MULTISPECIES: ribokinase [Enterobacteriaceae].

LOCUS       WP_001300603             309 aa            linear   BCT 16-DEC-2020
ACCESSION   WP_001300603
VERSION     WP_001300603.1
KEYWORDS    RefSeq.
SOURCE      Enterobacteriaceae
  ORGANISM  Enterobacteriaceae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales.
REFERENCE   1  (residues 1 to 309)
  AUTHORS   Paul,R., Patra,M.D. and Sen,U.
  TITLE     Crystal structure of apo and ligand bound vibrio cholerae
            ribokinase (Vc-RK): role of monovalent cation induced activation
            and structural flexibility in sugar phosphorylation
  JOURNAL   Adv. Exp. Med. Biol. 842, 293-307 (2015)
   PUBMED   25408351
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  :: HMM
            Evidence Accession :: NF008353.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK11142
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..309
                     /organism="Enterobacteriaceae"
                     /db_xref="taxon:543"
     gene            1..309
                     /gene="rbsK"
     Protein         1..309
                     /product="ribokinase"
                     /EC_number="2.7.1.15"
                     /GO_function="GO:0004747 - ribokinase activity [Evidence
                     IEA]"
                     /GO_process="GO:0006014 - D-ribose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32159
     Region          4..308
                     /region_name="PRK11142"
                     /note="ribokinase; Provisional"
                     /db_xref="CDD:236858"
     Site            order(14,16,41..43,46,98,100,110,112,143,251..252,255,291)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238579"
     Site            order(17,19,24..30,43,97,99..101,107..114,169)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238579"
     Site            order(187,223..225,228,241,247,250,253..254,257,279,
                     282..283,286)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238579"
ORIGIN      
        1 mqnagslvvl gsinadhiln lqsfptpget vtgnhyqvaf ggkganqava agrsganiaf
       61 iactgddsig esvrqqlatd niditpvsvi kgestgvali fvngegenvi gihaganaal
      121 spalveaqre rianasallm qlesplesvm aaakiahqnk tivalnpapa relpdellal
      181 vdiitpnete aekltgirve ndedaakaaq vlhekgirtv litlgsrgvw asvngegqrv
      241 pgfrvqavdt iaagdtfnga litalleekp lpeairfaha aaaiavtrkg aqpsvpwree
      301 idafldrqr