type I pantothenate kinase [Klebsiella pneumoniae].

LOCUS       WP_004220326             288 aa            linear   BCT 29-APR-2021
ACCESSION   WP_004220326
VERSION     WP_004220326.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 288)
  AUTHORS   Song,W.J. and Jackowski,S.
  TITLE     Kinetics and regulation of pantothenate kinase from Escherichia
            coli
  JOURNAL   J Biol Chem 269 (43), 27051-27058 (1994)
   PUBMED   7929447
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 :: TIGR00554.2
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..288
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     gene            1..288
                     /gene="coaA"
     Protein         1..288
                     /product="type I pantothenate kinase"
                     /EC_number="2.7.1.33"
                     /GO_function="GO:0004594 - pantothenate kinase activity
                     [Evidence IEA]"
                     /GO_process="GO:0015937 - coenzyme A biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32738
     Region          1..288
                     /region_name="NK"
                     /note="Nucleoside/nucleotide kinase (NK) is a protein
                     superfamily consisting of multiple families of enzymes
                     that share structural similarity and are functionally
                     related to the catalysis of the reversible phosphate group
                     transfer from nucleoside triphosphates...; cl17190"
                     /db_xref="CDD:450170"
     Site            order(70,73..76,211,215,275,279)
                     /site_type="other"
                     /note="ATP-binding site [chemical binding]"
                     /db_xref="CDD:238983"
     Site            order(73..74,78,149,215,219,279)
                     /site_type="other"
                     /note="CoA-binding site [chemical binding]"
                     /db_xref="CDD:238983"
     Site            order(74,171)
                     /site_type="other"
                     /note="Mg2+-binding site [ion binding]"
                     /db_xref="CDD:238983"
ORIGIN      
        1 mtlteeeitr lkginedlsl eevaeiylpl srllnfyiss nlrrqavleq flgtngqrip
       61 yiisiagsva vgksttarvl qallsrwpeh rhvelittdg flhpnsvlke rglmkkkgfp
      121 qsydmhrlvk fvsdlksgvp qatapvyshl iydvipngdk tvaqpdilil eglnvlqsgm
      181 dyphdphhvf vsdfvdfsiy vdapeellks wyinrflkfr egaftdpdsy fhnyaklske
      241 eavdiatslw neinlmnlke nilptreras limtksanhs vnqvrlrk