ID   PDXK_STAAC              Reviewed;         276 AA.
AC   Q5HI96;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Putative pyridoxine kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=PN/PL/PM kinase;
DE   AltName: Full=Pyridoxal kinase;
DE   AltName: Full=Pyridoxamine kinase;
DE   AltName: Full=Vitamin B6 kinase;
GN   Name=pdxK; OrderedLocusNames=SACOL0626;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage pathway.
CC       Uses pyridoxal, pyridoxine, and pyridoxamine as substrates (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC         EC=2.7.1.35;
CC   -!- SIMILARITY: Belongs to the ThiD family. {ECO:0000305}.
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DR   EMBL; CP000046; AAW37735.1; -; Genomic_DNA.
DR   RefSeq; WP_001185462.1; NC_002951.2.
DR   AlphaFoldDB; Q5HI96; -.
DR   SMR; Q5HI96; -.
DR   EnsemblBacteria; AAW37735; AAW37735; SACOL0626.
DR   KEGG; sac:SACOL0626; -.
DR   HOGENOM; CLU_020520_0_0_9; -.
DR   OMA; KDEVGYA; -.
DR   Proteomes; UP000000530; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01169; HMPP_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR045029; HMP/HMP-P_kinase.
DR   InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR20858; PTHR20858; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00097; HMP-P_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..276
FT                   /note="Putative pyridoxine kinase"
FT                   /id="PRO_0000192027"
FT   BINDING         139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         176..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29857 MW;  62C5F054E4D56779 CRC64;
     MALKKVLTIA GSDTSAGAGM QADLKTFQEL DTYGMVALTA IVTMDKDTWS HDVTPLPMDV
     FEKQLETALS IGPDAIKTGM LGTEEIIKRA GEVYEASNAQ YFVVDPVMVC KGEDEVLNPG
     NTEAMIKYLL PKATVVTPNL FEAGQLSGLG KLNSIEDMKK AATIIFDKGA QHVIIKGGKA
     LDQDKSYDLY YDGQTFYQLT TDMFQQSYNH GAGCTFAAAT TAYLANGKSP KEAVISAKAF
     VASAIKNGWK MNDFVGPVDH GAYNRIEHID VEVTEV