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InterPro: IPR005982 Thioredoxin reductase

Protein matchesHelp
UniProtKB
Matches:
1804 proteins
AccessionHelp IPR005982 Thioredox_Rdtase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000103 Pyridine nucleotide-disulphide oxidoreductase, class-II
Contains IPR001327 Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR008255 Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
GO Term annotationHelp
Process GO:0019430 removal of superoxide radicals
GO:0055114 oxidation reduction
Function GO:0004791 thioredoxin-disulfide reductase activity
Component GO:0005737 cytoplasm
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Reactive oxygen species (ROS) are known mediators of intracellular signalling cascades. Excessive production of ROS may, however, lead to oxidative stress, loss of cell function, and ultimately apoptosis or necrosis. A balance between oxidant and antioxidant intracellular systems is hence vital for cell function, regulation, and adaptation to diverse growth conditions. Thioredoxin reductase in conjunction with thioredoxin is a ubiquitous oxidoreductase system with antioxidant and redox regulatory roles. Thioredoxin reductase (EC:1.8.1.9) reduces oxidised thioredoxin in the presence of NADPH. Reduced thioredoxin serves as an electron donor for thioredoxin peroxidase which consequently reduces H2O2 to H2O. In mammals, extracellular forms of Trx also have cytokine-like effects. Mammalian TrxR has a highly reactive active site selenocysteine residue resulting in a profound reductive capacity, reducing several substrates in addition to Trx [1].

Structural linksHelp
SCOP: c.3.1.5
CATH: 3.50.50.60
Database linksHelp
Enzyme: EC:1.8.1.9

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR005982 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P0A9P4 Thioredoxin reductase

P29509 Thioredoxin reductase 1

P43496 Thioredoxin reductase

Q39243 Thioredoxin reductase 1

Q58931 Putative thioredoxin reductase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR008255 Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
IPR000103 Pyridine nucleotide-disulphide oxidoreductase, class-II
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
IPR001327 Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR005982 Thioredoxin reductase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Nordberg J, Arner ES.
Reactive oxygen species, antioxidants, and the mammalian thioredoxin system.
Free Radic. Biol. Med. 31 1287-312 2001 [PubMed: 11728801]
http://dx.doi.org/10.1016/S0891-5849(01)00724-9

Additional ReadingHelp
Lennon BW, Williams CH Jr, Ludwig ML.
Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase.
Science 289 2000 1190-4 [PubMed: 10947986]
http://dx.doi.org/10.1126/science.289.5482.1190
Gustafsson TN, Sandalova T, Lu J, Holmgren A, Schneider G.
High-resolution structures of oxidized and reduced thioredoxin reductase from Helicobacter pylori.
Acta Crystallogr. D Biol. Crystallogr. 63 2007 833-43 [PubMed: 17582174]
http://dx.doi.org/10.1107/S0907444907026303
Dai S, Saarinen M, Ramaswamy S, Meyer Y, Jacquot JP, Eklund H.
Crystal structure of Arabidopsis thaliana NADPH dependent thioredoxin reductase at 2.5 A resolution.
J. Mol. Biol. 264 1996 1044-57 [PubMed: 9000629]
http://dx.doi.org/10.1006/jmbi.1996.0695
Akif M, Suhre K, Verma C, Mande SC.
Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis.
Acta Crystallogr. D Biol. Crystallogr. 61 2005 1603-11 [PubMed: 16301794]
http://dx.doi.org/10.1107/S0907444905030519
Lennon BW, Williams CH Jr, Ludwig ML.
Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor.
Protein Sci. 8 1999 2366-79 [PubMed: 10595539]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=10595539&action=stream&blobtype=pdf
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InterPro 23.1