GST8_CAEEL
ID GST8_CAEEL Reviewed; 206 AA.
AC P91254;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable glutathione S-transferase 8;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
GN Name=gst-8; ORFNames=F11G11.1;
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; CCD69254.1; -; Genomic_DNA.
DR PIR; T29986; T29986.
DR RefSeq; NP_494884.1; NM_062483.1.
DR AlphaFoldDB; P91254; -.
DR SMR; P91254; -.
DR STRING; 6239.F11G11.1; -.
DR World-2DPAGE; 0020:P91254; -.
DR PaxDb; P91254; -.
DR PeptideAtlas; P91254; -.
DR EnsemblMetazoa; F11G11.1.1; F11G11.1.1; WBGene00001756.
DR GeneID; 184364; -.
DR KEGG; cel:CELE_F11G11.1; -.
DR UCSC; F11G11.1; c. elegans.
DR CTD; 184364; -.
DR WormBase; F11G11.1; CE07054; WBGene00001756; gst-8.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000196005; -.
DR HOGENOM; CLU_039475_1_1_1; -.
DR InParanoid; P91254; -.
DR OMA; IRWMFQI; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P91254; -.
DR PRO; PR:P91254; -.
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 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 8"
FT /id="PRO_0000185931"
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; 23433 MW; 53D50FE7794EA260 CRC64;
MVHYKLSYFP IRGAGEVIRQ IFVYAGQSFE DHRISIEEWA AVKPTTPFGQ LPLLEVDGKV
LPQSHSIARF LARQFGINGK CAWEEAQVNS IADQFKDYRN EVRPYVMVKM GFAEGDLDAL
SKDVFLPGFK KHYGFIYNFL KTAGSGYLVG DSLTFVDLLI AQHTADILST DPALLEEFPQ
FKAHQEKVHS NANIKKWLET RPETQF