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GSTX2_MAIZE
ID   GSTX2_MAIZE             Reviewed;         236 AA.
AC   P50472;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Probable glutathione S-transferase BZ2;
DE            EC=2.5.1.18;
DE   AltName: Full=Protein bronze-2;
GN   Name=BZ2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Seedling;
RX   PubMed=1967051; DOI=10.2307/3869257;
RA   Nash J., Luehrsen K.R., Walbot V.;
RT   "Bronze-2 gene of maize: reconstruction of a wild-type allele and analysis
RT   of transcription and splicing.";
RL   Plant Cell 2:1039-1049(1990).
RN   [2]
RP   ERRATUM OF PUBMED:1967051.
RA   Nash J., Luehrsen K.R., Walbot V.;
RL   Plant Cell 3:103-103(1991).
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   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- SIMILARITY: Belongs to the GST superfamily. HSP26 family.
CC       {ECO:0000305}.
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DR   EMBL; U14599; AAA50245.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50472; -.
DR   SMR; P50472; -.
DR   STRING; 4577.GRMZM2G016241_P02; -.
DR   PaxDb; P50472; -.
DR   PRIDE; P50472; -.
DR   MaizeGDB; 64140; -.
DR   eggNOG; KOG0406; Eukaryota.
DR   UniPathway; UPA00009; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P50472; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260; PTHR11260; 1.
DR   Pfam; PF13417; GST_N_3; 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   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..236
FT                   /note="Probable glutathione S-transferase BZ2"
FT                   /id="PRO_0000185861"
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT   DOMAIN          92..221
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..65
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  25563 MW;  BD7C087F60FA6E9A CRC64;
     MRVLGGEVSP FTARARLALD LRGVAYELLD EPLGPKKSDR LLAANPVYGK IPVLLLPDGR
     AICESAVIVQ YIEDVARESG GAEAGSLLLP DDPYERAMHR FWTAFIDDKF WPALDAVSLA
     PTPGARAQAA EDTRAALSLL EEAFKDRSNG RAFFSGGDAA PGLLDLALGC FLPALRACER
     LHGLSLIDAS ATPLLDGWSQ RFAAHPAAKR VLPDTEKVVQ FTRFLQVQAQ FRVHVS
 
 
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