ID A0A059AXY3_EUCGR Unreviewed; 213 AA.
AC A0A059AXY3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN ORFNames=EUGRSUZ_H01166 {ECO:0000313|EMBL:KCW58491.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW58491.1};
RN [1] {ECO:0000313|EMBL:KCW58491.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW58491.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK198760; KCW58491.1; -; Genomic_DNA.
DR RefSeq; XP_010069962.1; XM_010071660.2.
DR AlphaFoldDB; A0A059AXY3; -.
DR STRING; 71139.A0A059AXY3; -.
DR EnsemblPlants; KCW58491; KCW58491; EUGRSUZ_H01166.
DR GeneID; 104456802; -.
DR Gramene; KCW58491; KCW58491; EUGRSUZ_H01166.
DR eggNOG; KOG0867; Eukaryota.
DR InParanoid; A0A059AXY3; -.
DR OMA; THTYERN; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043295; F:glutathione binding; 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: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; 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:SF47; GLUTATHIONE S-TRANSFERASE F6-RELATED; 1.
DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01154; Main.5:_Phi-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|ARBA:ARBA00022490}.
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 88..213
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 213 AA; 23825 MW; 97AC7D9871E27150 CRC64;
MVMKVYGTVL STATMRIFAA LYEKDLEFEF VPIDMPAGEH KKEHFLALNP FGQVPAFEDG
DLKLFESRAV TQHIAHVFAD EGTPLICEGK SMATVGVWME VEAQQFEPLA LKLRREFLYK
PRSGVATDAA VVEESEAKLA KVLDVYEARL SQSKYLGCDC FTLADLHPLP TMTTLMGTPV
RKLFDARPKL SAWLADISAR PAWAKVLAMR NQQ
//
