| IED ID | IndEnz0018001618 |
| Enzyme Type ID | peroxidase001618 |
| Protein Name |
Thioredoxin-2 Thioredoxin II TR-II Thioredoxin-1 |
| Gene Name | TRX2 TRX1 YGR209C G7746 |
| 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 | MVTQLKSASEYDSALASGDKLVVVDFFATWCGPCKMIAPMIEKFAEQYSDAAFYKLDVDEVSDVAQKAEVSSMPTLIFYKGGKEVTRVVGANPAAIKQAIASNV |
| Enzyme Length | 104 |
| Uniprot Accession Number | P22803 |
| Absorption | |
| Active Site | ACT_SITE 31; /note=Nucleophile; ACT_SITE 34; /note=Nucleophile |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress. {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:11013218, ECO:0000269|PubMed:12410842, ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:12914955, ECO:0000269|PubMed:3060034, ECO:0000269|PubMed:9015301, ECO:0000269|PubMed:9657146, ECO:0000269|PubMed:9988687}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (5); Chain (1); Cross-link (2); Disulfide bond (1); Domain (1); Helix (4); Initiator methionine (1); Modified residue (1); Site (3); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;Deoxyribonucleotide synthesis;Direct protein sequencing;Disulfide bond;Electron transport;Golgi apparatus;Isopeptide bond;Membrane;Nucleus;Phosphoprotein;Protein transport;Redox-active center;Reference proteome;Transport;Ubl conjugation |
| Interact With | |
| Induction | INDUCTION: Strongly induced by hydrogen peroxide and diamide stress in a YAP1- and SKN7-dependent manner. Also induced by reducing stress by DTT. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" |
| Post Translational Modification | PTM: Reversible disulfide bond formation between Cys-31 and Cys-34, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4); NMR spectroscopy (1) |
| Cross Reference PDB | 2FA4; 2HSY; 3PIN; 4DSS; 7BVV; |
| Mapped Pubmed ID | 10037727; 10347154; 10497208; 10978547; 11078740; 11145102; 11283351; 11679167; 11805837; 11823419; 11889030; 11929546; 12702279; 14593506; 14616057; 14660704; 14690591; 14718172; 15032872; 15575969; 15701801; 16173060; 16209540; 16219769; 16272220; 16299179; 16507144; 16554755; 16574642; 16609834; 16862604; 17098852; 17253982; 17340205; 17349928; 17390130; 17659286; 18021067; 18039473; 18084898; 18435761; 18629168; 18719252; 18795957; 18987790; 19054132; 19424433; 19536198; 19581440; 19681600; 19930686; 19951944; 20074363; 20152017; 20235561; 20370606; 20726779; 20846146; 20958246; 20959147; 21115478; 21179020; 21326836; 21345799; 21549177; 21734149; 21763276; 21931558; 21933953; 22094416; 22209905; 22223102; 22230188; 22311637; 22474296; 22525247; 22842922; 22867795; 22878414; 22970195; 23007444; 23198979; 23202731; 23242256; 23414292; 23416294; 23874186; 23945562; 24376832; 24376860; 24376879; 24396728; 24410772; 25172136; 25247923; 25483965; 25640729; 26264138; 26626369; 2663070; 2668278; 26898146; 26923386; 27708136; 27766356; 27864171; 32531362; 34530076; 7929110; 8313910; 8603912; 8820636; 8910528; 9118942; 9159115; 9202020; 9382859; 9813082; |
| Motif | |
| Gene Encoded By | |
| Mass | 11,204 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |