	False	False	"{'PUB00000038': {'PMID': 3896121, 'ISBN': None, 'volume': '54', 'issue': None, 'year': 1985, 'title': 'Thioredoxin.', 'URL': None, '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': None, 'volume': '264', 'issue': '24', 'year': 1989, 'title': 'Thioredoxin and glutaredoxin systems.', 'URL': None, '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': None, 'volume': '3', 'issue': '3', 'year': 1995, 'title': 'Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.', 'URL': None, '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': None, 'volume': '3', 'issue': '3', 'year': 1995, 'title': 'Thioredoxin--a fold for all reasons.', 'URL': None, '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': None, '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': None, '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': None, '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': None, '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': None, 'volume': '231', 'issue': '2', 'year': 1995, 'title': 'Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese.', 'URL': None, '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': None, 'volume': '3', 'issue': '10', 'year': 1995, 'title': 'Crystal structure of thioredoxin-2 from Anabaena.', 'URL': None, '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': None, 'volume': '16', 'issue': '2', 'year': 1988, 'title': 'Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins.', 'URL': None, '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': None}, 'PUB00001495': {'PMID': 2537773, 'ISBN': None, 'volume': '3', 'issue': '5', 'year': 1989, 'title': 'Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit.', 'URL': None, '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': None, 'volume': '19', 'issue': '8', 'year': 1994, 'title': 'Protein disulphide isomerase: building bridges in protein folding.', 'URL': None, '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'}}"	"{'pirsf': {'PIRSF000077': 'Thioredoxin'}, 'ncbifam': {'TIGR01068': 'thioredoxin'}}"	"{'name': 'Thioredoxin', 'short': 'Thioredoxin'}"	"[{'accession': 'IPR036249', 'name': 'Thioredoxin-like superfamily', 'type': 'homologous_superfamily'}]"	"{'accession': '2yn1', 'name': 'Crystal Structure of Ancestral Thioredoxin Relative to Last Gamma- Proteobacteria Common Ancestor (LGPCA) from the Precambrian Period'}"	""	"interpro"	"family"	""