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Glutathione S-transferase 3 (EC 2.5.1.18) (GST class-phi member 3) (GST-III)

 GSTF3_MAIZE             Reviewed;         222 AA.
P04907; P15542;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 112.
RecName: Full=Glutathione S-transferase 3;
EC=2.5.1.18;
AltName: Full=GST class-phi member 3;
AltName: Full=GST-III;
Name=GST3;
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 [MRNA].
PubMed=3532034; DOI=10.1093/nar/14.18.7227;
Moore R.E., Davies M.S., O'Connell K.M., Harding E.I., Wiegand R.C.,
Tiemeier D.C.;
"Cloning and expression of a cDNA encoding a maize glutathione-S-
transferase in E. coli.";
Nucleic Acids Res. 14:7227-7235(1986).
[3]
PROTEIN SEQUENCE OF 143-153.
TISSUE=Coleoptile;
AGRICOLA=IND20551642; DOI=10.1007/BF00224104;
Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C.,
Pernollet J.-C., Zivy M., de Vienne D.;
"The maize two dimensional gel protein database: towards an integrated
genome analysis program.";
Theor. Appl. Genet. 93:997-1005(1996).
-!- 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.
-!- SIMILARITY: Belongs to the GST superfamily. Phi family.
{ECO:0000305}.
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EMBL; X06755; CAA29929.1; -; mRNA.
EMBL; X04375; CAA27957.1; -; mRNA.
EMBL; X04455; CAA28053.1; -; mRNA.
PIR; A24703; XUZM31.
PIR; S00717; XUZM32.
UniGene; Zm.103282; -.
UniGene; Zm.103382; -.
UniGene; Zm.93693; -.
ProteinModelPortal; P04907; -.
SMR; P04907; -.
PRIDE; P04907; -.
MaizeGDB; 65344; -.
HOGENOM; HOG000125746; -.
Proteomes; UP000007305; Unplaced.
GO; GO:0043234; C:protein complex; NAS:AgBase.
GO; GO:0004364; F:glutathione transferase activity; IDA:AgBase.
GO; GO:0042803; F:protein homodimerization activity; NAS:AgBase.
GO; GO:0009635; P:response to herbicide; IDA:AgBase.
CDD; cd03187; GST_C_Phi; 1.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR034347; GST_Phi_C.
InterPro; IPR036249; Thioredoxin-like_sf.
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;
Complete proteome; Direct protein sequencing; Reference proteome;
Transferase.
INIT_MET 1 1 Removed.
CHAIN 2 222 Glutathione S-transferase 3.
/FTId=PRO_0000185842.
DOMAIN 2 83 GST N-terminal.
DOMAIN 89 219 GST C-terminal.
REGION 41 42 Glutathione binding. {ECO:0000250}.
REGION 54 55 Glutathione binding. {ECO:0000250}.
REGION 67 68 Glutathione binding. {ECO:0000250}.
BINDING 12 12 Glutathione. {ECO:0000250}.
CONFLICT 108 108 H -> Y (in Ref. 2). {ECO:0000305}.
CONFLICT 111 127 ASPLVFQLLVRPLLGGA -> RVAAGVPAAREAAPGRR
(in Ref. 2; CAA27957/CAA28053).
{ECO:0000305}.
CONFLICT 134 134 E -> D (in Ref. 2; CAA27957/CAA28053).
{ECO:0000305}.
CONFLICT 149 180 AHLARNKYLAGDEFTLADANHALLPALTSARP -> RTSPA
TSTSPGTSSRSPTPTTRSYLLYLSKT (in Ref. 2;
CAA27957). {ECO:0000305}.
CONFLICT 184 189 GCVAAR -> ARRRP (in Ref. 2; CAA27957).
{ECO:0000305}.
CONFLICT 200 200 A -> V (in Ref. 2; CAA27957/CAA28053).
{ECO:0000305}.
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


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