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