ID   GST2_CAEEL              Reviewed;         188 AA.
AC   O16115; Q21356;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Glutathione S-transferase 2;
DE            EC=2.5.1.18;
DE   AltName: Full=CeGST2;
DE   AltName: Full=GST class-sigma;
GN   Name=gst-2; ORFNames=K08F4.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Bristol N2;
RA   Tawe W.N., Eschbach M.-L., Walter R.D., Henkle-Duehrsen K.;
RT   "Paraquat mediates differential gene expression in C. elegans.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000250|UniProtKB:P46436}.
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         Evidence={ECO:0000250|UniProtKB:P46436};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; AF010240; AAB65418.1; -; mRNA.
DR   EMBL; Z68879; CAA93087.2; -; Genomic_DNA.
DR   PIR; T23484; T23484.
DR   PIR; T37463; T37463.
DR   RefSeq; NP_501847.1; NM_069446.3.
DR   AlphaFoldDB; O16115; -.
DR   SMR; O16115; -.
DR   STRING; 6239.K08F4.6; -.
DR   PaxDb; O16115; -.
DR   EnsemblMetazoa; K08F4.6.1; K08F4.6.1; WBGene00001750.
DR   EnsemblMetazoa; K08F4.6.2; K08F4.6.2; WBGene00001750.
DR   GeneID; 177884; -.
DR   KEGG; cel:CELE_K08F4.6; -.
DR   UCSC; K08F4.6; c. elegans.
DR   CTD; 177884; -.
DR   WormBase; K08F4.6; CE25051; WBGene00001750; gst-2.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00970000196017; -.
DR   HOGENOM; CLU_039475_1_0_1; -.
DR   InParanoid; O16115; -.
DR   OMA; ADINTYC; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; O16115; -.
DR   PRO; PR:O16115; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..188
FT                   /note="Glutathione S-transferase 2"
FT                   /id="PRO_0000185925"
FT   DOMAIN          2..79
FT                   /note="GST N-terminal"
FT   DOMAIN          81..188
FT                   /note="GST C-terminal"
FT   BINDING         43
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P46088"
FT   BINDING         49..51
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         63..64
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
SQ   SEQUENCE   188 AA;  21848 MW;  06B095CC022C7CED CRC64;
     MVHYKLMCFD VRGLGEVIRQ LFYLGDVSFE DFRVSREEFK SLKSNLPSGQ LPVLEIDGVM
     ISQSASIGRF LARQYGYSGK TPTEEMQVDS IIDLFKDFML TFRQFFFAVI HGYPEYEKER
     MKRDIVKPAI KNYFIALNKI LLRSKSGFLV GDDLTWADLQ IADNLSTLIN IRLFAEKEPH
     LNVFIRKL