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 27-MAR-2024, entry version 143. 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}. 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; 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.P04907; -. DR PaxDb; 4577-GRMZM2G146246_P02; -. DR MaizeGDB; 65344; -. DR eggNOG; KOG0867; Eukaryota. DR InParanoid; P04907; -. 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; IBA:GO_Central. DR GO; GO:0009635; P:response to herbicide; 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; 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:SF98; GLUTATHIONE S-TRANSFERASE 2; 1. DR PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01150; Main.1:_Beta-like; 1. DR SFLD; SFLDG01154; Main.5:_Phi-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 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 //