MULTISPECIES: 2-dehydro-3-deoxy-6-phosphogalactonate aldolase

LOCUS       WP_001198722             205 aa            linear   BCT 16-DEC-2020
            [Enterobacteriaceae].
ACCESSION   WP_001198722
VERSION     WP_001198722.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 205)
  AUTHORS   Walters,M.J., Srikannathasan,V., McEwan,A.R., Naismith,J.H.,
            Fierke,C.A. and Toone,E.J.
  TITLE     Characterization and crystal structure of Escherichia coli KDPGal
            aldolase
  JOURNAL   Bioorg. Med. Chem. 16 (2), 710-720 (2008)
   PUBMED   17981470
REFERENCE   2  (residues 1 to 205)
  AUTHORS   Deacon,J. and Cooper,R.A.
  TITLE     D-Galactonate utilisation by enteric bacteria. The catabolic
            pathway in Escherichia coli
  JOURNAL   FEBS Lett. 77 (2), 201-205 (1977)
   PUBMED   324806
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  :: BlastRule
            Evidence Accession :: NBR011119
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..205
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..205
                     /gene="dgoA"
     Protein         1..205
                     /product="2-dehydro-3-deoxy-6-phosphogalactonate aldolase"
                     /EC_number="4.1.2.21"
                     /calculated_mol_wt=21260
     Region          1..203
                     /region_name="PRK09140"
                     /note="2-dehydro-3-deoxy-6-phosphogalactonate aldolase;
                     Reviewed"
                     /db_xref="CDD:181670"
     Site            order(12,37,41,66,126,128,154)
                     /site_type="active"
                     /db_xref="CDD:188632"
     Site            order(41,66,68,87..90,110..113,115,119,128..129,140,
                     144..145)
                     /site_type="other"
                     /note="intersubunit interface [polypeptide binding]"
                     /db_xref="CDD:188632"
     Site            126
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188632"
ORIGIN      
        1 mqwqtklpli ailrgitpde alahvgavid agfdaveipl nspqweqsip aivdaygdka
       61 ligagtvlkp eqvdalarmg cqlivtpnih sevirravgy gmtvcpgcat ateaftalea
      121 gaqalkifps safgpqyika lkavlpsdia vfavggvtpe nlaqwidagc agaglgsdly
      181 ragqsverta qqaaafvkay reavq