sugar kinase [Escherichia coli].

LOCUS       WP_001302823             310 aa            linear   BCT 01-JAN-2025
ACCESSION   WP_001302823
VERSION     WP_001302823.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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..310
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..310
                     /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=33329
     Region          5..292
                     /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(42..43,46,98,112,114,142,173,252,255,291)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238571"
     Site            order(222,227,242,252..254,257,279,283)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238571"
ORIGIN      
        1 mdnldvicig aaivdiplqp vsknifdvds ypleriamtt ggdaineati isrlghctal
       61 msrigkdaag qfildhcrke nidiqslkqd vnidtsinvg lvtedgertf vtnrngslwk
      121 lniddvdfar fsqakllsla sifnsplldg kalteiftqa karqmnicad mikprlnetl
      181 ddicealsyv nyaeaklltg ketldeiads flacgvktvv iktgkdgcfi krgdmtmkvp
      241 avagitaidt igagdnfasg fiaallegkn lrecarfana taaisvlsvg attgvknrkl
      301 veqlleeyeg