GSTF1_MAIZE
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 03-AUG-2022, entry version 140.
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}.
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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.GRMZM2G116273_P01; -.
DR PaxDb; P12653; -.
DR PRIDE; P12653; -.
DR GeneID; 542366; -.
DR KEGG; zma:542366; -.
DR MaizeGDB; 65344; -.
DR eggNOG; KOG0867; Eukaryota.
DR OrthoDB; 1231780at2759; -.
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; IEA:InterPro.
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 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 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
