MULTISPECIES: bifunctional thioredoxin/glutathione peroxidase

LOCUS       WP_001154168             183 aa            linear   BCT 16-DEC-2020
            [Enterobacteriaceae].
ACCESSION   WP_001154168
VERSION     WP_001154168.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 183)
  AUTHORS   Arenas,F.A., Diaz,W.A., Leal,C.A., Perez-Donoso,J.M., Imlay,J.A.
            and Vasquez,C.C.
  TITLE     The Escherichia coli btuE gene, encodes a glutathione peroxidase
            that is induced under oxidative stress conditions
  JOURNAL   Biochem. Biophys. Res. Commun. 398 (4), 690-694 (2010)
   PUBMED   20621065
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.
            REFSEQ INFORMATION: The reference sequence is identical to P06610.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR010964
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..183
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..183
                     /gene="btuE"
     Protein         1..183
                     /product="bifunctional thioredoxin/glutathione peroxidase"
                     /EC_number="1.11.1.9"
                     /calculated_mol_wt=20338
     Region          1..183
                     /region_name="btuE"
                     /note="putative glutathione peroxidase; Provisional;
                     PRK10606"
                     /db_xref="CDD:182585"
     Site            order(37,71,145)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:238207"
     Site            order(70,73,75,78,81,85)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238207"
ORIGIN      
        1 mqdsilttvv kdidgevttl ekfagnvlli vnvaskcglt pqyeqleniq kawvdrgfmv
       61 lgfpcnqfle qepgsdeeik tyctttwgvt fpmfskievn gegrhplyqk liaaaptava
      121 peesgfyarm vskgraplyp ddilwnfekf lvgrdgkviq rfspdmtped pivmesikla
      181 lak