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Glutathione S-transferase 1 (EC 2.5.1.18) (GST class-phi member 1) (GST-29) (GST-I)

 GSTF1_MAIZE             Reviewed;         214 AA.
P12653;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
10-MAY-2017, entry version 115.
RecName: Full=Glutathione S-transferase 1;
EC=2.5.1.18;
AltName: Full=GST class-phi member 1;
AltName: Full=GST-29;
AltName: Full=GST-I;
Name=GST1;
Zea mays (Maize).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
Zea.
NCBI_TaxID=4577;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3277162; DOI=10.1093/nar/16.2.425;
Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F.,
Tu C.-P.D.;
"Characterization and heterospecific expression of cDNA clones of
genes in the maize GSH S-transferase multigene family.";
Nucleic Acids Res. 16:425-438(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
AGRICOLA=IND86033490; DOI=10.1007/BF00015226;
Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G.,
Tiemeier D.C.;
"Structural analysis of a maize gene coding for glutathione-S-
transferase involved in herbicide detoxification.";
Plant Mol. Biol. 6:203-211(1986).
[3]
PROTEIN SEQUENCE OF 2-16.
AGRICOLA=IND87010820; DOI=10.1007/BF00752897;
Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J.,
Saunders C., Jaworski E.G., Tiemeier D.C.;
"Messenger RNA encoding a glutathione-S-transferase responsible for
herbicide tolerance in maize is induced in response to safener
treatment.";
Plant Mol. Biol. 7:235-243(1986).
[4]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH
LACTOYLGLUTATHIONE, AND SUBUNIT.
PubMed=9417926; DOI=10.1006/jmbi.1997.1402;
Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.;
"Crystal structure of herbicide-detoxifying maize glutathione S-
transferase-I in complex with lactoylglutathione: evidence for an
induced-fit mechanism.";
J. Mol. Biol. 274:446-453(1997).
[5]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH
ATRAZINE-GLUTATHIONE CONJUGATE.
PubMed=9817846; DOI=10.1016/S0969-2126(98)00143-9;
Prade L., Huber R., Bieseler B.;
"Structures of herbicides in complex with their detoxifying enzyme
glutathione S-transferase -- explanations for the selectivity of the
enzyme in plants.";
Structure 6:1445-1452(1998).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. Involved in
the detoxification of certain herbicides.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer or heterodimer of GST-I and GST-IV (=GST-II).
{ECO:0000269|PubMed:9417926, ECO:0000269|PubMed:9817846}.
-!- TISSUE SPECIFICITY: Expressed in the stem and leaves, lower levels
are seen in the pollen and endosperm.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
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EMBL; X06754; CAA29928.1; -; mRNA.
EMBL; M16901; AAA33470.1; -; mRNA.
EMBL; M16902; AAA33469.1; -; Genomic_DNA.
EMBL; M16900; AAA33469.1; JOINED; Genomic_DNA.
PIR; S03726; XUZM1.
RefSeq; NP_001105412.1; NM_001111942.1.
UniGene; Zm.9; -.
PDB; 1AXD; X-ray; 2.50 A; A/B=2-210.
PDB; 1BYE; X-ray; 2.80 A; A/B/C/D=2-214.
PDBsum; 1AXD; -.
PDBsum; 1BYE; -.
ProteinModelPortal; P12653; -.
SMR; P12653; -.
STRING; 4577.GRMZM2G116273_P01; -.
PaxDb; P12653; -.
PRIDE; P12653; -.
GeneID; 542366; -.
KEGG; zma:542366; -.
MaizeGDB; 65344; -.
eggNOG; KOG0867; Eukaryota.
eggNOG; COG0625; LUCA.
HOGENOM; HOG000125746; -.
KO; K00799; -.
BRENDA; 2.5.1.18; 6752.
SABIO-RK; P12653; -.
EvolutionaryTrace; P12653; -.
Proteomes; UP000007305; Unplaced.
GO; GO:0043234; C:protein complex; IDA:AgBase.
GO; GO:0004364; F:glutathione transferase activity; IDA:AgBase.
GO; GO:0009635; P:response to herbicide; TAS:AgBase.
GO; GO:0042542; P:response to hydrogen peroxide; TAS:AgBase.
GO; GO:0000302; P:response to reactive oxygen species; IEP:AgBase.
GO; GO:0009751; P:response to salicylic acid; TAS:AgBase.
GO; GO:0009410; P:response to xenobiotic stimulus; IEP:AgBase.
CDD; cd03187; GST_C_Phi; 1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR034347; GST_Phi_C.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.3}.
CHAIN 2 214 Glutathione S-transferase 1.
/FTId=PRO_0000185841.
DOMAIN 2 83 GST N-terminal.
DOMAIN 88 214 GST C-terminal.
REGION 41 42 Glutathione binding.
REGION 54 55 Glutathione binding.
REGION 67 68 Glutathione binding.
BINDING 12 12 Glutathione. {ECO:0000250}.
CONFLICT 15 15 L -> V (in Ref. 2; AAA33470/AAA33469).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:1AXD}.
STRAND 10 14 {ECO:0000244|PDB:1BYE}.
HELIX 15 25 {ECO:0000244|PDB:1AXD}.
STRAND 29 32 {ECO:0000244|PDB:1AXD}.
TURN 36 39 {ECO:0000244|PDB:1AXD}.
HELIX 40 42 {ECO:0000244|PDB:1AXD}.
HELIX 44 47 {ECO:0000244|PDB:1AXD}.
STRAND 57 60 {ECO:0000244|PDB:1AXD}.
STRAND 63 67 {ECO:0000244|PDB:1AXD}.
HELIX 68 79 {ECO:0000244|PDB:1AXD}.
HELIX 81 84 {ECO:0000244|PDB:1AXD}.
TURN 85 87 {ECO:0000244|PDB:1AXD}.
HELIX 89 104 {ECO:0000244|PDB:1AXD}.
HELIX 106 117 {ECO:0000244|PDB:1AXD}.
HELIX 119 122 {ECO:0000244|PDB:1AXD}.
HELIX 129 152 {ECO:0000244|PDB:1AXD}.
STRAND 154 160 {ECO:0000244|PDB:1AXD}.
HELIX 163 166 {ECO:0000244|PDB:1AXD}.
HELIX 169 175 {ECO:0000244|PDB:1AXD}.
HELIX 179 186 {ECO:0000244|PDB:1AXD}.
HELIX 188 199 {ECO:0000244|PDB:1AXD}.
HELIX 201 209 {ECO:0000244|PDB:1AXD}.
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


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