ID   GSTE_PSEP1              Reviewed;         220 AA.
AC   P82998; A5VWX0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
GN   OrderedLocusNames=Pput_0205;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-21, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11900268; DOI=10.1016/s0923-2508(01)01293-1;
RA   Santos P.M., Mignogna G., Heipieper H.J., Zennaro E.;
RT   "Occurrence and properties of glutathione S-transferases in phenol-
RT   degrading Pseudomonas strains.";
RL   Res. Microbiol. 153:89-98(2002).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles.
CC       {ECO:0000269|PubMed:11900268}.
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:0000269|PubMed:11900268};
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:11900268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11900268}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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; CP000712; ABQ76380.1; -; Genomic_DNA.
DR   AlphaFoldDB; P82998; -.
DR   SMR; P82998; -.
DR   KEGG; ppf:Pput_0205; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_9_3_6; -.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0004364; F:glutathione transferase activity; NAS:UniProtKB.
DR   CDD; cd10424; GST_C_9; 1.
DR   CDD; cd00570; GST_N_family; 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; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43968; -; 1.
DR   PANTHER; PTHR43968:SF15; GLUTATHIONE TRANSFERASE; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Transferase.
FT   CHAIN           1..220
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185982"
FT   DOMAIN          1..77
FT                   /note="GST N-terminal"
FT   DOMAIN          82..211
FT                   /note="GST C-terminal"
FT   BINDING         12
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         49
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..62
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   220 AA;  24476 MW;  8559D8501EDB8A6E CRC64;
     MLKLHGFSVS NYYNMVKLAL LEKGLPFEEV TFYGGQAPQA LEVSPRGKVP VLETEHGFLS
     ETSVILDYIE QTQSGKALLP ADPFEQAKVR ELLKEIELYI ELPARTCYAE SFFGMSVEPL
     IKEKARADLL AGFATLKRNG RFAPYVAGEQ LTLADLMFCF SVDLANAVGK KVLSIDFLAD
     FPQAKALLQL MGENPHMARI MADKEASMPA FMEMIRSGKR
//