Detail Information for IndEnz0018001328
IED ID IndEnz0018001328
Enzyme Type ID peroxidase001328
Protein Name Thioredoxin-1
Thioredoxin I
TR-I
Thioredoxin-2
Gene Name TRX1 TRX2 YLR043C
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 MVTQFKTASEFDSAIAQDKLVVVDFYATWCGPCKMIAPMIEKFSEQYPQADFYKLDVDELGDVAQKNEVSAMPTLLLFKNGKEVAKVVGANPAAIKQAIAANA
Enzyme Length 103
Uniprot Accession Number P22217
Absorption
Active Site ACT_SITE 30; /note=Nucleophile; ACT_SITE 33; /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. {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:12410842, ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:3060034, ECO:0000269|PubMed:8603912, 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 (6); Chain (1); Cross-link (3); Disulfide bond (1); Domain (1); Helix (4); Initiator methionine (1); Site (3); Turn (1)
Keywords 3D-structure;Cytoplasm;Deoxyribonucleotide synthesis;Direct protein sequencing;Disulfide bond;Electron transport;Golgi apparatus;Isopeptide bond;Membrane;Mitochondrion;Nucleus;Protein transport;Redox-active center;Reference proteome;Transport;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8603912}. Golgi apparatus membrane {ECO:0000269|PubMed:22984289}; Peripheral membrane protein {ECO:0000255}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Modified Residue
Post Translational Modification PTM: Reversible disulfide bond formation between Cys-30 and Cys-33, reverted by thioredoxin reductase TRR1 using NADPH as hydrogen donor.
Signal Peptide
Structure 3D X-ray crystallography (2); NMR spectroscopy (3)
Cross Reference PDB 2I9H; 2N5A; 2N5B; 3F3Q; 3F3R;
Mapped Pubmed ID 10037727; 10497208; 10978547; 11679167; 11823419; 11889030; 11929546; 12840001; 14593506; 14690591; 15032872; 15701801; 16173060; 16272220; 16299179; 16429126; 16554755; 16574642; 16609834; 17082750; 17098852; 17349928; 17390130; 17659286; 18021067; 18039473; 18245329; 18391437; 18629168; 19054132; 19153453; 19424433; 19581440; 19681600; 19801666; 19930686; 19951944; 20062004; 20074363; 20235561; 20698499; 21549177; 21763276; 22094416; 22209905; 22412017; 22842922; 22867795; 22878414; 22970195; 22985967; 23198979; 23874186; 23945562; 23983899; 24376879; 24396728; 24410772; 25109985; 25172136; 25247923; 25483965; 25640729; 25830254; 26482062; 2663070; 2668278; 26898146; 26916166; 26923386; 27576599; 27708136; 31877266; 7733663; 7929110; 8820636; 8910528; 9159115; 9202020; 9382859; 9813082;
Motif
Gene Encoded By
Mass 11,235
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda