ID   GSTF1_TOBAC             Reviewed;         213 AA.
AC   P30109;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Glutathione S-transferase PARB {ECO:0000303|PubMed:1729717};
DE            EC=2.5.1.18 {ECO:0000250|UniProtKB:O80852};
DE   AltName: Full=GST class-phi {ECO:0000303|PubMed:1729717};
GN   Name=PARB {ECO:0000303|PubMed:1729717};
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], DEVELOPMENTAL STAGE, AND INDUCTION BY AUXIN.
RC   STRAIN=cv. Xanthi NC; TISSUE=Leaf mesophyll;
RX   PubMed=1729717; DOI=10.1073/pnas.89.1.56;
RA   Takahashi Y., Nagata T.;
RT   "parB: an auxin-regulated gene encoding glutathione S-transferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:56-59(1992).
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   -!- DEVELOPMENTAL STAGE: Its expression was observed during transition from
CC       G0 to the S phase of tobacco mesophyll protoplasts in vitro.
CC       {ECO:0000269|PubMed:1729717}.
CC   -!- INDUCTION: By auxin. {ECO:0000269|PubMed:1729717}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; D10524; BAA01394.1; -; mRNA.
DR   PIR; A41789; A41789.
DR   RefSeq; NP_001312529.1; NM_001325600.1.
DR   AlphaFoldDB; P30109; -.
DR   SMR; P30109; -.
DR   STRING; 4097.P30109; -.
DR   PaxDb; 4097-P30109; -.
DR   GeneID; 107795177; -.
DR   KEGG; nta:107795177; -.
DR   OrthoDB; 639740at2759; -.
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; 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; 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: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; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01154; Main.5:_Phi-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   Reference proteome; Transferase.
FT   CHAIN           1..213
FT                   /note="Glutathione S-transferase PARB"
FT                   /id="PRO_0000185856"
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;  23967 MW;  0AB971171E7CCFDC CRC64;
     MAIKVHGSPM STATMRVAAC LIEKELDFEF VPVDMASGEH KKHPYLSLNP FGQVPAFEDG
     DLKLFESRAI TQYIAHVYAD NGYQLILQDP KKMPSMSVWM EVEGQKFEPP ATKLTWELGI
     KPIIGMTTDD AAVKESEAQL SKVLDIYETQ LAESKYLGGD SFTLVDLHHI PNIYYLMSSK
     VKEVFDSRPR VSAWCADILA RPAWVKGLEK LQK
//