ID   GSTK2_CAEEL             Reviewed;         225 AA.
AC   Q18973;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Glutathione s-transferase kappa 2;
DE            EC=2.5.1.18;
GN   Name=gstk-2; ORFNames=D2024.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19663909; DOI=10.1111/j.1742-4658.2009.07200.x;
RA   Petit E., Michelet X., Rauch C., Bertrand-Michel J., Terce F., Legouis R.,
RA   Morel F.;
RT   "Glutathione transferases kappa 1 and kappa 2 localize in peroxisomes and
RT   mitochondria, respectively, and are involved in lipid metabolism and
RT   respiration in Caenorhabditis elegans.";
RL   FEBS J. 276:5030-5040(2009).
CC   -!- FUNCTION: Has roles in respiratory and lipid metabolism.
CC       {ECO:0000269|PubMed:19663909}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19663909}.
CC   -!- TISSUE SPECIFICITY: Expressed in the pharynx, body wall muscles and
CC       epidermis. Weaker expression is seen in the intestine.
CC       {ECO:0000269|PubMed:19663909}.
CC   -!- DISRUPTION PHENOTYPE: Significant decrease in respiration rate and a
CC       lower concentration of the monounsaturated fatty acid cis-vaccenic
CC       acid. {ECO:0000269|PubMed:19663909}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Kappa family.
CC       {ECO:0000305}.
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DR   EMBL; FO080386; CCD63360.1; -; Genomic_DNA.
DR   PIR; T34201; T34201.
DR   RefSeq; NP_501148.1; NM_068747.4.
DR   AlphaFoldDB; Q18973; -.
DR   SMR; Q18973; -.
DR   BioGRID; 42617; 13.
DR   STRING; 6239.D2024.7.1; -.
DR   EPD; Q18973; -.
DR   PaxDb; Q18973; -.
DR   PeptideAtlas; Q18973; -.
DR   EnsemblMetazoa; D2024.7.1; D2024.7.1; WBGene00017054.
DR   EnsemblMetazoa; D2024.7.2; D2024.7.2; WBGene00017054.
DR   GeneID; 177498; -.
DR   KEGG; cel:CELE_D2024.7; -.
DR   CTD; 177498; -.
DR   WormBase; D2024.7; CE04296; WBGene00017054; gstk-2.
DR   eggNOG; ENOG502R0HS; Eukaryota.
DR   GeneTree; ENSGT00440000033697; -.
DR   HOGENOM; CLU_069253_1_1_1; -.
DR   InParanoid; Q18973; -.
DR   OMA; AFHNIQP; -.
DR   OrthoDB; 1320977at2759; -.
DR   PhylomeDB; Q18973; -.
DR   Reactome; R-CEL-156590; Glutathione conjugation.
DR   Reactome; R-CEL-9033241; Peroxisomal protein import.
DR   PRO; PR:Q18973; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00017054; Expressed in larva and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   CDD; cd03021; DsbA_GSTK; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR044088; GSTK.
DR   InterPro; IPR014440; HCCAis_GSTk.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Reference proteome; Transferase.
FT   CHAIN           1..225
FT                   /note="Glutathione s-transferase kappa 2"
FT                   /id="PRO_0000185894"
FT   BINDING         15..17
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..201
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   225 AA;  25951 MW;  23D0A3D6762B7232 CRC64;
     MPNRKVVKFF FDVISPYSYF GFEGITRHRS VWKTPIQMKP FFFAGVVRHT ENPGLPLRIP
     IKEKYMHKDL LFSAQYWGIP FRLPKDYTNM MLNTSSIVPQ RILVASQLRD NVLMEDVARG
     LWHRFYAYGK PIFTKSQVAE VLRDLHVKDV DELVMMSDSA EVKNILRENT DEAIGNGCFG
     APWMHITDGH GKVLQTVFGS DRLPQVADFL AEPFKGPMRE KKPNA