GSTXC_TOBAC
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 03-AUG-2022, entry version 86.
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=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 -!- 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 GeneID; 107823949; -.
DR KEGG; nta:107823949; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260; PTHR11260; 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 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 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