| IED ID | IndEnz0018000456 |
| Enzyme Type ID | peroxidase000456 |
| Protein Name |
Glutathione S-transferase kappa 1 EC 2.5.1.18 GST 13-13 GST class-kappa GSTK1-1 rGSTK1 Glutathione S-transferase subunit 13 |
| Gene Name | Gstk1 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MGPAPRVLELFYDVLSPYSWLGFEVLCRYQHLWNIKLKLRPALLAGIMKDSGNQPPAMVPHKGQYILKEIPLLKQLFQVPMSVPKDFFGEHVKKGTVNAMRFLTAVSMEQPEMLEKVSRELWMRIWSRDEDITESQNILSAAEKAGMATAQAQHLLNKISTELVKSKLRETTGAACKYGAFGLPTTVAHVDGKTYMLFGSDRMELLAYLLGEKWMGPVPPTLNARL |
| Enzyme Length | 226 |
| Uniprot Accession Number | P24473 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | BINDING 53; /note=Glutathione; /evidence=ECO:0000269|PubMed:14717589; BINDING 183; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:14717589 |
| Calcium Binding | |
| catalytic Activity | 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:14717589}; |
| DNA Binding | |
| EC Number | 2.5.1.18 |
| Enzyme Function | FUNCTION: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds. {ECO:0000269|PubMed:14717589}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (4); Binding site (2); Chain (1); Helix (11); Initiator methionine (1); Modified residue (20); Mutagenesis (1); Region (2); Sequence conflict (1); Turn (3) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Mitochondrion;Reference proteome;Transferase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:1883325}. |
| Modified Residue | MOD_RES 36; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 49; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 68; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 68; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 74; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 74; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 85; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 93; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 93; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 116; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 116; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 144; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 158; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 158; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 165; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 167; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 167; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 177; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 177; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 193; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1R4W; |
| Mapped Pubmed ID | 14561759; 19935650; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,493 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:16437 |
| Cross Reference Brenda |