| IED ID | IndEnz0018001481 |
| Enzyme Type ID | peroxidase001481 |
| Protein Name |
Thioredoxin reductase 1, cytoplasmic TR EC 1.8.1.9 Peroxidase TXNRD1 EC 1.11.1.2 Thioredoxin reductase TR1 |
| Gene Name | Txnrd1 Trxr1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPVDDCWLYFPASRGRTFVQTVWVAPTCPNCCWFPGFLPPVPRPPHVPRVLLRGPRGAVLPASRPSKTLPSSSQTPCPTDPCICPPPSTPDSRQEKNTQSELPNKKGQLQKLPTMNGSKDPPGSYDFDLIIIGGGSGGLAAAKEAAKFDKKVLVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLRVTAQSTNSEETIEGEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRDNNKCYAKIICNLKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTLSVTKRSGGDILQSGCUG |
| Enzyme Length | 613 |
| Uniprot Accession Number | Q9JMH6 |
| Absorption | |
| Active Site | ACT_SITE 586; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 275; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 280; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 314; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 340; /note=NADP; /evidence=ECO:0000250|UniProtKB:O89049; BINDING 429; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 448; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 455; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; BINDING 586; /note=FAD; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q16881 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000250|UniProtKB:Q16881};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347; Evidence={ECO:0000250|UniProtKB:Q16881}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2; Evidence={ECO:0000250|UniProtKB:Q16881};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174; Evidence={ECO:0000250|UniProtKB:Q16881}; |
| DNA Binding | |
| EC Number | 1.8.1.9; 1.11.1.2 |
| Enzyme Function | FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2). {ECO:0000250|UniProtKB:Q16881}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 136..137; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 156..157; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 172..173; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 177..181; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 245..246; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 312..318; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 335..336; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 340..342; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 406..407; /note=NADP; /evidence=ECO:0000250|UniProtKB:Q16881; NP_BIND 455..457; /note=FAD; /evidence=ECO:0000250|UniProtKB:Q16881 |
| Features | Active site (1); Alternative sequence (1); Binding site (8); Chain (1); Compositional bias (1); Cross-link (1); Disulfide bond (1); Erroneous termination (3); Modified residue (2); Non-standard residue (1); Nucleotide binding (10); Region (1); Sequence conflict (3) |
| Keywords | Alternative splicing;Cytoplasm;Disulfide bond;FAD;Flavoprotein;NADP;Oxidoreductase;Phosphoprotein;Redox-active center;Reference proteome;Selenocysteine;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10721726}. |
| Modified Residue | MOD_RES 182; /note=N6-succinyllysine; /evidence=ECO:0007744|PubMed:23806337; MOD_RES 245; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:15592455 |
| Post Translational Modification | PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10455115; 10512203; 10769168; 11217851; 11259642; 12466851; 12904583; 14610273; 14681479; 15703188; 15713651; 15831471; 15840001; 15901730; 16615898; 17697936; 17901053; 17937623; 17971875; 18350150; 18614015; 18799693; 19244202; 19319191; 19433132; 19466610; 19584930; 19820694; 20018845; 20463017; 20536427; 20571049; 21045148; 21267068; 21554947; 21943784; 22198266; 22348009; 22594686; 22791808; 23364477; 23604909; 23732520; 23743293; 23865454; 23901112; 24039713; 24295151; 24434121; 24608031; 24624337; 25753394; 25790857; 25886253; 27089175; 27262435; 27346647; 27689697; 28218609; 28442342; 28658624; 28686716; 28775321; 29749372; 30802940; 30805084; 30894323; 31097586; 31911946; 32096759; 33171211; 33230666; 33254076; 35031135; |
| Motif | |
| Gene Encoded By | |
| Mass | 67,084 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:20345; RHEA:20347; RHEA:15173; RHEA:15174 |
| Cross Reference Brenda | 1.8.1.9; |