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Database: UniProt
Entry: A3FMP5_SOLLC
LinkDB: A3FMP5_SOLLC
Original site: A3FMP5_SOLLC 
ID   A3FMP5_SOLLC            Unreviewed;       224 AA.
AC   A3FMP5;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN   Name=gst {ECO:0000313|EMBL:ABN54441.1};
GN   Synonyms=100037735 {ECO:0000313|EnsemblPlants:Solyc01g099590.3.1};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EMBL:ABN54441.1};
RN   [1] {ECO:0000313|EMBL:ABN54441.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gafni Y., Levy Y.;
RT   "Putative Glutathione-S-transferase from Solanum lycopersicum cv. Rio
RT   Grande.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:Solyc01g099590.3.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g099590.3.1};
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [3] {ECO:0000313|EnsemblPlants:Solyc01g099590.3.1}
RP   IDENTIFICATION.
RC   STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc01g099590.3.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2019) to UniProtKB.
CC   -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC       wide number of exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000256|RuleBase:RU369102}.
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:0000256|ARBA:ARBA00000710,
CC         ECO:0000256|RuleBase:RU369102};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU369102}.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU369102}.
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DR   EMBL; EF409975; ABN54441.1; -; mRNA.
DR   RefSeq; NP_001234222.1; NM_001247293.1.
DR   AlphaFoldDB; A3FMP5; -.
DR   SMR; A3FMP5; -.
DR   STRING; 4081.A3FMP5; -.
DR   PaxDb; 4081-Solyc01g099590-2-1; -.
DR   EnsemblPlants; Solyc01g099590.3.1; Solyc01g099590.3.1; Solyc01g099590.3.
DR   GeneID; 100037735; -.
DR   Gramene; Solyc01g099590.3.1; Solyc01g099590.3.1; Solyc01g099590.3.
DR   KEGG; sly:100037735; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_1_1; -.
DR   InParanoid; A3FMP5; -.
DR   OMA; ETWPLIN; -.
DR   OrthoDB; 1110520at2759; -.
DR   Proteomes; UP000004994; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF696; GLUTATHIONE S-TRANSFERASE U7-LIKE; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF13410; GST_C_2; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004994};
KW   Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:ABN54441.1}.
FT   DOMAIN          2..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..219
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   224 AA;  25482 MW;  5690E3117D7311A0 CRC64;
     MEDVKLLGTK ESIFTQRIIW ALKLKGICYE FIEQDFSSRS SPLLVKLNPV YNKVPVIVHD
     GKSLAESLVI LEYIEETWPL INPLFPLDPF QRASTRFWAR FVDGKFYEAA KKAFFSSGET
     KAEGVESVVE GLHLLEGQII GKKFFGGEKI GYLDIITGWI AYWFQYIEEI GEFKAMDSTK
     YPCLHAWINN FIQLPIIKQS LPTPDVVKSV FRGFKDAAAL ADAN
//
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