IED ID | IndEnz0018000964 |
Enzyme Type ID | peroxidase000964 |
Protein Name |
Glutathione S-transferase kappa 1 EC 2.5.1.18 GST 13-13 GST class-kappa GSTK1-1 hGSTK1 Glutathione S-transferase subunit 13 |
Gene Name | GSTK1 HDCMD47P |
Organism | Homo sapiens (Human) |
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
Enzyme Sequence | MGPLPRTVELFYDVLSPYSWLGFEILCRYQNIWNINLQLRPSLITGIMKDSGNKPPGLLPRKGLYMANDLKLLRHHLQIPIHFPKDFLSVMLEKGSLSAMRFLTAVNLEHPEMLEKASRELWMRVWSRNEDITEPQSILAAAEKAGMSAEQAQGLLEKIATPKVKNQLKETTEAACRYGAFGLPITVAHVDGQTHMLFGSDRMELLAHLLGEKWMGPIPPAVNARL |
Enzyme Length | 226 |
Uniprot Accession Number | Q9Y2Q3 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | BINDING 53; /note=Glutathione; /evidence=ECO:0000269|PubMed:16081649; BINDING 183; /note=Glutathione; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000269|PubMed:16081649 |
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:14709161, ECO:0000269|PubMed:14742434}; |
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 (PubMed:14709161, PubMed:14742434). Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB) (PubMed:14709161). {ECO:0000269|PubMed:14709161, ECO:0000269|PubMed:14742434}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Alternative sequence (3); Beta strand (6); Binding site (2); Chain (1); Helix (11); Modified residue (10); Region (2); Sequence conflict (5); Turn (2) |
Keywords | 3D-structure;Acetylation;Alternative splicing;Peroxisome;Reference proteome;Transferase |
Interact With | O95273; Q8IZU0; Q60994; Q7Z3Y8 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:14742434}. |
Modified Residue | MOD_RES 49; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:Q9DCM2; MOD_RES 71; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 85; /note=N6-acetyllysine; /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 169; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1YZX; 3RPN; 3RPP; |
Mapped Pubmed ID | 10022913; 11101887; 12456682; 12559034; 12578380; 12885776; 17007944; 17353931; 17601350; 18624398; 18712838; 18774560; 18977241; 19197237; 19225211; 19584060; 19632994; 19639233; 19738201; 20178365; 20472488; 21728995; 21976670; 21988832; 22002062; 22583869; 22623428; 22747494; 23330092; 23426619; 23963456; 24235149; 25416956; 25739441; 25854684; 26058080; 26220973; 26638075; 27010189; 27044684; 27377684; 28287017; 28765278; 28787099; 29099786; 29569850; 30606929; 30791996; 31502701; 32167139; 32249844; 32948751; 33538302; 33843164; 7719337; 7790377; 8824437; 8858165; 9653144; 9668159; 9837948; |
Motif | |
Gene Encoded By | |
Mass | 25,497 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:16437 |
Cross Reference Brenda |