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Database: UniProt
Entry: E5F6N8_PICSI
LinkDB: E5F6N8_PICSI
Original site: E5F6N8_PICSI 
ID   E5F6N8_PICSI            Unreviewed;       205 AA.
AC   E5F6N8;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE   Flags: Fragment;
OS   Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX   NCBI_TaxID=3332 {ECO:0000313|EMBL:ADP95082.1};
RN   [1] {ECO:0000313|EMBL:ADP95082.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KD400 {ECO:0000313|EMBL:ADP95082.1};
RX   PubMed=20738783; DOI=10.1111/j.1365-294X.2010.04767.x;
RA   Holliday J.A., Yuen M., Ritland K., Aitken S.N.;
RT   "Postglacial history of a widespread conifer produces inverse clines in
RT   selective neutrality tests.";
RL   Mol. Ecol. 19:3857-3864(2010).
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; HM204170; ADP95082.1; -; mRNA.
DR   AlphaFoldDB; E5F6N8; -.
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:ADP95082.1}.
FT   DOMAIN          4..85
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          92..205
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADP95082.1"
FT   NON_TER         205
FT                   /evidence="ECO:0000313|EMBL:ADP95082.1"
SQ   SEQUENCE   205 AA;  22866 MW;  6DA4A55F411E9929 CRC64;
     LVMAVIKLHG HPISTATAMV LCCLNEKEVE YDFALVELSA GAHKQPQYLA LNPFGVVPTI
     QDGDLTLFES RAIVKYLAKK YKGQGADLLG NTLTEQALVE QWCEVEGHSF FPPASTILFQ
     TVLRPLRGGT TDEAVVEINI GKLNKVLDIY EERLSKSKYL AGDFFSLADL QHLPWTQYLV
     TACKKGDLIS SRKHVNAWWE DISSR
//
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