MULTISPECIES: 2-dehydro-3-deoxygluconokinase [Enterobacteriaceae].

LOCUS       WP_001301733             309 aa            linear   BCT 03-DEC-2023
ACCESSION   WP_001301733
VERSION     WP_001301733.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Ohshima,N., Inagaki,E., Yasuike,K., Takio,K. and Tahirov,T.H.
  TITLE     Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase:
            evidence for recognition of an open chain substrate
  JOURNAL   J. Mol. Biol. 340 (3), 477-489 (2004)
   PUBMED   15210349
REFERENCE   2  (residues 1 to 309)
  AUTHORS   Inagaki,E., Ukita,Y., Kumei,M., Kajihara,Y. and Tahirov,T.H.
  TITLE     Crystallization and preliminary crystallographic analysis of
            2-keto-3-deoxygluconate kinase from Thermus thermophilus
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 60 (Pt 4), 761-763 (2004)
   PUBMED   15039578
REFERENCE   3  (residues 1 to 309)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Condemine,G., Nasser,W. and
            Reverchon,S.
  TITLE     Regulation of pectinolysis in Erwinia chrysanthemi
  JOURNAL   Annu. Rev. Microbiol. 50, 213-257 (1996)
   PUBMED   8905080
REFERENCE   4  (residues 1 to 309)
  AUTHORS   Hugouvieux-Cotte-Pattat,N., Nasser,W. and Robert-Baudouy,J.
  TITLE     Molecular characterization of the Erwinia chrysanthemi kdgK gene
            involved in pectin degradation
  JOURNAL   J. Bacteriol. 176 (8), 2386-2392 (1994)
   PUBMED   8157608
REFERENCE   5  (residues 1 to 309)
  AUTHORS   Pouyssegur,J. and Stoeber,F.
  TITLE     [Study of the common degradative pathway of hexuronates in
            Escherichia coli K 12. Purification, properties and individuality
            of 2-keto-3-deoxy-D-gluconnokinase]
  JOURNAL   Biochimie 53 (6), 771-781 (1971)
   PUBMED   4944816
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 :: NBR008619
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..309
                     /gene="kdgK"
     Protein         1..309
                     /product="2-dehydro-3-deoxygluconokinase"
                     /EC_number="2.7.1.45"
                     /calculated_mol_wt=33816
     Region          4..301
                     /region_name="KdgK"
                     /note="2-keto-3-deoxygluconate kinase (KdgK)
                     phosphorylates 2-keto-3-deoxygluconate (KDG) to form
                     2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the
                     common intermediate product, that allows organisms to
                     channel D-glucuronate and/or D-galacturinate into the...;
                     cd01166"
                     /db_xref="CDD:238571"
     Site            order(28..29,32,88,102,104,136,170,261,264,300)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(228,233,252,261..263,266,288,292)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mskkiavige cmielsekga dvkrgfggdt lntsvyiarq vdpaaltvhy vtalgtdsfs
       61 qqmldawhge nvdtsltqrm enrlpglyyi etdstgertf yywrneaaak fwlesdqsaa
      121 iceelanfdy lylsgislai lsptsrekll sllrecrang gkvifdnnyr prlwaskeet
      181 qqvyqqmlec tdiafltldd edalwgqqpv edviarthna gvkevvvkrg adsclvsiag
      241 eglvdvpavk lpkekvidtt aagdsfsagy lavrltggsa enaakrghlt astviqyrga
      301 iipreampa