ID   GSTX3_SOYBN             Reviewed;         219 AA.
AC   P46417;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Glutathione S-transferase 3;
DE            EC=2.5.1.18;
GN   Name=GST3;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Koellner B., Finkelnburg B., Mayerbacher R., Paulus C., Springer B.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=10666306; DOI=10.1006/abbi.1999.1596;
RA   Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R.;
RT   "Cloning and characterization of glyoxalase I from soybean.";
RL   Arch. Biochem. Biophys. 374:261-268(2000).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Involved in the
CC       detoxification of certain herbicides.
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:10666306};
CC   -!- SUBUNIT: Homodimer. degradation; (R)-lactate from methylglyoxal: step
CC       1/2. {ECO:0000269|PubMed:10666306}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally (Ref.1) thought to be a glyoxalase I.
CC       {ECO:0000305}.
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DR   EMBL; X68819; CAA48717.1; -; mRNA.
DR   PIR; S47177; S47177.
DR   RefSeq; NP_001236181.1; NM_001249252.2.
DR   AlphaFoldDB; P46417; -.
DR   SMR; P46417; -.
DR   STRING; 3847.GLYMA15G40290.1; -.
DR   PRIDE; P46417; -.
DR   EnsemblPlants; KRH13625; KRH13625; GLYMA_15G252200.
DR   GeneID; 547925; -.
DR   Gramene; KRH13625; KRH13625; GLYMA_15G252200.
DR   KEGG; gmx:547925; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   HOGENOM; CLU_011226_18_2_1; -.
DR   InParanoid; P46417; -.
DR   OMA; PECSILM; -.
DR   OrthoDB; 1225872at2759; -.
DR   Proteomes; UP000008827; Chromosome 15.
DR   Genevisible; P46417; GM.
DR   GO; GO:0005737; C:cytoplasm; 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:0042221; P:response to chemical; IEA:UniProt.
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; IPR004046; GST_C.
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; 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   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..219
FT                   /note="Glutathione S-transferase 3"
FT                   /id="PRO_0000185873"
FT   DOMAIN          3..82
FT                   /note="GST N-terminal"
FT   DOMAIN          88..216
FT                   /note="GST C-terminal"
FT   BINDING         13
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   219 AA;  25901 MW;  6A2E46B759476A8C CRC64;
     MSDEVVLLDT WASMYGMRAR IALAEKGVRY EYKEENLMNR SPLLLQMNPI HKKIPVLIHN
     GKPICESAII VQYIDEVWND KSPLMPSDPY KRSQARFWVD YIDKKIYDTW KKMWLSKGEE
     HEEGKKELIS IFKQLEETLT DKPFYGDDTF GFVDLCLITF SSWFYTYETY GNFKMEEECP
     KLMAWVKRCM ERETVSNTLP DAKKVYGLIV ELQKTLESK