ID GST23_MAIZE Reviewed; 222 AA.
AC Q9FQA3; Q9FQB6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Glutathione transferase GST 23;
DE EC=2.5.1.18;
DE AltName: Full=Glutathione transferase GST 36;
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 [MRNA], AND VARIANTS ASP-141; ASP-179 AND VAL-195.
RX PubMed=11080288; DOI=10.1104/pp.124.3.1105;
RA McGonigle B., Keeler S.J., Lau S.M., Koeppe M.K., O'Keefe D.P.;
RT "A genomics approach to the comprehensive analysis of the glutathione S-
RT transferase gene family in soybean and maize.";
RL Plant Physiol. 124:1105-1120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RA Yu Y., Currie J., Lomeli R., Angelova A., Collura K., Wissotski M.,
RA Campos D., Kudrna D., Golser W., Ashely E., Haller K., Descour A.,
RA Fernandes J., Zuccolo A., Soderlund C., Walbot V.;
RT "Maize full-length cDNA project.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS, AND FUNCTION.
RX PubMed=21490302; DOI=10.1073/pnas.1011739108;
RA Wisser R.J., Kolkman J.M., Patzoldt M.E., Holland J.B., Yu J.,
RA Krakowsky M., Nelson R.J., Balint-Kurti P.J.;
RT "Multivariate analysis of maize disease resistances suggests a pleiotropic
RT genetic basis and implicates a GST gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7339-7344(2011).
CC -!- FUNCTION: Involved in multiple disease resistance (MDR).
CC {ECO:0000269|PubMed:21490302}.
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 -!- MISCELLANEOUS: The presence of Asp-179 is significantly associated with
CC a multiple disease resistance.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:11080288 describes GST23 and GST36 as two different
CC members of the GST family but they seem to be allelic variants of the
CC same gene. {ECO:0000305}.
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DR EMBL; AF244688; AAG34831.1; -; mRNA.
DR EMBL; AF244701; AAG34844.1; -; mRNA.
DR EMBL; BT040471; ACF85476.1; -; mRNA.
DR EMBL; EU963788; ACG35906.1; -; mRNA.
DR RefSeq; NP_001104994.1; NM_001111524.2.
DR AlphaFoldDB; Q9FQA3; -.
DR SMR; Q9FQA3; -.
DR STRING; 4577.Q9FQA3; -.
DR PaxDb; 4577-GRMZM2G416632_P01; -.
DR EnsemblPlants; Zm00001eb315490_T001; Zm00001eb315490_P001; Zm00001eb315490.
DR GeneID; 541845; -.
DR Gramene; Zm00001eb315490_T001; Zm00001eb315490_P001; Zm00001eb315490.
DR KEGG; zma:541845; -.
DR MaizeGDB; 452083; -.
DR MaizeGDB; 542096; -.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_18_1_1; -.
DR InParanoid; Q9FQA3; -.
DR OMA; MPLLNAW; -.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; Q9FQA3; baseline and differential.
DR Genevisible; Q9FQA3; ZM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 CDD; cd03058; GST_N_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260:SF764; GLUTATHIONE S-TRANSFERASE U1; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-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 2: Evidence at transcript level;
KW Plant defense; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Glutathione transferase GST 23"
FT /id="PRO_0000411116"
FT DOMAIN 4..83
FT /note="GST N-terminal"
FT DOMAIN 89..220
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"
FT VARIANT 141
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:11080288"
FT VARIANT 179
FT /note="H -> D"
FT /evidence="ECO:0000269|PubMed:11080288"
FT VARIANT 195
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:11080288"
SQ SEQUENCE 222 AA; 24879 MW; C56E9A67CC4EE9CC CRC64;
MAEKGVKVLG MWASPMVIRV EWALRLKGVE YEYVDEDLAN KSADLLRHNP VTKKVPVLVH
DGKPVAESTI IVEYIDEVWK GGYPIMPGDP YERAQARFWA RFAEDKCNAA LYPIFTATGE
AQRKAVHEAQ QCLKTLETAL EGKKFFGGDA VGYLDIVVGW FAHWLPVIEE VTGASVVTHE
ELPLMKAWFG RFLALDVVKA ALPDRDRLLA ANKARREQLL SA
//
