ID O24595_MAIZE Unreviewed; 224 AA.
AC O24595; A0A317Y1J7;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 24-JAN-2024, entry version 117.
DE RecName: Full=Glutathione S-transferase {ECO:0000256|RuleBase:RU369102};
DE EC=2.5.1.18 {ECO:0000256|RuleBase:RU369102};
GN Name=GST5 {ECO:0000313|EMBL:CAA73369.1};
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 {ECO:0000313|EMBL:CAA73369.1};
RN [1] {ECO:0000313|EMBL:CAA73369.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=9484464; DOI=10.1023/A:1005958711207;
RA Dixon D.P., Cole D.J., Edwards R.;
RT "Purification, regulation and cloning of a glutathione transferase (GST)
RT from maize resembling the auxin-inducible type-III GSTs.";
RL Plant Mol. Biol. 36:75-87(1998).
CC -!- FUNCTION: Is involved in the conjugation of reduced glutathione to a
CC wide number of exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000256|RuleBase:RU369102}.
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 Evidence={ECO:0000256|ARBA:ARBA00000710,
CC ECO:0000256|RuleBase:RU369102};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU369102}.
CC -!- SIMILARITY: Belongs to the GST superfamily.
CC {ECO:0000256|RuleBase:RU369102}.
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DR EMBL; Y12862; CAA73369.1; -; mRNA.
DR PIR; T04358; T04358.
DR AlphaFoldDB; O24595; -.
DR SMR; O24595; -.
DR ExpressionAtlas; O24595; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:AgBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:AgBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR CDD; cd03185; GST_C_Tau; 1.
DR CDD; cd03058; GST_N_Tau; 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; IPR045074; GST_C_Tau.
DR InterPro; IPR045073; Omega/Tau-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11260:SF732; GLUTATHIONE S-TRANSFERASE GSTU1-RELATED; 1.
DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|RuleBase:RU369102};
KW Transferase {ECO:0000256|RuleBase:RU369102, ECO:0000313|EMBL:CAA73369.1}.
SQ SEQUENCE 224 AA; 25119 MW; E5C39DC4BD535D4A CRC64;
MAEEKKQGLQ LLDFWVSPFG QRCRIAMDEK GLAYEYLEQD LGNKSELLLR ANPVHKKIPV
LLHDGRPVCE SLVIVQYLDE AFPAAAPALL PADPYARAQA RFWADYVDKK LYDCGTRLWK
LKGDGQAQAR AEMVEILRTL EGALGDGPFF GGDALGFVDV ALVPFTSWFL AYDRFGGVSV
EKECPRLAAW AKRCAERPSV AKNLYPPEKV YDFVCGMKKR LGIE
//
