ID   D7LWY3_ARALL            Unreviewed;       214 AA.
AC   D7LWY3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   Name=ATGSTF12 {ECO:0000313|EMBL:EFH48014.1};
GN   ORFNames=ARALYDRAFT_488585 {ECO:0000313|EMBL:EFH48014.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family.
CC       {ECO:0000256|ARBA:ARBA00010128}.
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; GL348718; EFH48014.1; -; Genomic_DNA.
DR   RefSeq; XP_002871755.1; XM_002871709.1.
DR   AlphaFoldDB; D7LWY3; -.
DR   STRING; 81972.D7LWY3; -.
DR   EnsemblPlants; fgenesh2_kg.6__1719__AT5G17220.1; fgenesh2_kg.6__1719__AT5G17220.1; fgenesh2_kg.6__1719__AT5G17220.1.
DR   Gramene; fgenesh2_kg.6__1719__AT5G17220.1; fgenesh2_kg.6__1719__AT5G17220.1; fgenesh2_kg.6__1719__AT5G17220.1.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_5_1_1; -.
DR   OrthoDB; 639740at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblPlants.
DR   GO; GO:0009705; C:plant-type vacuole membrane; IEA:EnsemblPlants.
DR   GO; GO:0043169; F:cation binding; IEA:EnsemblPlants.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IEA:EnsemblPlants.
DR   GO; GO:1900384; P:regulation of flavonol biosynthetic process; IEA:EnsemblPlants.
DR   GO; GO:0009407; P:toxin catabolic process; IEA:UniProt.
DR   CDD; cd03187; GST_C_Phi; 1.
DR   CDD; cd03053; GST_N_Phi; 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; IPR034347; GST_Phi_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43900:SF54; GLUTATHIONE S-TRANSFERASE F12; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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|ARBA:ARBA00022490};
KW   Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW   Transferase {ECO:0000313|EMBL:EFH48014.1}.
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          89..214
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   214 AA;  24604 MW;  FC424A98CFCCF492 CRC64;
     MVVKLYGQVT AACPQRVLLC FLEKEIEFEI IHIDLDTLEQ KKPEHLLRQP FGQVPAIEDG
     DFKLFESRAI ARYYATKYAD QGTNLLGKSL EHRAIVDQWA DVETHYFNAL AHPIVINLII
     KPRLGEKCDV VLVEELKVKL GVVLDIYNNR LSSNRFLAGE EFTMADLTHM PAMGYLMSIT
     DINQMVKARG SFNRWWEEIS DRPSWKKLMV LAGH
//