GST6_CAEEL
ID GST6_CAEEL Reviewed; 206 AA.
AC P91252;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable glutathione S-transferase 6;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
GN Name=gst-6; ORFNames=F11G11.3;
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).
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; FO081119; CCD69256.1; -; Genomic_DNA.
DR PIR; T29984; T29984.
DR RefSeq; NP_494882.2; NM_062481.7.
DR AlphaFoldDB; P91252; -.
DR SMR; P91252; -.
DR BioGRID; 39195; 9.
DR STRING; 6239.F11G11.3; -.
DR EPD; P91252; -.
DR PaxDb; P91252; -.
DR PeptideAtlas; P91252; -.
DR EnsemblMetazoa; F11G11.3.1; F11G11.3.1; WBGene00001754.
DR GeneID; 173841; -.
DR KEGG; cel:CELE_F11G11.3; -.
DR UCSC; F11G11.3; c. elegans.
DR CTD; 173841; -.
DR WormBase; F11G11.3; CE32622; WBGene00001754; gst-6.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000196017; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; P91252; -.
DR OMA; LLISQHV; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P91252; -.
DR PRO; PR:P91252; -.
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; 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 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 6"
FT /id="PRO_0000185929"
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; 23617 MW; 347CF944862A1571 CRC64;
MVHYKLVYFP LRARAEIARQ IFAYAGQDYS EENLSFEQWP ARKNNTPFGQ LPILEVDGKP
LGQSYAIARY LAREFGIAGQ NDTEAAEVDA IADQFKDYLN DVSPYLTVLA GFKPGDKDQL
RTDVFVPAFK KNFEFFENIL ASNHSGFFVG NSLTWVDLLI SQHVQDILDK DLAVVEEFKK
VLAHRKKVQS IDRIQKYIAN RPDYPF