ID GST9_CAEEL Reviewed; 206 AA.
AC Q21743; Q21744;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Probable glutathione S-transferase 9;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
GN Name=gst-9; ORFNames=R05F9.5;
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; FO081120; CCD69273.1; -; Genomic_DNA.
DR PIR; T16683; T16683.
DR PIR; T16685; T16685.
DR RefSeq; NP_001022266.1; NM_001027095.1.
DR AlphaFoldDB; Q21743; -.
DR SMR; Q21743; -.
DR STRING; 6239.R05F9.5.1; -.
DR PaxDb; 6239-R05F9-5; -.
DR PeptideAtlas; Q21743; -.
DR EnsemblMetazoa; R05F9.5.1; R05F9.5.1; WBGene00001757.
DR GeneID; 187615; -.
DR KEGG; cel:CELE_R05F9.5; -.
DR UCSC; R05F9.5; c. elegans.
DR AGR; WB:WBGene00001757; -.
DR WormBase; R05F9.5; CE04807; WBGene00001757; gst-9.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00970000196005; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; Q21743; -.
DR OMA; YDEMANI; -.
DR OrthoDB; 2881536at2759; -.
DR PhylomeDB; Q21743; -.
DR Reactome; R-CEL-156590; Glutathione conjugation.
DR Reactome; R-CEL-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR PRO; PR:Q21743; -.
DR Proteomes; UP000001940; Chromosome II.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd03192; GST_C_Sigma_like; 1.
DR CDD; cd03039; GST_N_Sigma_like; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF263; GLUTATHIONE S-TRANSFERASE 9-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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 9"
FT /id="PRO_0000185932"
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; 23537 MW; 3C4B2ADC081970D4 CRC64;
MVSYKLIYFQ SRGNGEIARQ VFAFAGQEFI DERISKEQWA EIKNMTPFGQ VPVLEVDGRQ
LAQSITIVRY LSKQFGISGK SSWEEAQVDA LGDQFKDYRV EARPFFRAKM GFSDGDVDQL
YKDLFVPAFN KMYSIFTESL KSSGSGFLVG DSLTWMDLAI AQHSADLLEA DGKILDTFLE
MKDHQKKIHS IPNVKKWIEK RPVTSR
//
