ID   PDXK_BORA1              Reviewed;         296 AA.
AC   Q2L1P5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Pyridoxine kinase;
DE            EC=2.7.1.35;
DE   AltName: Full=Pyridoxal kinase;
DE   AltName: Full=Vitamin B6 kinase;
DE   AltName: Full=Pyridoxamine kinase;
DE   AltName: Full=PN/PL/PM kinase;
GN   Name=pdxK; OrderedLocusNames=BAV1601;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage
CC       pathway. Uses pyridoxal, pyridoxine, and pyridoxamine as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- COFACTOR: Zinc or magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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DR   EMBL; AM167904; CAJ49211.1; -; Genomic_DNA.
DR   RefSeq; YP_786122.1; -.
DR   GeneID; 6265510; -.
DR   GenomeReviews; AM167904_GR; BAV1601.
DR   KEGG; bav:BAV1601; -.
DR   NMPDR; fig|521.1.peg.2726; -.
DR   HOGENOM; Q2L1P5; -.
DR   OMA; Q2L1P5; RARMLVS.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004340; F:glucokinase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01638; -; 1.
DR   InterPro; IPR013749; HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    296       Pyridoxine kinase.
FT                                /FTId=PRO_0000268831.
FT   NP_BIND     195    196       ATP (By similarity).
FT   BINDING      23     23       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     234    234       Substrate (By similarity).
SQ   SEQUENCE   296 AA;  31504 MW;  92AD82068C41703E CRC64;
     MSSGQGYVAS GRPLLFDVVS VQSQVVYGHV GNNVAAPALR AHGLHPGIVP TVLLSNTPHY
     PTLHGGALPL SWFEGYLQDL QARGALQALR AILVGYLGSA EQARVLGRWI ARIREVHPQV
     LVIVDPVMGD DDHGLYVTEG LAEASRECLV PQAHGLTPNS FELGLLTGCE VGRVDQAVAA
     ARRLLAQGLR WVVVTSAAQQ DCPPGQVQLL AVTASQAHLL RHQRVDTAPK GTGDLFCAEL
     TAHLLAGASL ERAVEASSRY LVQALACTRL ADSAELLMPS RDPAQAQAVQ WIPLEN
//