ID   GSTXC_TOBAC             Reviewed;         221 AA.
AC   P49332;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   RecName: Full=Probable glutathione S-transferase parC;
DE            EC=2.5.1.18;
DE   AltName: Full=Auxin-regulated protein parC;
GN   Name=PARC;
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].
RC   STRAIN=cv. Xanthi NC; TISSUE=Leaf mesophyll;
RA   Takahashi Y., Nagata T.;
RT   "Differential expression of an auxin-regulated gene, parC, and a novel
RT   related gene, C-7 from tobacco mesophyll protoplasts in response to
RT   external stimuli and plant tissues.";
RL   Plant Cell Physiol. 33:779-787(1992).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RX + glutathione = an S-substituted glutathione + a halide
CC         anion + 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   -!- TISSUE SPECIFICITY: Abundant in seedlings and roots. It is also found
CC       in the shoot tips, flowers and leaves.
CC   -!- INDUCTION: By auxin.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; X64398; CAA45740.1; -; mRNA.
DR   PIR; S19185; S19185.
DR   RefSeq; NP_001313053.1; NM_001326124.1.
DR   AlphaFoldDB; P49332; -.
DR   SMR; P49332; -.
DR   STRING; 4097.P49332; -.
DR   PaxDb; 4097-P49332; -.
DR   GeneID; 107823949; -.
DR   KEGG; nta:107823949; -.
DR   OrthoDB; 1215279at2759; -.
DR   Proteomes; UP000790787; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03185; GST_C_Tau; 1.
DR   CDD; cd03058; GST_N_Tau; 1.
DR   FunFam; 1.20.1050.10:FF:000018; Glutathione S-transferase U20; 1.
DR   FunFam; 3.40.30.10:FF:000014; Tau class glutathione S-transferase; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF726; GLUTATHIONE S-TRANSFERASE PARC-RELATED; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF00043; GST_C; 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   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   2: Evidence at transcript level;
KW   Auxin signaling pathway; Reference proteome; Transferase.
FT   CHAIN           1..221
FT                   /note="Probable glutathione S-transferase parC"
FT                   /id="PRO_0000185864"
FT   DOMAIN          4..83
FT                   /note="GST N-terminal"
FT   DOMAIN          90..214
FT                   /note="GST C-terminal"
FT   BINDING         14
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         67..68
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  25743 MW;  18D27C69857EB3AE CRC64;
     MANEEVILLD FWPSMFGMRL RIALAEKEIK YEYKQEDLRN KSPLLLQMNP IHKKIPVLIH
     NGKPICESII AVEYIEEVWK DKAPSLLPSD PYDRAQARFW ADYIDKKLYD FGRKLWATKG
     EEQEAAKKDF IECLKVLEGA LGDRPYFGGE SFGFVDIALI GFYSWFYAYE TFGNFSTEAE
     CPKFVAWAKR CMQRESVAKS LPDQPKVLEF VKVLRQKFGL E
//