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Database: UniProt
Entry: M1CB11_SOLTU
LinkDB: M1CB11_SOLTU
Original site: M1CB11_SOLTU 
ID   M1CB11_SOLTU            Unreviewed;       224 AA.
AC   M1CB11;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN   Name=102602918 {ECO:0000313|EnsemblPlants:PGSC0003DMT400063686};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400063686, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400063686}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400063686};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) 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   RefSeq; XP_006344661.1; XM_006344599.2.
DR   AlphaFoldDB; M1CB11; -.
DR   STRING; 4113.M1CB11; -.
DR   PaxDb; 4113-PGSC0003DMT400063686; -.
DR   EnsemblPlants; PGSC0003DMT400063686; PGSC0003DMT400063686; PGSC0003DMG400024752.
DR   GeneID; 102602918; -.
DR   Gramene; PGSC0003DMT400063686; PGSC0003DMT400063686; PGSC0003DMG400024752.
DR   Gramene; RHC01H1G3641.2.1; RHC01H1G3641.2.1; RHC01H1G3641.2.
DR   KEGG; sot:102602918; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_1_1; -.
DR   InParanoid; M1CB11; -.
DR   OMA; ETWPLIN; -.
DR   OrthoDB; 767442at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1CB11; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR11260:SF696; GLUTATHIONE TRANSFERASE; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369102}.
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;  25394 MW;  284F8AD3170D36D1 CRC64;
     MEDVKLLGTK ESIFTQRIMW ALKLKGICYE FIEQDFSSRS SPLLVKLNPV YNKVPVIVHD
     GNSLAESLVI LEYIEETWPL INPLFPVDPF ERASGRFWAR FVDGKFYEAA KRAFFSSGET
     KAEGVESVVE GLHLLEGQII GKKFFGGEKI GYLDIIIGWI AYWFQYIEEI GEFKAMDSTK
     YPCLHAWINN FIQLPIIQQS LPTPDVVKAV FRGFKDAAAL AGAN
//
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