InterPro : IPR005746

Name  Thioredoxin Short Name  Thioredoxin
Type  Family Description  Thioredoxins [, , , ]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 [].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 beta-strand 4, which makes contact with the active site cysteines, and is important for stability and function []. Thioredoxin belongs to a structuralfamily that includes glutaredoxin, glutathione peroxidase, bacterial protein disulphide isomerase DsbA, and the N-terminal domain of glutathione transferase []. Thioredoxins have a beta-alpha unit preceding the motif common to all these proteins.A number of eukaryotic proteins contain domains evolutionary related to thioredoxin, most of them are protein disulphide isomerases (PDI). PDI () [, , ]is an endoplasmic reticulum multi-functional enzyme that catalyses the formation and rearrangement of disulphide bonds during protein folding []. 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 []. Moreover, PDI exhibits chaperone-like activity towards proteins that contain no disulphide bonds, i.e. behaving independently of its disulphide isomerase activity []. The various forms of PDI which are currently known are:PDI major isozyme; a multifunctional protein that also function as the beta subunit of prolyl 4-hydroxylase (), as a component of oligosaccharyl transferase (), as thyroxine deiodinase (), as glutathione-insulin transhydrogenase () and as a thyroid hormone-binding proteinERp60 (ER-60; 58 Kd microsomal protein). ERp60 was originally thought to be a phosphoinositide-specific phospholipase C isozyme and later to be a protease.ERp72.ERp5.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:Escherichia coliDsbA (or PrfA) and its orthologs in Vibrio cholerae(TtcpG) and Haemophilus influenzae(Por).E. coli DsbC (or XpRA) and its orthologues in Erwinia chrysanthemiand H. influenzae.E. coli DsbD (or DipZ) and its H. influenzae orthologue.E. coli DsbE (or CcmG) and orthologues in H. influenzae.Rhodobacter capsulatus(Rhodopseudomonas capsulata) (HelX), Rhiziobiacae (CycY and TlpA).This entry represents thioredoxin protein family.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR013766 Thioredoxin domain Thioredoxin_domain Domain
IPR017937 Thioredoxin, conserved site Thioredoxin_CS Conserved_site

0 Found In

0 Parent Features

11 Publications

First Author Title Year Journal Volume Pages
Holmgren A Thioredoxin and glutaredoxin systems. 1989 J Biol Chem 264 13963-6
Holmgren A Thioredoxin. 1985 Annu Rev Biochem 54 237-71
Holmgren A Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. 1995 Structure 3 239-43
Martin JL Thioredoxin--a fold for all reasons. 1995 Structure 3 245-50
Freedman RB Protein disulphide-isomerase: a homologue of thioredoxin implicated in the biosynthesis of secretory proteins. 1988 Biochem Soc Trans 16 96-9
Song JL Chaperone-like activity of protein disulfide-isomerase in the refolding of rhodanese. 1995 Eur J Biochem 231 312-6
Kivirikko KI Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. 1989 FASEB J 3 1609-17
Puig A The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase. 1994 J Biol Chem 269 19128-35
Lyles MM Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains. 1994 J Biol Chem 269 30946-52
Saarinen M Crystal structure of thioredoxin-2 from Anabaena. 1995 Structure 3 1097-108
Freedman RB Protein disulphide isomerase: building bridges in protein folding. 1994 Trends Biochem Sci 19 331-6

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)