GSTF4_MAIZE
ID GSTF4_MAIZE Reviewed; 223 AA.
AC P46420;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Glutathione S-transferase 4;
DE EC=2.5.1.18;
DE AltName: Full=GST class-phi member 4;
DE AltName: Full=GST-27;
DE AltName: Full=GST-IV;
GN Name=GST4;
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].
RC STRAIN=cv. UE95; TISSUE=Seedling root;
RX PubMed=7858222; DOI=10.1007/bf00019498;
RA Jepson I., Lay V.J., Holt D.C., Bright S.W.J., Greenland A.J.;
RT "Cloning and characterization of maize herbicide safener-induced cDNAs
RT encoding subunits of glutathione S-transferase isoforms I, II and IV.";
RL Plant Mol. Biol. 26:1855-1866(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Pioneer hybrid 3906;
RX PubMed=7870838; DOI=10.1104/pp.107.1.311;
RA Irzyk G.P., Potter S., Ward E., Fuerst E.P.;
RT "A cDNA clone encoding the 27-kilodalton subunits of glutathione S-
RT transferase IV from Zea mays.";
RL Plant Physiol. 107:311-312(1995).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX PubMed=8278534; DOI=10.1104/pp.102.3.803;
RA Irzyk G.P., Fuerst E.P.;
RT "Purification and characterization of a glutathione S-transferase from
RT benoxacor-treated maize (Zea mays).";
RL Plant Physiol. 102:803-810(1993).
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. Most active with substrates
CC possessing a chloroacetamide structure. Trans-cinnamic acid and 1-
CC chloro-2,4-dinitrobenzene are not effective substrates. May play an
CC important role in the benoxacor-mediated protection of maize from
CC metolachlor injury.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8. Active from pH 6 to 9.;
CC -!- SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II).
CC -!- TISSUE SPECIFICITY: Seedling roots.
CC -!- INDUCTION: By herbicides.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; X79515; CAA56047.1; -; mRNA.
DR EMBL; U12679; AAA20585.1; -; mRNA.
DR PIR; S52037; S52037.
DR RefSeq; NP_001105366.1; NM_001111896.2.
DR AlphaFoldDB; P46420; -.
DR SMR; P46420; -.
DR STRING; 4577.GRMZM2G132093_P01; -.
DR PaxDb; P46420; -.
DR PRIDE; P46420; -.
DR EnsemblPlants; Zm00001eb418060_T001; Zm00001eb418060_P001; Zm00001eb418060.
DR GeneID; 542311; -.
DR Gramene; Zm00001eb418060_T001; Zm00001eb418060_P001; Zm00001eb418060.
DR KEGG; zma:542311; -.
DR MaizeGDB; 113242; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_5_1_1; -.
DR OMA; RAWWEEL; -.
DR OrthoDB; 1231780at2759; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; P46420; baseline and differential.
DR Genevisible; P46420; ZM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0043295; F:glutathione binding; IDA:AgBase.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IDA:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:AgBase.
DR CDD; cd03187; GST_C_Phi; 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; IPR034347; GST_Phi_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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 Direct protein sequencing; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..223
FT /note="Glutathione S-transferase 4"
FT /id="PRO_0000185843"
FT DOMAIN 4..85
FT /note="GST N-terminal"
FT DOMAIN 90..223
FT /note="GST C-terminal"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 56..57
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 69..70
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="Blocked amino end (Ala)"
SQ SEQUENCE 223 AA; 24570 MW; 24235245AFB4A403 CRC64;
MATPAVKVYG WAISPFVSRA LLALEEAGVD YELVPMSRQD GDHRRPEHLA RNPFGKVPVL
EDGDLTLFES RAIARHVLRK HKPELLGGGR LEQTAMVDVW LEVEAHQLSP PAIAIVVECV
FAPFLGRERN QAVVDENVEK LKKVLEVYEA RLATCTYLAG DFLSLADLSP FTIMHCLMAT
EYAALVHALP HVSAWWQGLA ARPAANKVAQ FMPVGAGAPK EQE
