ID   PDXK_ECOUT              Reviewed;         283 AA.
AC   Q1R8V2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
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=UTI89_C2752;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE08212.1; -; Genomic_DNA.
DR   RefSeq; YP_541743.1; -.
DR   SMR; Q1R8V2; 2-280.
DR   GeneID; 3989917; -.
DR   GenomeReviews; CP000243_GR; UTI89_C2752.
DR   KEGG; eci:UTI89_C2752; -.
DR   HOGENOM; Q1R8V2; -.
DR   OMA; Q1R8V2; ACICNEL.
DR   BioCyc; ECOL364106:UTI89_C2752-MON; -.
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    283       Pyridoxine kinase.
FT                                /FTId=PRO_0000268835.
FT   NP_BIND     195    196       ATP (By similarity).
FT   NP_BIND     220    232       ATP (By similarity).
FT   BINDING      23     23       Substrate (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     233    233       Substrate (By similarity).
SQ   SEQUENCE   283 AA;  30848 MW;  303C85C8DEDA369D CRC64;
     MSSLLLFNDK SRALQADIVA VQSQVVYGSV GNSIAVPAIK QNGLNVFAVP TVLLSNTPHY
     DTFYGGAIPD EWFSGYLRAL QERDALRQLR AVTTGYMGTA SQIKILAEWL TALRKDHPDL
     LIMVDPVIGD IDSGIYVKPD LPEAYRQYLL PLAQGITPNI FELEILTGKD CRDLDSAIAA
     AKSLLSDTLK WVVITSASGN EENQEMQVVV VSADSVNVIS HSRVKTDLKG TGDLFCAQLI
     SGLLKGKALT DAVHRAGLRV LEVMRYTQQH ESDELILPPL AEA
//