ID GSTF1_MAIZE Reviewed; 214 AA. AC P12653; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JAN-2024, entry version 147. DE RecName: Full=Glutathione S-transferase 1; DE EC=2.5.1.18; DE AltName: Full=GST class-phi member 1; DE AltName: Full=GST-29; DE AltName: Full=GST-I; GN Name=GST1; 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]. 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 [GENOMIC DNA]. RX AGRICOLA=IND86033490; DOI=10.1007/BF00015226; RA Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G., RA Tiemeier D.C.; RT "Structural analysis of a maize gene coding for glutathione-S-transferase RT involved in herbicide detoxification."; RL Plant Mol. Biol. 6:203-211(1986). RN [3] RP PROTEIN SEQUENCE OF 2-16. RX AGRICOLA=IND87010820; DOI=10.1007/BF00752897; RA Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J., RA Saunders C., Jaworski E.G., Tiemeier D.C.; RT "Messenger RNA encoding a glutathione-S-transferase responsible for RT herbicide tolerance in maize is induced in response to safener treatment."; RL Plant Mol. Biol. 7:235-243(1986). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH LACTOYLGLUTATHIONE, RP AND SUBUNIT. RX PubMed=9417926; DOI=10.1006/jmbi.1997.1402; RA Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.; RT "Crystal structure of herbicide-detoxifying maize glutathione S- RT transferase-I in complex with lactoylglutathione: evidence for an induced- RT fit mechanism."; RL J. Mol. Biol. 274:446-453(1997). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATRAZINE-GLUTATHIONE RP CONJUGATE. RX PubMed=9817846; DOI=10.1016/s0969-2126(98)00143-9; RA Prade L., Huber R., Bieseler B.; RT "Structures of herbicides in complex with their detoxifying enzyme RT glutathione S-transferase -- explanations for the selectivity of the enzyme RT in plants."; RL Structure 6:1445-1452(1998). 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. 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 -!- SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II). CC {ECO:0000269|PubMed:9417926, ECO:0000269|PubMed:9817846}. CC -!- TISSUE SPECIFICITY: Expressed in the stem and leaves, lower levels are CC seen in the pollen and endosperm. 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; X06754; CAA29928.1; -; mRNA. DR EMBL; M16901; AAA33470.1; -; mRNA. DR EMBL; M16902; AAA33469.1; -; Genomic_DNA. DR EMBL; M16900; AAA33469.1; JOINED; Genomic_DNA. DR PIR; S03726; XUZM1. DR RefSeq; NP_001105412.1; NM_001111942.1. DR PDB; 1AXD; X-ray; 2.50 A; A/B=2-210. DR PDB; 1BYE; X-ray; 2.80 A; A/B/C/D=2-214. DR PDBsum; 1AXD; -. DR PDBsum; 1BYE; -. DR AlphaFoldDB; P12653; -. DR SMR; P12653; -. DR STRING; 4577.P12653; -. DR PaxDb; 4577-GRMZM2G116273_P01; -. DR GeneID; 542366; -. DR KEGG; zma:542366; -. DR MaizeGDB; 65344; -. DR eggNOG; KOG0867; Eukaryota. DR InParanoid; P12653; -. DR OrthoDB; 444791at2759; -. DR BRENDA; 2.5.1.18; 6752. DR SABIO-RK; P12653; -. DR EvolutionaryTrace; P12653; -. DR Proteomes; UP000007305; Unplaced. DR ExpressionAtlas; P12653; 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; 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; TAS:AgBase. DR GO; GO:0042542; P:response to hydrogen peroxide; TAS:AgBase. DR GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase. DR GO; GO:0009751; P:response to salicylic acid; TAS:AgBase. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP: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:SF39; GLUTATHIONE S-TRANSFERASE GSTF2-RELATED; 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. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.3" FT CHAIN 2..214 FT /note="Glutathione S-transferase 1" FT /id="PRO_0000185841" FT DOMAIN 2..83 FT /note="GST N-terminal" FT DOMAIN 88..214 FT /note="GST C-terminal" FT BINDING 12 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250" FT BINDING 41..42 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT BINDING 54..55 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT BINDING 67..68 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT CONFLICT 15 FT /note="L -> V (in Ref. 2; AAA33470/AAA33469)" FT /evidence="ECO:0000305" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:1AXD" FT STRAND 10..14 FT /evidence="ECO:0007829|PDB:1BYE" FT HELIX 15..25 FT /evidence="ECO:0007829|PDB:1AXD" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:1AXD" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:1AXD" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:1AXD" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:1AXD" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 89..104 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 106..117 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 129..152 FT /evidence="ECO:0007829|PDB:1AXD" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 169..175 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 179..186 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 188..199 FT /evidence="ECO:0007829|PDB:1AXD" FT HELIX 201..209 FT /evidence="ECO:0007829|PDB:1AXD" SQ SEQUENCE 214 AA; 23822 MW; 97DA6337ADF03CB1 CRC64; MAPMKLYGAV MSWNLTRCAT ALEEAGSDYE IVPINFATAE HKSPEHLVRN PFGQVPALQD GDLYLFESRA ICKYAARKNK PELLREGNLE EAAMVDVWIE VEANQYTAAL NPILFQVLIS PMLGGTTDQK VVDENLEKLK KVLEVYEARL TKCKYLAGDF LSLADLNHVS VTLCLFATPY ASVLDAYPHV KAWWSGLMER PSVQKVAALM KPSA //