MULTISPECIES: pyridoxine/pyridoxal/pyridoxamine kinase [Listeria].

LOCUS       WP_003721779             271 aa            linear   BCT 19-AUG-2020
ACCESSION   WP_003721779
VERSION     WP_003721779.1
KEYWORDS    RefSeq.
SOURCE      Listeria
  ORGANISM  Listeria
            Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae.
REFERENCE   1  (residues 1 to 271)
  AUTHORS   Newman,J.A., Das,S.K., Sedelnikova,S.E. and Rice,D.W.
  TITLE     Cloning, purification and preliminary crystallographic analysis of
            a putative pyridoxal kinase from Bacillus subtilis
  JOURNAL   Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (Pt 10),
            1006-1009 (2006)
   PUBMED   17012797
REFERENCE   2  (residues 1 to 271)
  AUTHORS   Park,J.H., Burns,K., Kinsland,C. and Begley,T.P.
  TITLE     Characterization of two kinases involved in thiamine pyrophosphate
            and pyridoxal phosphate biosynthesis in Bacillus subtilis:
            4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal
            kinase
  JOURNAL   J. Bacteriol. 186 (5), 1571-1573 (2004)
   PUBMED   14973012
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 :: NF009077.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK12412
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..271
                     /organism="Listeria"
                     /db_xref="taxon:1637"
     gene            1..271
                     /gene="pdxK"
     Protein         1..271
                     /product="pyridoxine/pyridoxal/pyridoxamine kinase"
                     /GO_function="GO:0008972 - phosphomethylpyrimidine kinase
                     activity [Evidence IEA]"
                     /GO_process="GO:0009228 - thiamine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=28688
     Region          3..267
                     /region_name="ribokinase_pfkB_like"
                     /note="ribokinase/pfkB superfamily: Kinases that accept a
                     wide variety of substrates, including carbohydrates and
                     aromatic small molecules, all are phosphorylated at a
                     hydroxyl group. The superfamily includes ribokinase,
                     fructokinase, ketohexokinase; cl00192"
                     /db_xref="CDD:469648"
     Site            order(5,12,14..15,17,21,24..25,28,31..36,38,41..45,52..53,
                     55,57..58,61,64,68..69)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238574"
     Site            order(11,23,44,82,216)
                     /site_type="other"
                     /note="substrate binding site [chemical binding]"
                     /db_xref="CDD:238574"
     Site            order(107,144,178,213,215)
                     /site_type="other"
                     /note="ATP binding site [chemical binding]"
                     /db_xref="CDD:238574"
ORIGIN      
        1 mtikktltia gsdssggagl qadlktfeey gtygfsaitt ivtmdpdnnw ahgvtpidaq
       61 lvreqlktil sggpvdamkt gmlgsieiik atreaidkyd lknvvidpvm vckgedeliq
      121 penaeairdl llpkatittp nlfeagqlsg lgklttlddm kaaakkiiel gakyvvikgg
      181 kalesdkaid llydgkefti yevekispsh nhgagctfaa aitaglakgl tveeavakak
      241 dfvtaaikgg falnefigpv whgaynkaen r