Description

IPR013766 is a Thioredoxin domain.

<p>This entry represents the thioredoxin domain.</p> <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> <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> <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> <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> <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> <li>ERp72.</li> <li>ERp5.</li></ul> <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> <ul><li>Escherichia coli DsbA (or PrfA) and its orthologs in Vibrio cholerae (TtcpG) and Haemophilus influenzae (Por).</li> <li>E. coli DsbC (or XpRA) and its orthologues in Erwinia chrysanthemi and H. influenzae.</li> <li>E. coli DsbD (or DipZ) and its H. influenzae orthologue.</li> <li>E. coli DsbE (or CcmG) and orthologues in H. influenzae.</li> <li>Rhodobacter capsulatus (Rhodopseudomonas capsulata) (HelX), Rhiziobiacae (CycY and TlpA).</li></ul>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 164