ID   GST7_CAEEL              Reviewed;         206 AA.
AC   P91253;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Probable glutathione S-transferase 7;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
GN   Name=gst-7; ORFNames=F11G11.2;
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.
RX   PubMed=22216003; DOI=10.1371/journal.ppat.1002453;
RA   Hoeven R.V., McCallum K.C., Cruz M.R., Garsin D.A.;
RT   "Ce-Duox1/BLI-3 generated reactive oxygen species trigger protective SKN-1
RT   activity via p38 MAPK signaling during infection in C. elegans.";
RL   PLoS Pathog. 7:E1002453-E1002453(2011).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles (By similarity). May
CC       play a role in the detoxification of reactive oxygen species produced
CC       during pathogenic bacterial infection (PubMed:22216003).
CC       {ECO:0000250|UniProtKB:P46436, ECO:0000269|PubMed:22216003}.
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; FO081119; CCD69255.1; -; Genomic_DNA.
DR   PIR; T29985; T29985.
DR   RefSeq; NP_494883.1; NM_062482.4.
DR   AlphaFoldDB; P91253; -.
DR   SMR; P91253; -.
DR   BioGRID; 39196; 49.
DR   DIP; DIP-24504N; -.
DR   IntAct; P91253; 1.
DR   STRING; 6239.F11G11.2; -.
DR   EPD; P91253; -.
DR   PaxDb; P91253; -.
DR   PeptideAtlas; P91253; -.
DR   EnsemblMetazoa; F11G11.2.1; F11G11.2.1; WBGene00001755.
DR   GeneID; 173842; -.
DR   KEGG; cel:CELE_F11G11.2; -.
DR   UCSC; F11G11.2; c. elegans.
DR   CTD; 173842; -.
DR   WormBase; F11G11.2; CE07055; WBGene00001755; gst-7.
DR   eggNOG; KOG1695; Eukaryota.
DR   GeneTree; ENSGT00970000196005; -.
DR   HOGENOM; CLU_039475_1_1_1; -.
DR   InParanoid; P91253; -.
DR   OMA; EDNRIPK; -.
DR   OrthoDB; 1162336at2759; -.
DR   PhylomeDB; P91253; -.
DR   PRO; PR:P91253; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; HEP:WormBase.
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   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..206
FT                   /note="Probable glutathione S-transferase 7"
FT                   /id="PRO_0000185930"
FT   DOMAIN          2..79
FT                   /note="GST N-terminal"
FT   DOMAIN          81..206
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
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   206 AA;  23085 MW;  0F72B5425295934E CRC64;
     MVHYKVSYFP IRGAGEIARQ ILAYAGQDFE DNRIPKEEWP AVKPSTPFGQ LPLLEVDGKV
     LAQSHAIARY LARQFGINGK CAWEEAQVNS VADQFKDYLN EVRPYFMVKM GFAEGDLDAL
     AKDVFLPGFK KHYGFFANFL KSAGSGYLVG DSLTFVDLLV AQHTADLLAA NAALLDEFPQ
     FKAHQEKVHS NANIKKWLET RPVTPF