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 27-MAR-2024, entry version 139. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.P46420; -. DR PaxDb; 4577-GRMZM2G132093_P01; -. 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 InParanoid; P46420; -. DR OMA; RAIVMQW; -. DR OrthoDB; 444791at2759; -. DR Proteomes; UP000007305; Chromosome 10. DR ExpressionAtlas; P46420; baseline and differential. 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; IBA:GO_Central. 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 CDD; cd03053; GST_N_Phi; 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; 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 PANTHER; PTHR43900:SF17; GLUTATHIONE S-TRANSFERASE 4; 1. DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01154; Main.5:_Phi-like; 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. DR Genevisible; P46420; ZM. 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 //