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Database: UniProt
Entry: D2X9S0_POPTR
LinkDB: D2X9S0_POPTR
Original site: D2X9S0_POPTR 
ID   D2X9S0_POPTR            Unreviewed;       220 AA.
AC   D2X9S0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE            EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS   trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=3694 {ECO:0000313|EMBL:ADB11362.1};
RN   [1] {ECO:0000313|EMBL:ADB11362.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19996377; DOI=10.1105/tpc.109.070219;
RA   Lan T., Yang Z.L., Yang X., Liu Y.J., Wang X.R., Zeng Q.Y.;
RT   "Extensive functional diversification of the Populus glutathione S-
RT   transferase supergene family.";
RL   Plant Cell 21:3749-3766(2009).
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; GU065669; ADB11362.1; -; mRNA.
DR   AlphaFoldDB; D2X9S0; -.
DR   ExpressionAtlas; D2X9S0; differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   CDD; cd03058; GST_N_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; IPR040079; Glutathione_S-Trfase.
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:SF547; GLUTATHIONE S-TRANSFERASE, AMINO-TERMINAL DOMAIN PROTEIN; 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; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 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   Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:ADB11362.1}.
FT   DOMAIN          4..84
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          89..209
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   220 AA;  24952 MW;  1321D8C62869C84F CRC64;
     MSKEDLLLLD FWVSPFCMRV KIALAEKGLN YESKEEDLFG GKSELLLKSN PVYQKVPVLL
     HNGKPLNESA IIVGYIDEKW PSPPLLPACA YGRSQARFWA DYIDKKVIDA TCTVWRSTGE
     AVEVAKKDFI EVLKVLEEAL GEKTFFGGET FGFVDIVAIP MASWFYASEK FGNFTVEAEC
     PKLSAWIKRS MQRESVAKVL PDPEKVYDFV VMFRKMQGIE
//
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