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Database: UniProt
Entry: C7F8A3_ARAHY
LinkDB: C7F8A3_ARAHY
Original site: C7F8A3_ARAHY 
ID   C7F8A3_ARAHY            Unreviewed;       218 AA.
AC   C7F8A3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   Name=GST {ECO:0000313|EMBL:ACT82511.1};
GN   ORFNames=Ahy_A06g026173 {ECO:0000313|EMBL:RYR51126.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:ACT82511.1};
RN   [1] {ECO:0000313|EMBL:ACT82511.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu L.S., He N.Y., Yan L.Q.;
RT   "Molecular cloning and characterization of a glutathione S-transferase from
RT   Arachis hypogaea.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RYR51126.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738}, and
RC   GDAAS-fuhuasheng2018 {ECO:0000313|EMBL:RYR51126.1};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR51126.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Phi family.
CC       {ECO:0000256|ARBA:ARBA00010128}.
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DR   EMBL; GQ338321; ACT82511.1; -; mRNA.
DR   EMBL; SDMP01000006; RYR51126.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7F8A3; -.
DR   STRING; 3818.C7F8A3; -.
DR   OrthoDB; 639740at2759; -.
DR   Proteomes; UP000289738; Chromosome a06.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009407; P:toxin catabolic process; IEA:UniProt.
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; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   PANTHER; PTHR43900:SF3; GLUTATHIONE TRANSFERASE; 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   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW   Transferase {ECO:0000313|EMBL:ACT82511.1}.
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          91..218
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   218 AA;  24707 MW;  D633D19838E16868 CRC64;
     MAAVKVYGPT LSTAVSRVLA CLIEKDVQFE VIPVDMSKGE HKRPEFLSLQ PFGQVPVFQD
     GNISLFESRA ICRYVCEKYA ERGNKGLYGT DPLAKASIDQ WVEAEGQSFN PPSSALVFQL
     AFAPRMKLKQ DQGVIRQNEE KLAKVLDVYE KRLSQTRFLA GDDFSLADLS HLPNAHYLVT
     GTDRAPLFTQ RDNVSRWWND ISTRQSWNEV LHLHKTAY
//
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