ID   Q4KED9_PSEF5            Unreviewed;       234 AA.
AC   Q4KED9;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:AAY91560.1};
DE            EC=2.5.1.18 {ECO:0000313|EMBL:AAY91560.1};
GN   OrderedLocusNames=PFL_2287 {ECO:0000313|EMBL:AAY91560.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91560.1, ECO:0000313|Proteomes:UP000008540};
RN   [1] {ECO:0000313|EMBL:AAY91560.1, ECO:0000313|Proteomes:UP000008540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC   {ECO:0000313|Proteomes:UP000008540};
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
RN   [2] {ECO:0007829|PDB:4IKH}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-234 IN COMPLEX WITH
RP   GLUTATHIONE.
RG   Enzyme Function Initiative (EFI);
RA   Vetting M.W., Sauder J.M., Morisco L.L., Wasserman S.R., Sojitra S.,
RA   Imker H.J., Burley S.K., Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of a glutathione transferase family member from
RT   Pseudomonas fluorescens pf-5, target efi-900003, with two glutathione
RT   bound.";
RL   Submitted (DEC-2012) to the PDB data bank.
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; CP000076; AAY91560.1; -; Genomic_DNA.
DR   RefSeq; WP_011060585.1; NC_004129.6.
DR   PDB; 4IKH; X-ray; 2.10 A; A=2-234.
DR   PDBsum; 4IKH; -.
DR   AlphaFoldDB; Q4KED9; -.
DR   SMR; Q4KED9; -.
DR   STRING; 220664.PFL_2287; -.
DR   DNASU; 3475845; -.
DR   KEGG; pfl:PFL_2287; -.
DR   PATRIC; fig|220664.5.peg.2326; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_14_4_6; -.
DR   Proteomes; UP000008540; Chromosome.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03178; GST_C_Ure2p_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_like; 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; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 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   3D-structure {ECO:0007829|PDB:4IKH};
KW   Transferase {ECO:0000313|EMBL:AAY91560.1}.
FT   DOMAIN          18..105
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          108..234
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   BINDING         30
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         30
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         57
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         70
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         71
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         90
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:4IKH"
FT   BINDING         152
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:4IKH"
SQ   SEQUENCE   234 AA;  26348 MW;  97F606301F0C9DBA CRC64;
     MSDLSAFAVT QKWPAQFPEW IQLYSLPTPN GVKVSIMLEE IGLPYEAHRV SFETQDQMTP
     EFLSVSPNNK IPAILDPHGP GDQPLALFES GAILIYLADK SGQLLAQESA ARYETIQWLM
     FQMGGIGPMF GQVGFFNKFA GREYEDKRPL ERYVNEAKRL LGVLDKHLGG REWIMGERYT
     IADIATFPWI RNLIGFYEAG ELVGIDNFPE VKRVLAKFVA RPAVIRGLEI PKVS
//