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 27-MAR-2024, entry version 149.
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; 50.
DR DIP; DIP-24504N; -.
DR IntAct; P91253; 1.
DR STRING; 6239.F11G11.2.1; -.
DR EPD; P91253; -.
DR PaxDb; 6239-F11G11-2; -.
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 AGR; WB:WBGene00001755; -.
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; SDIYIDW; -.
DR OrthoDB; 1385810at2759; -.
DR PhylomeDB; P91253; -.
DR PRO; PR:P91253; -.
DR Proteomes; UP000001940; Chromosome II.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; HEP:WormBase.
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; IPR040079; Glutathione_S-Trfase.
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:SF98; GLUTATHIONE S-TRANSFERASE 7-RELATED; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 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
//
