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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//