| IED ID | IndEnz0018001129 |
| Enzyme Type ID | peroxidase001129 |
| Protein Name |
Glutaredoxin-2 EC 1.11.1.9 EC 2.5.1.18 Glutathione-dependent oxidoreductase 2 Thioltransferase |
| Gene Name | GRX2 TTR TTR1 YDR513W D9719.17 |
| 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 | METNFSFDSNLIVIIIITLFATRIIAKRFLSTPKMVSQETVAHVKDLIGQKEVFVAAKTYCPYCKATLSTLFQELNVPKSKALVLELDEMSNGSEIQDALEEISGQKTVPNVYINGKHIGGNSDLETLKKNGKLAEILKPVFQ |
| Enzyme Length | 143 |
| Uniprot Accession Number | P17695 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 109; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:18992757 |
| 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. GRX2 is more active as an oxidoreductase than GRX1 (PubMed:9571241, PubMed:18992757, PubMed:20417731). Responsible for the S-glutathionylation of DHBP synthase (PubMed:21565288). {ECO:0000269|PubMed:11875065, ECO:0000269|PubMed:12684511, ECO:0000269|PubMed:18992757, ECO:0000269|PubMed:20417731, ECO:0000269|PubMed:21565288, ECO:0000269|PubMed:9571241}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (4); Binding site (1); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Helix (7); Initiator methionine (1); Modified residue (3); Mutagenesis (4); Region (2); Transit peptide (1); Turn (1) |
| Keywords | 3D-structure;Alternative initiation;Cytoplasm;Direct protein sequencing;Disulfide bond;Electron transport;Glutathionylation;Mitochondrion;Oxidoreductase;Phosphoprotein;Redox-active center;Reference proteome;Transferase;Transit peptide;Transport |
| Interact With | |
| Induction | INDUCTION: In response to exposure to reactive oxygen species (ROS) and upon entry into stationary phase. {ECO:0000269|PubMed:10786615, ECO:0000269|PubMed:9571241}. |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:11958675, ECO:0000269|PubMed:16606613}. |
| Modified Residue | MOD_RES 37; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956"; MOD_RES 61; /note="S-glutathionyl cysteine; alternate"; /evidence="ECO:0000269|PubMed:18992757"; MOD_RES 91; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3CTF; 3CTG; 3D4M; 3D5J; |
| Mapped Pubmed ID | 10497208; 10567543; 10844700; 11013218; 11018134; 11169096; 11283351; 11679167; 11929546; 12135599; 12839777; 15032872; 15038548; 15277542; 16880213; 16915356; 17576017; 17659286; 17996374; 18021067; 18039473; 18435761; 18719252; 19166312; 19424433; 19536198; 19930686; 19951944; 20059400; 20074363; 20522499; 20698499; 20707985; 21235502; 21385868; 21734149; 21931558; 21933953; 22094416; 22209905; 22326886; 22389629; 22583368; 22928493; 22970195; 23198979; 23242256; 23970950; 24396728; 24410772; 24611845; 25109985; 25247923; 25392302; 25640729; 27085841; 27530428; 27693354; 29790350; |
| Motif | |
| Gene Encoded By | |
| Mass | 15,861 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.0 mM for H(2)O(2) {ECO:0000269|PubMed:12684511}; KM=2.2 mM for tert-butyl hydroperoxide {ECO:0000269|PubMed:12684511}; KM=0.87 mM for cumene hydroperoxide {ECO:0000269|PubMed:12684511}; KM=0.17 mM for 1-chloro-2,4-dinitrobenzene {ECO:0000269|PubMed:12684511}; KM=0.27 mM for 1,2-dichloro-4-nitrobenzene {ECO:0000269|PubMed:12684511}; KM=0.9 mM for reduced glutathione {ECO:0000269|PubMed:18992757}; |
| Metal Binding | |
| Rhea ID | RHEA:16833; RHEA:51220; RHEA:16437 |
| Cross Reference Brenda |