ID   PDXK_SHISS              Reviewed;         283 AA.
AC   Q3YZC3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=SSON_2508;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000038; AAZ89139.1; -; Genomic_DNA.
DR   RefSeq; YP_311374.1; -.
DR   SMR; Q3YZC3; 2-280.
DR   GeneID; 3667660; -.
DR   GenomeReviews; CP000038_GR; SSON_2508.
DR   KEGG; ssn:SSON_2508; -.
DR   HOGENOM; Q3YZC3; -.
DR   OMA; Q3YZC3; ACICNEL.
DR   BioCyc; SSON300269:SSO_2508-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_0000268844.
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;  30860 MW;  902F8C55E5B7804B CRC64;
     MSSLLLFNDK SRALQADIVA VQSQVVYGSV GNSIAVPAIK QNGLNVFAVP TVLLSNTPHY
     DTFYGGAIPD EWFSGYLRAL QERDALRQLR AVTTGYMGTA SQIKILAEWL TALRKDHPDL
     LIMVDPVIGD IDSGIYVKPD LPEAYRQYLL PLAQGITPNI FELEILTGKN CRDLDSAIAA
     AKSLLSDTLK WVVITSASGN EENQEMQVVV VSADSVNVIS HSRVKTDLKG TGDLFCAQLI
     SGLLKGKALN DAVHRAGLRV LEVMRYTQQH ESDELILPPL AEA
//