Protein Domain : IPR017937

Type:  Conserved_site Name:  Thioredoxin, conserved site
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 structural family 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 a conserved site found in the thioredoxin domain. This site contains two cysteines that form the redox-active disulphide bond. Short Name:  Thioredoxin_CS

0 Child Features

0 Contains

1 Cross References

Identifier
PS00194

9 Found Ins

DB identifier Type Name
IPR012336 Domain Thioredoxin-like fold
IPR013766 Domain Thioredoxin domain
IPR005746 Family Thioredoxin
IPR005788 Domain Disulphide isomerase
IPR005792 Family Protein disulphide isomerase
IPR011915 Family Glutaredoxin-like protein, actinobacteria
IPR004799 Family Periplasmic protein thiol:disulphide oxidoreductase DsbE
IPR021170 Family DnaJ homologue subfamily C member 10
IPR017068 Family Protein disulphide-isomerase A4

1 GO Annotation

GO Term Gene Name
GO:0045454 IPR017937

1 Ontology Annotations

GO Term Gene Name
GO:0045454 IPR017937

0 Parent Features

0 Proteins

11 Publications

First Author Title Year Journal Volume Pages PubMed ID
            2668278
            3896121
            3371540
            7635143
            2537773
            7913469
            7983029
            8590004
            7788289
            7788290
            7940678