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Database: UniProt
Entry: D1FK70_PTEVI
LinkDB: D1FK70_PTEVI
Original site: D1FK70_PTEVI 
ID   D1FK70_PTEVI            Unreviewed;       217 AA.
AC   D1FK70;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
GN   Name=GST2 {ECO:0000313|EMBL:ABY84871.1};
OS   Pteris vittata (Chinese ladder brake).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Pteridoideae; Pteris; Pteris subgen. Pteris; Pteris sect. Pteris.
OX   NCBI_TaxID=13821 {ECO:0000313|EMBL:ABY84871.1};
RN   [1] {ECO:0000313|EMBL:ABY84871.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Csonka L.N., Khan A., Ellis D.R., Salt D.E.;
RT   "Isolation of Glutathione-S-Transferases from the Arsenic Hyperaccumulator
RT   Fern Pteris vittata that Increase Arsenate Resistance in Escherichia
RT   coli.";
RL   Submitted (NOV-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; EU259320; ABY84871.1; -; mRNA.
DR   AlphaFoldDB; D1FK70; -.
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; 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; SFLDG01154; Main.5:_Phi-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   Transferase {ECO:0000313|EMBL:ABY84871.1}.
FT   DOMAIN          1..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..217
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   217 AA;  24515 MW;  D5FBEB5A5473C60B CRC64;
     MTITVHGQAT SSCTQRVLTT LFEKDVSDFQ LLHVDLSTGA HKQPEYLALQ PFGVIPVVQD
     GDLTIFESRA IIRYLALKYE DQGSPLYGRT LEERANVEQW LEVESQNFHV AASAIVNQLS
     SRAKKGLPPE EGVVKTNMEK LEAILDVYEK RLSESSFLAG DFFSLADLSH LPRTKSLVKS
     CKLPHLITSR KHVHEWWQRI STRPSWIKVI EMAAPSK
//
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