ID   GSTF_HYOMU              Reviewed;         212 AA.
AC   P46423;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Glutathione S-transferase {ECO:0000303|PubMed:8108497};
DE            EC=2.5.1.18 {ECO:0000269|PubMed:8108497};
DE   AltName: Full=25 kDa auxin-binding protein {ECO:0000303|PubMed:8108497};
DE   AltName: Full=GST class-phi {ECO:0000303|PubMed:8108497};
OS   Hyoscyamus muticus (Egyptian henbane).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC   Hyoscyamus.
OX   NCBI_TaxID=35626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RX   PubMed=8108497; DOI=10.1104/pp.102.1.29;
RA   Bilang J., Macdonald H., King P.J., Sturm A.;
RT   "A soluble auxin-binding protein from Hyoscyamus muticus is a glutathione
RT   S-transferase.";
RL   Plant Physiol. 102:29-34(1993).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000269|PubMed:8108497}.
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:0000269|PubMed:8108497};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR   EMBL; X78203; CAA55039.1; -; mRNA.
DR   AlphaFoldDB; P46423; -.
DR   SMR; P46423; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
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; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   PANTHER; PTHR43900:SF27; GLUTATHIONE S-TRANSFERASE-LIKE; 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   1: Evidence at protein level;
KW   Auxin signaling pathway; Direct protein sequencing; Transferase.
FT   CHAIN           1..212
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185854"
FT   DOMAIN          1..82
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          89..212
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   212 AA;  23677 MW;  9FFDB1A6A4582AD8 CRC64;
     MGMKLHGPAM SPAVMRVIAT LKEKDLDFEL VPVNMQAGDH KKEPFITLNP FGQVPAFEDG
     DLKLFESRAI TQYIAHTYAD KGNQLLANDP KKMAIMSVWM EVESQKFDPV ASKLTFEIVI
     KPMLGMVTDD AAVAENEEKL GKVLDVYESR LKDSKYLGGD SFTLADLHHA PAMNYLMGTK
     VKSLFDSRPH VSAWCADILA RPAWSKAIEY KQ
//