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Database: UniProt
Entry: A7UHA4_9POAL
LinkDB: A7UHA4_9POAL
Original site: A7UHA4_9POAL 
ID   A7UHA4_9POAL            Unreviewed;       229 AA.
AC   A7UHA4;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   08-NOV-2023, entry version 56.
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:ABU56005.1};
OS   Dasypyrum villosum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Dasypyrum.
OX   NCBI_TaxID=40247 {ECO:0000313|EMBL:ABU56005.1};
RN   [1] {ECO:0000313|EMBL:ABU56005.1}
RP   NUCLEOTIDE SEQUENCE.
RA   He H.G., Gao A.L., Wang X.E., Chen P.D.;
RT   "Cloning and expression analysis of a glutathione S-transferase gene from
RT   Haynaldia villosa.";
RL   Submitted (JUL-2007) 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   -!- SIMILARITY: Belongs to the GST superfamily. Phi family.
CC       {ECO:0000256|ARBA:ARBA00010128}.
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DR   EMBL; EU070904; ABU56005.1; -; mRNA.
DR   AlphaFoldDB; A7UHA4; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042221; P:response to chemical; 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:SF76; GLUTATHIONE S-TRANSFERASE 1; 1.
DR   PANTHER; PTHR43900; GLUTATHIONE S-TRANSFERASE RHO; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000313|EMBL:ABU56005.1}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..229
FT                   /note="glutathione transferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002713665"
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          93..221
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   229 AA;  25624 MW;  4EE16E89902EAF72 CRC64;
     MSPMKVFGHP MLTNVARVLL FLEEVGAEYE LVPVDFVAGE HKKPQHLQLN PFGKMPGFQD
     GDLVLFESRA IGKYIIRKYG GTAGLDLLGE NSGIEGSAMV DLWTEVEAQE YYPAIAPVVF
     ECIINPFIMG DAETNQSVVD ESLVRLRGVL GIYEARLEKS SYLAGDSISF ADLNHIPFTF
     YFMTTQYASV FDEYPKVKAW WEAIMARPAV QRVCKNMPTQ FSVGMRAAF
//
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