| IED ID | IndEnz0018000970 |
| Enzyme Type ID | peroxidase000970 |
| Protein Name |
Glutaredoxin-1 EC 1.11.1.9 EC 2.5.1.18 Glutathione-dependent oxidoreductase 1 |
| Gene Name | GRX1 YCL035C YCL35C |
| 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 | MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN |
| Enzyme Length | 110 |
| Uniprot Accession Number | P25373 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 63; /note="Glutathione"; /evidence="ECO:0000269|PubMed:17327665, ECO:0000269|PubMed:18473363"; BINDING 75; /note="Glutathione; via amide nitrogen and carbonyl oxygen"; /evidence="ECO:0000269|PubMed:17327665, ECO:0000269|PubMed:18473363" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:11875065}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:12684511}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:12684511}; |
| DNA Binding | |
| EC Number | 1.11.1.9; 2.5.1.18 |
| Enzyme Function | FUNCTION: Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity (PubMed:11875065, PubMed:12684511). The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2 (PubMed:9571241, PubMed:18992757, PubMed:20417731). {ECO:0000269|PubMed:11875065, ECO:0000269|PubMed:12684511, ECO:0000269|PubMed:18992757, ECO:0000269|PubMed:20417731, ECO:0000269|PubMed:9571241}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Binding site (2); Chain (1); Cross-link (1); Disulfide bond (1); Domain (1); Helix (7); Modified residue (1); Mutagenesis (2); Region (2); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;Disulfide bond;Electron transport;Glutathionylation;Isopeptide bond;Nucleus;Oxidoreductase;Redox-active center;Reference proteome;Transferase;Transport;Ubl conjugation |
| Interact With | P34230 |
| Induction | INDUCTION: In response to heat shock and osmotic stress. {ECO:0000269|PubMed:10786615, ECO:0000269|PubMed:9571241}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. |
| Modified Residue | MOD_RES 27; /note="S-glutathionyl cysteine; alternate"; /evidence="ECO:0000269|PubMed:17327665, ECO:0000269|PubMed:18473363" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 2JAC; 2JAD; 3C1R; 3C1S; 6MWS; |
| Mapped Pubmed ID | 10497208; 10801893; 11013218; 11018134; 11169096; 11283351; 11679167; 11805837; 11929546; 12839777; 15032872; 15277542; 15766533; 16475825; 16915356; 16946480; 17576017; 17659286; 18021067; 18039473; 19166312; 19424433; 19515841; 19536198; 19622355; 19930686; 19951944; 19968277; 20074363; 20489023; 20522499; 20726779; 20737429; 21444828; 21933953; 22094416; 22179789; 22326886; 22842922; 22928493; 22952687; 22970195; 23198979; 24410772; 24611845; 25247923; 25640729; 29790350; 31045569; |
| Motif | |
| Gene Encoded By | |
| Mass | 12,380 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.88 mM for H(2)O(2) {ECO:0000269|PubMed:11875065}; KM=0.52 mM for cumene hydroperoxide {ECO:0000269|PubMed:11875065}; KM=0.37 mM for tert-butyl hydroperoxide {ECO:0000269|PubMed:11875065}; KM=4.2 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:12684511}; KM=1.3 mM for 1,2-dichloro-4-nitrobenzene {ECO:0000269|PubMed:12684511}; KM=6.2 mM for reduced glutathione {ECO:0000269|PubMed:18992757}; Vmax=110 umol/min/mg enzyme for H(2)O(2) {ECO:0000269|PubMed:11875065}; Vmax=32.5 umol/min/mg enzyme for cumene hydroperoxide {ECO:0000269|PubMed:11875065}; Vmax=7.5 umol/min/mg enzyme for tert-butyl hydroperoxide {ECO:0000269|PubMed:11875065}; |
| Metal Binding | |
| Rhea ID | RHEA:16833; RHEA:51220; RHEA:16437 |
| Cross Reference Brenda |