MULTISPECIES: ribokinase [Enterobacterales].

LOCUS       WP_004184063             313 aa            linear   BCT 24-FEB-2024
ACCESSION   WP_004184063
VERSION     WP_004184063.1
KEYWORDS    RefSeq.
SOURCE      Enterobacterales
  ORGANISM  Enterobacterales
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
REFERENCE   1  (residues 1 to 313)
  AUTHORS   Cheek,S., Zhang,H. and Grishin,N.V.
  TITLE     Sequence and structure classification of kinases
  JOURNAL   J Mol Biol 320 (4), 855-881 (2002)
   PUBMED   12095261
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 10100282
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..313
                     /organism="Enterobacterales"
                     /db_xref="taxon:91347"
     Protein         1..313
                     /product="ribokinase"
                     /EC_number="2.7.1.15"
                     /GO_function="GO:0005524 - ATP binding [Evidence IEA]"
                     /GO_function="GO:0019200 - carbohydrate kinase activity
                     [Evidence IEA]"
                     /calculated_mol_wt=32070
     Region          4..294
                     /region_name="ribokinase"
                     /note="Ribokinase catalyses the phosphorylation of ribose
                     to ribose-5-phosphate using ATP. This reaction is the
                     first step in the ribose metabolism. It traps ribose
                     within the cell after uptake and also prepares the sugar
                     for use in the synthesis of nucleotides...; cd01174"
                     /db_xref="CDD:238579"
     Site            order(12,14,39..41,44,96,98,109,111,142,250..251,254,290)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238579"
     Site            order(15,17,22..28,41,95,97..99,106..113,168)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238579"
     Site            order(186,222..224,227,240,246,249,252..253,256,278,
                     281..282,285)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238579"
ORIGIN      
        1 msgkvcvfgs fnfdmvarvd rfpvpgeslv acgsmtsagg kganqataal kaganvhyig
       61 kigndtfghf arrhlkgvgf navtllvaee iptgnaliyv agndaenmia vdpganmtvt
      121 ddeiagcipa igcadvvlvq lennlsaieq vidagkqaga lvilnpapwq pvehallrkv
      181 dlltpnatea glmtgrrvds ltaaaeaadv lhaqgarnvi itlgasgall sehgvkspip
      241 cfpshprdtt gagdafngal aarlacgepl qaaarfaaay aavsvekqga sslpeyleaq
      301 erllraaady ema