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InterPro: IPR005982 Thioredoxin reductase
Protein matches
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UniProtKB Matches: 1804 proteins |
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Accession
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IPR005982 Thioredox_Rdtase |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR000103 Pyridine nucleotide-disulphide oxidoreductase, class-II
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Contains
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IPR001327 Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
IPR008255 Pyridine nucleotide-disulphide oxidoreductase, class-II, active site
IPR013027 FAD-dependent pyridine nucleotide-disulphide oxidoreductase
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GO Term annotation
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Process
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GO:0019430 removal of superoxide radicals
GO:0055114 oxidation reduction
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Function
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GO:0004791 thioredoxin-disulfide reductase activity
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Component
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GO:0005737 cytoplasm
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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].
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Structural links
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Database links
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Additional Reading
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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
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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
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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
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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
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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
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