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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//