Detail Information for IndEnz0018000964
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