IED Industry Enzyme Database

Detail Information for IndEnz0018001497
IED ID IndEnz0018001497
Enzyme Type ID peroxidase001497
Protein Name Thioredoxin reductase 1, mitochondrial
TrxR-1
EC 1.8.1.9
Gene Name Trxr-1 GR CG2151
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MNLCNSRFSVTFVRQCSTILTSPSAGIIQNRGSLTTKVPHWISSSLSCAHHTFQRTMNLTGQRGSRDSTGATGGNAPAGSGAGAPPPFQHPHCDRAAMYAQPVRKMSTKGGSYDYDLIVIGGGSAGLACAKEAVLNGARVACLDFVKPTPTLGTKWGVGGTCVNVGCIPKKLMHQASLLGEAVHEAAAYGWNVDEKIKPDWHKLVQSVQNHIKSVNWVTRVDLRDKKVEYINGLGSFVDSHTLLAKLKSGERTITAQTFVIAVGGRPRYPDIPGAVEYGITSDDLFSLDREPGKTLVVGAGYIGLECAGFLKGLGYEPTVMVRSIVLRGFDQQMAELVAASMEERGIPFLRKTVPLSVEKQDDGKLLVKYKNVETGEEAEDVYDTVLWAIGRKGLVDDLNLPNAGVTVQKDKIPVDSQEATNVANIYAVGDIIYGKPELTPVAVLAGRLLARRLYGGSTQRMDYKDVATTVFTPLEYACVGLSEEDAVKQFGADEIEVFHGYYKPTEFFIPQKSVRYCYLKAVAERHGDQRVYGLHYIGPVAGEVIQGFAAALKSGLTINTLINTVGIHPTTAEEFTRLAITKRSGLDPTPASCCS
Enzyme Length 596
Uniprot Accession Number P91938
Absorption
Active Site ACT_SITE 569; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:17385893
Activity Regulation
Binding Site BINDING 282; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; BINDING 286; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; BINDING 302; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; BINDING 355; /note=NADP; /evidence=ECO:0000269|PubMed:17385893; BINDING 472; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; BINDING 570; /note=FAD; /evidence=ECO:0000269|PubMed:17385893
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:0000269|PubMed:11158675};
DNA Binding
EC Number 1.8.1.9
Enzyme Function FUNCTION: Thioredoxin system is a major player in glutathione metabolism, due to the demonstrated absence of a glutathione reductase. Functionally interacts with the Sod/Cat reactive oxidation species (ROS) defense system and thereby has a role in preadult development and life span. Lack of a glutathione reductase suggests antioxidant defense in Drosophila, and probably in related insects, differs fundamentally from that in other organisms. {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11525742, ECO:0000269|PubMed:11796729}.
Temperature Dependency
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6 for isoform A with Trx-2 and NADPH as substrates. {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392};
Pathway
nucleotide Binding NP_BIND 120..126; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 143..147; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 159..170; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 233..235; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 262..266; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 322..328; /note=NADP; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 392..399; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 429..432; /note=FAD; /evidence=ECO:0000269|PubMed:17385893; NP_BIND 438..443; /note=FAD; /evidence=ECO:0000269|PubMed:17385893
Features Active site (1); Alternative sequence (4); Beta strand (21); Binding site (6); Chain (1); Compositional bias (1); Disulfide bond (2); Helix (18); Mutagenesis (5); Nucleotide binding (9); Region (1); Sequence caution (1); Sequence conflict (25); Transit peptide (1); Turn (4)
Keywords 3D-structure;Alternative initiation;Alternative splicing;Cytoplasm;Disulfide bond;FAD;Flavoprotein;Mitochondrion;NADP;Nucleotide-binding;Oxidoreductase;Redox-active center;Reference proteome;Transit peptide
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Isoform B]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform A]: Cytoplasm.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 2NVK; 3DGH; 3DH9;
Mapped Pubmed ID 10506576; 11013257; 11060283; 11250117; 11348656; 11744370; 12466289; 12539239; 12626737; 12743125; 12816954; 12865422; 14680800; 15120069; 15458575; 15670839; 17173140; 17194782; 17242409; 17550271; 17661444; 18042644; 18407920; 18433294; 18508973; 18931788; 18986163; 19079254; 19543366; 19761846; 20015541; 20371351; 20617381; 20618965; 20869434; 21074052; 21389620; 21987827; 22100409; 22427708; 22940110; 23071443; 23639798; 23865454; 24231732; 24393022; 24393533; 24464041; 24490974; 24599608; 25122658; 25294944; 25634895; 25687947; 25776889; 26117601; 26526100; 26859353; 26980113; 27582081; 27585844; 27687474; 28031247; 28076795; 28132818; 28474396; 28529177; 28887920; 29080449; 29259189; 29379413; 29563863; 29565247; 29575479; 30052295; 30082411; 30110626; 30818813; 31101394; 31317820; 31636947; 33083121; 33992327;
Motif
Gene Encoded By
Mass 64,322
Kinetics BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.5 uM for NADPH (at pH 7.4) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=1 uM for NADPH (at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=1 uM for NADPH (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=7.0 uM for dhd (at pH 7.4, 200 uM NADPH, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=141 uM for dhd (at pH 7.0, 0.15 mM NADPH, 1 mM EDTA, 1 mg/ml insulin, 50 mM KPO(4), 25 degrees Celsius) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=7 uM for dhd (at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=19 uM for dhd (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=5.9 uM for Trx-2 (at pH 7.4, 100 uM NADPH, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=310 uM for 5,5'-dithiobis-2-nitrobenzoic acid (DTNB) (at pH 7.4, 100 uM NADPH, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=0.17 mM for DTNB (at pH 7.0, 0.2 mM NADPH, 10 mM EDTA, 100 mM KPO(4), 25 degrees Celsius) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=380 uM for DTNB (at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=410 uM for DTNB (isoform B at pH 7.4, 2 mM EDTA, 100 mM KPO(4)) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; KM=675 uM for methylseleninate (100 uM NADPH) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; Vmax=24.3 umol/min/mg enzyme toward NADPH (at pH 7.4) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; Vmax=16 umol/min/mg enzyme toward Trx-2 (at pH 7.4, 100 uM NADPH, 2 mM EDTA, 100 mM KPO(4), 25 degrees Celsius) {ECO:0000269|PubMed:11158675, ECO:0000269|PubMed:11782468, ECO:0000269|PubMed:11796729, ECO:0000269|PubMed:11877442, ECO:0000269|PubMed:17385893, ECO:0000269|PubMed:18211101, ECO:0000269|PubMed:18991392}; Note=Measurements were conducted with isoform A unless noted otherwise.;
Metal Binding
Rhea ID RHEA:20345
Cross Reference Brenda 1.8.1.9;