LOCUS       WP_014900175             220 aa            linear   BCT 31-DEC-2024
DEFINITION  glutathione S-transferase family protein [Burkholderia cepacia].
ACCESSION   WP_014900175
VERSION     WP_014900175.1
KEYWORDS    RefSeq.
SOURCE      Burkholderia cepacia
  ORGANISM  Burkholderia cepacia
            Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
            Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia
            cepacia complex.
REFERENCE   1  (residues 1 to 220)
  AUTHORS   Frova,C.
  TITLE     Glutathione transferases in the genomics era: new insights and
            perspectives
  JOURNAL   Biomol Eng 23 (4), 149-169 (2006)
   PUBMED   16839810
REFERENCE   2  (residues 1 to 220)
  AUTHORS   Hayes,J.D., Flanagan,J.U. and Jowsey,I.R.
  TITLE     Glutathione transferases
  JOURNAL   Annu Rev Pharmacol Toxicol 45, 51-88 (2005)
   PUBMED   15822171
REFERENCE   3  (residues 1 to 220)
  AUTHORS   Armstrong,R.N.
  TITLE     Structure, catalytic mechanism, and evolution of the glutathione
            transferases
  JOURNAL   Chem Res Toxicol 10 (1), 2-18 (1997)
   PUBMED   9074797
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122607
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..220
                     /organism="Burkholderia cepacia"
                     /db_xref="taxon:292"
     Protein         1..220
                     /product="glutathione S-transferase family protein"
                     /EC_number="2.5.1.-"
                     /GO_function="GO:0004364 - glutathione transferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006749 - glutathione metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=24621
     Region          8..79
                     /region_name="GST_N_1"
                     /note="GST_N family, unknown subfamily 1; composed of
                     uncharacterized proteins, predominantly from bacteria,
                     with similarity to GSTs. GSTs are cytosolic dimeric
                     proteins involved in cellular detoxification by catalyzing
                     the conjugation of glutathione (GSH) with...; cd03043"
                     /db_xref="CDD:239341"
     Site            order(19,21..22,24..25,28..29,72,75..76)
                     /site_type="other"
                     /note="putative C-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(19,57..59,70..71)
                     /site_type="other"
                     /note="putative GSH binding site (G-site) [chemical
                     binding]"
                     /db_xref="CDD:239341"
     Site            order(57,69..70,72..73,76)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:239341"
     Region          92..205
                     /region_name="GST_C_3"
                     /note="C-terminal, alpha helical domain of an unknown
                     subfamily 3 of Glutathione S-transferases; cd03194"
                     /db_xref="CDD:198303"
     Site            order(95,102,163,166..167,170,174)
                     /site_type="other"
                     /note="putative N-terminal domain interface [polypeptide
                     binding]"
                     /db_xref="CDD:198303"
     Site            order(95..96,99..100,103,139)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:198303"
     Site            order(102,106..107,110..111,171,174)
                     /site_type="other"
                     /note="putative substrate binding pocket (H-site)
                     [chemical binding]"
                     /db_xref="CDD:198303"
ORIGIN      
        1 mestgpttlt issrnyssws mrgwllakls glafetvsvp idaasraell llspsilvpc
       61 lthegstvwd tlaiaeylne vqpqarllpd drharahcrs icgemhsgfs alrsalpmnl
      121 rahfpgfriw sraqhdieri vtiwreclaa yggpwlfgeq igiadamyap vvtrfltydv
      181 klepdiaeyc mrmlahpfva ewidaakaeh edideldmef
//