MULTISPECIES: sugar kinase [Klebsiella].

LOCUS       WP_002921921             311 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_002921921
VERSION     WP_002921921.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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 10100205
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..311
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..311
                     /product="sugar kinase"
                     /EC_number="2.7.1.-"
                     /GO_component="GO:0005829 - cytosol [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32984
     Region          5..300
                     /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(36..37,40,92,107,109,138,171,260,263,299)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(229,234,250,260..262,265,287,291)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 menldvitig eamamfvate tgdlaevehf mkrvagaeln vatglarlgl kvgwvsrvgn
       61 dsfgrfvlqs lakegidsha vaidnrfatg fqmkskveng tdpiveyfrk gsaashlspd
      121 dfradyftsa rhlhlsgvaa alsessyall ehaakvmkae gktlsfdpnl rpvlwkseae
      181 mveklnrlaf qadwvlpglk egviltgqqt pegiadfyls rgvkavvikt gcdgawfksa
      241 sgeqgtvdai kvdnvvdtvg agdgfavgvi sallegktll qavnrgnkig slaiqvqgds
      301 eglptrdalg e