GSTF2_TOBAC
ID GSTF2_TOBAC Reviewed; 213 AA.
AC P46440;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Glutathione S-transferase APIC {ECO:0000303|Ref.1};
DE EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE AltName: Full=GST class-phi {ECO:0000303|Ref.1};
GN Name=APIC {ECO:0000303|Ref.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY ALUMINUM STRESS AND PHOSPHATE
RP STARVATION.
RC STRAIN=cv. Samsun;
RX DOI=10.1034/j.1399-3054.1995.930103.x;
RA Ezaki B., Yamamoto Y., Matsumoto H.;
RT "Cloning and sequencing of the cDNAs induced by aluminium treatment and Pi
RT starvation in cultured tobacco cells.";
RL Physiol. Plantarum 93:11-18(1995).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:O80852}.
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:0000250|UniProtKB:O80852};
CC -!- INDUCTION: By aluminum stress and phosphate starvation.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; D29680; BAA06150.1; -; mRNA.
DR RefSeq; NP_001312208.1; NM_001325279.1.
DR AlphaFoldDB; P46440; -.
DR SMR; P46440; -.
DR STRING; 4097.P46440; -.
DR GeneID; 107779283; -.
DR KEGG; nta:107779283; -.
DR OMA; NARRVWV; -.
DR PhylomeDB; P46440; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03187; GST_C_Phi; 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 Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Stress response; Transferase.
FT CHAIN 1..213
FT /note="Glutathione S-transferase APIC"
FT /id="PRO_0000185857"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 89..213
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 12..13
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 40..41
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 53..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 66..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
SQ SEQUENCE 213 AA; 24113 MW; EFFBE1A23094037B CRC64;
MAIKVHGSPM STATMRVAAC LIEKDLDFEL VPVDMVSGEH KKHPYLSLNP FGQVPAFEDG
DLKLFESRAI TQYIAHVYAD NGYQLILQDP KKMPIMSVWM EVEGQKFEPH ASKLTWELGI
KPIIGMTTDD DAVKESEVQL SKVLDIYETR LAESKYLGGD SFTLVDLHHI PNIYYLMSTK
VKEVFDSRPR VSAWCADILA RPAWVKGLEK LQK
