| IED ID | IndEnz0018001502 |
| Enzyme Type ID | peroxidase001502 |
| Protein Name |
Thioredoxin reductase 1 TR TrxR EC 1.8.1.9 Thioredoxin peroxidase 1 TPx Thioredoxin-dependent peroxide reductase 1 |
| Gene Name | TRR1 YDR353W D9476.5 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MVHNKVTIIGSGPAAHTAAIYLARAEIKPILYEGMMANGIAAGGQLTTTTEIENFPGFPDGLTGSELMDRMREQSTKFGTEIITETVSKVDLSSKPFKLWTEFNEDAEPVTTDAIILATGASAKRMHLPGEETYWQKGISACAVCDGAVPIFRNKPLAVIGGGDSACEEAQFLTKYGSKVFMLVRKDHLRASTIMQKRAEKNEKIEILYNTVALEAKGDGKLLNALRIKNTKKNEETDLPVSGLFYAIGHTPATKIVAGQVDTDEAGYIKTVPGSSLTSVPGFFAAGDVQDSKYRQAITSAGSGCMAALDAEKYLTSLE |
| Enzyme Length | 319 |
| Uniprot Accession Number | P29509 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 45; /note="FAD; via amide nitrogen"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; BINDING 54; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; BINDING 87; /note="FAD; via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; BINDING 145; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; BINDING 288; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561" |
| 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:7961686};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20346; Evidence={ECO:0000269|PubMed:7961686}; |
| DNA Binding | |
| EC Number | 1.8.1.9 |
| Enzyme Function | FUNCTION: Central component in the thioredoxin system. Reduces thioredoxins 1 and 2. {ECO:0000269|PubMed:20235561, ECO:0000269|PubMed:7961686}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 11..14; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; NP_BIND 40..41; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561"; NP_BIND 295..297; /note="FAD"; /evidence="ECO:0000269|PubMed:18930846, ECO:0000269|PubMed:20235561" |
| Features | Beta strand (21); Binding site (5); Chain (1); Disulfide bond (1); Helix (11); Initiator methionine (1); Modified residue (1); Nucleotide binding (3); Sequence conflict (4); Turn (4) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Mitochondrion;NADP;Oxidoreductase;Phosphoprotein;Redox-active center;Reference proteome |
| Interact With | P53879; P38816 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}. |
| Modified Residue | MOD_RES 303; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:18407956 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3D8X; 3ITJ; |
| Mapped Pubmed ID | 10037727; 10347154; 10397262; 10801893; 10930459; 11013218; 11018134; 11145102; 11169096; 11169101; 11283351; 11679167; 11805837; 12376468; 12410842; 12612609; 12668662; 12702279; 14616057; 15051715; 15701801; 16087409; 16173060; 16272220; 16328372; 16418165; 16429126; 16507144; 16554755; 16862604; 17253982; 17352532; 17659286; 18039473; 18216266; 18271751; 18406344; 18719252; 18795957; 19424433; 19536198; 19581440; 19622355; 19681600; 19951944; 20370606; 20485559; 20698499; 20726779; 20934449; 21478822; 21549177; 21931558; 22094416; 22209905; 22842922; 22970195; 22985967; 23198979; 23390587; 23414292; 24022485; 24373875; 24376879; 24410772; 24784154; 25109985; 25247923; 25483965; 26484664; 26990313; 29871930; 9202020; 9488661; 9571241; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,238 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:20345; RHEA:20346 |
| Cross Reference Brenda | 1.8.1.9; |