GSTF3_MAIZE
ID GSTF3_MAIZE Reviewed; 222 AA.
AC P04907; P15542;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutathione S-transferase 3 {ECO:0000303|PubMed:3277162, ECO:0000303|PubMed:3532034};
DE EC=2.5.1.18 {ECO:0000269|PubMed:3277162, ECO:0000269|PubMed:3532034};
DE AltName: Full=GST class-phi member 3 {ECO:0000303|PubMed:3277162, ECO:0000303|PubMed:3532034};
DE AltName: Full=GST-III {ECO:0000303|PubMed:3277162, ECO:0000303|PubMed:3532034};
GN Name=GST3 {ECO:0000303|PubMed:3277162, ECO:0000303|PubMed:3532034};
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3277162; DOI=10.1093/nar/16.2.425;
RA Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., Tu C.-P.D.;
RT "Characterization and heterospecific expression of cDNA clones of genes in
RT the maize GSH S-transferase multigene family.";
RL Nucleic Acids Res. 16:425-438(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=3532034; DOI=10.1093/nar/14.18.7227;
RA Moore R.E., Davies M.S., O'Connell K.M., Harding E.I., Wiegand R.C.,
RA Tiemeier D.C.;
RT "Cloning and expression of a cDNA encoding a maize glutathione-S-
RT transferase in E. coli.";
RL Nucleic Acids Res. 14:7227-7235(1986).
RN [3]
RP PROTEIN SEQUENCE OF 143-153.
RC TISSUE=Coleoptile;
RX AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., Pernollet J.-C.,
RA Zivy M., de Vienne D.;
RT "The maize two dimensional gel protein database: towards an integrated
RT genome analysis program.";
RL Theor. Appl. Genet. 93:997-1005(1996).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (PubMed:3277162,
CC PubMed:3532034). Involved in the detoxification of certain herbicides
CC (PubMed:3532034). {ECO:0000269|PubMed:3277162,
CC ECO:0000269|PubMed:3532034}.
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; Evidence={ECO:0000269|PubMed:3277162,
CC ECO:0000269|PubMed:3532034};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3532034}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Phi family. {ECO:0000305}.
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DR EMBL; X06755; CAA29929.1; -; mRNA.
DR EMBL; X04375; CAA27957.1; -; mRNA.
DR EMBL; X04455; CAA28053.1; -; mRNA.
DR PIR; A24703; XUZM31.
DR PIR; S00717; XUZM32.
DR AlphaFoldDB; P04907; -.
DR SMR; P04907; -.
DR STRING; 4577.GRMZM2G146246_P02; -.
DR PRIDE; P04907; -.
DR MaizeGDB; 65344; -.
DR eggNOG; KOG0867; Eukaryota.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P04907; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; NAS:AgBase.
DR GO; GO:0043295; F:glutathione binding; IBA:GO_Central.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:AgBase.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; 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; 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 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..222
FT /note="Glutathione S-transferase 3"
FT /id="PRO_0000185842"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 89..219
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 12
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 13..14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 41..42
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 54..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT BINDING 67..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O80852"
FT CONFLICT 108
FT /note="H -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..127
FT /note="ASPLVFQLLVRPLLGGA -> RVAAGVPAAREAAPGRR (in Ref. 2;
FT CAA27957/CAA28053)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="E -> D (in Ref. 2; CAA27957/CAA28053)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..180
FT /note="AHLARNKYLAGDEFTLADANHALLPALTSARP -> RTSPATSTSPGTSSRS
FT PTPTTRSYLLYLSKT (in Ref. 2; CAA27957)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..189
FT /note="GCVAAR -> ARRRP (in Ref. 2; CAA27957)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="A -> V (in Ref. 2; CAA27957/CAA28053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 23849 MW; 4CB77A3B1B6E3C46 CRC64;
MAPLKLYGMP LSPNVVRVAT VLNEKGLDFE IVPVDLTTGA HKQPDFLALN PFGQIPALVD
GDEVLFESRA INRYIASKYA SEGTDLLPAT ASAAKLEVWL EVESHHFHPN ASPLVFQLLV
RPLLGGAPDA AVVEKHAEQL AKVLDVYEAH LARNKYLAGD EFTLADANHA LLPALTSARP
PRPGCVAARP HVKAWWEAIA ARPAFQKTVA AIPLPPPPSS SA
