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Database: UniProt
Entry: C6F762_PSEMZ
LinkDB: C6F762_PSEMZ
Original site: C6F762_PSEMZ 
ID   C6F762_PSEMZ            Unreviewed;       115 AA.
AC   C6F762;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE   Flags: Fragment;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357 {ECO:0000313|EMBL:ACH61673.1};
RN   [1] {ECO:0000313|EMBL:ACH61673.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=28-4 {ECO:0000313|EMBL:ACH61673.1};
RX   PubMed=19596906; DOI=10.1534/genetics.109.103895;
RA   Eckert A.J., Wegrzyn J.L., Pande B., Jermstad K.D., Lee J.M., Liechty J.D.,
RA   Tearse B.R., Krutovsky K.V., Neale D.B.;
RT   "Multilocus patterns of nucleotide diversity and divergence reveal positive
RT   selection at candidate genes related to cold hardiness in coastal Douglas
RT   Fir (Pseudotsuga menziesii var. menziesii).";
RL   Genetics 183:289-298(2009).
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};
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DR   EMBL; EU864945; ACH61673.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6F762; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   GO; GO:0042221; P:response to chemical; IEA:UniProt.
DR   CDD; cd03185; GST_C_Tau; 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; IPR045074; GST_C_Tau.
DR   InterPro; IPR045073; Omega/Tau-like.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11260:SF781; GLUTATHIONE S-TRANSFERASE U22; 1.
DR   PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:ACH61673.1}.
FT   DOMAIN          1..38
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          45..115
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACH61673.1"
FT   NON_TER         115
FT                   /evidence="ECO:0000313|EMBL:ACH61673.1"
SQ   SEQUENCE   115 AA;  12811 MW;  F7B6B62D28219C9D CRC64;
     LQSNPVHKKI PVLIHNGKPV CESMIIVQYI DEAWDTMSPN LMPKNPYDRA IARFWSAFVD
     DKLVPSFQEV FKGQGKQLQR AVEESVANFL LLEEALRTSS SSGKAYFGGD GIGLV
//
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