ID   PDXK_RALME              Reviewed;         288 AA.
AC   Q1LFU5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=Rmet_4114;
OS   Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839).
OG   Plasmid megaplasmid.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Mergeay M., Benotmane M.A.,
RA   Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of the megaplasmid of Ralstonia metallidurans
RT   CH34.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000353; ABF10981.1; -; Genomic_DNA.
DR   RefSeq; YP_586250.1; -.
DR   GeneID; 4040972; -.
DR   GenomeReviews; CP000353_GR; Rmet_4114.
DR   KEGG; rme:Rmet_4114; -.
DR   HOGENOM; Q1LFU5; -.
DR   OMA; Q1LFU5; ACICNEL.
DR   BioCyc; RMET266264:RMET_4114-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; IPR011611; Carb/pur_kinase.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF00294; PfkB; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Plasmid; Transferase; Zinc.
FT   CHAIN         1    288       Pyridoxine kinase.
FT                                /FTId=PRO_0000268839.
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   288 AA;  30799 MW;  C2410E0E277F9EA2 CRC64;
     MFGETGTGDA LRPIFMDVVS VQSQVVYGHV GNNVALPTLR AHGLNVAAVP TVMFSNTPHY
     PTLHGGALPI DWFGGYLSDL SARGALQRLK AILVGYLGNP EQVAVLSRWI NQVLAEHPDV
     QVIVDPVIGD HDTGIYVADG MVEAVRELLL PLAHGLTPND FELGHLSGRS ADSVEQVVAA
     ARSLLTDRVQ WMVVTSAAPG TWGHDDMKLL IVTRDDAQVL SHPRIPVSPK GTGDLFSAKL
     TARLLEGMPL AEAAASASDH VVTALEATRR AQSLELQLPS NPCITHRE
//