| IED ID | IndEnz0002014699 |
| Enzyme Type ID | protease014699 |
| Protein Name |
Glutathione-independent glyoxalase HSP31 EC 4.2.1.130 Glyoxalase 3 homolog 1 Heat shock protein 31 |
| Gene Name | HSP31 YDR533C D9719.36 |
| 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 | MAPKKVLLALTSYNDVFYSDGAKTGVFVVEALHPFNTFRKEGFEVDFVSETGKFGWDEHSLAKDFLNGQDETDFKNKDSDFNKTLAKIKTPKEVNADDYQIFFASAGHGTLFDYPKAKDLQDIASEIYANGGVVAAVCHGPAIFDGLTDKKTGRPLIEGKSITGFTDVGETILGVDSILKAKNLATVEDVAKKYGAKYLAPVGPWDDYSITDGRLVTGVNPASAHSTAVRSIDALKN |
| Enzyme Length | 237 |
| Uniprot Accession Number | Q04432 |
| Absorption | |
| Active Site | ACT_SITE 138; /evidence="ECO:0000305|PubMed:14745011, ECO:0000305|PubMed:15130476"; ACT_SITE 139; /evidence="ECO:0000305|PubMed:14745011, ECO:0000305|PubMed:15130476"; ACT_SITE 170; /evidence="ECO:0000305|PubMed:14745011, ECO:0000305|PubMed:15130476" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + methylglyoxal = (R)-lactate + H(+); Xref=Rhea:RHEA:27754, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:17158; EC=4.2.1.130; Evidence={ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24758716}; |
| DNA Binding | |
| EC Number | 4.2.1.130 |
| Enzyme Function | FUNCTION: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals (PubMed:24302734). Involved in protection against reactive oxygen species (ROS) (PubMed:17395014). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed:24706893). {ECO:0000269|PubMed:17395014, ECO:0000269|PubMed:24302734, ECO:0000269|PubMed:24706893}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (8); Chain (1); Helix (15); Modified residue (1); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Cytoplasm;Lyase;Oxidation;Reference proteome;Stress response |
| Interact With | |
| Induction | INDUCTION: Up-regulated 10- to 30-fold during entry into stationary phase, by hydrogen peroxide or diamide stress, by heat stress, and by growth in the presence of the proline analog azetidine-2-carboxylic acid. {ECO:0000269|PubMed:17395014, ECO:0000269|PubMed:24706893}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:24706893}. Note=Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock. {ECO:0000269|PubMed:24706893}. |
| Modified Residue | MOD_RES 138; /note=Cysteine sulfinic acid (-SO2H); /evidence=ECO:0000269|PubMed:14745011 |
| Post Translational Modification | PTM: Cys-138 is easily oxidized to sulfinic acid. {ECO:0000269|PubMed:14745011}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1QVV; 1QVW; 1QVZ; 4QYX; |
| Mapped Pubmed ID | 11283351; 15766533; 16328372; 16489413; 16554755; 17257049; 17651441; 17847089; 19536198; 21267445; 22842922; 23226681; 23420633; 24070869; 25058424; 26306045; 26370081; 26466368; 26777405; 27097320; 27690738; 27984092; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,670 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for methylglyoxal {ECO:0000269|PubMed:24758716}; Note=kcat is 75.0 min(-1) with methylglyoxal as substrate. {ECO:0000269|PubMed:24758716}; |
| Metal Binding | |
| Rhea ID | RHEA:27754 |
| Cross Reference Brenda | 4.2.1.130; |