ID   PDXY_BURTA              Reviewed;         287 AA.
AC   Q2SXQ4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=BTH_I1763;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage
CC       pathway. Uses pyridoxamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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DR   EMBL; CP000086; ABC37853.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_442295.1; -.
DR   GeneID; 3850009; -.
DR   GenomeReviews; CP000086_GR; BTH_I1763.
DR   KEGG; bte:BTH_I1763; -.
DR   TIGR; BTH_I1763; -.
DR   HOGENOM; Q2SXQ4; -.
DR   BioCyc; BTHA271848:BTH_I1763-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004340; F:glucokinase activity; 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_01639; -; 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; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    287       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269801.
FT   NP_BIND     180    181       ATP (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING     221    221       Substrate (By similarity).
SQ   SEQUENCE   287 AA;  31218 MW;  913217DE3998462E CRC64;
     MKNVLSIQSH VIYGHAGNSA AVFPMQRLGV NVWPLNTVQL SNHMQYGHWA GSAIDAAKME
     QLVDGIAAIG ALKRCDAVLS GFLGSPAQAR AAVEIVRTVK ATNPNAWYFC DPAMGQTGGI
     RPEPGVEEFI VAELPELADG MAPNHGELQK LAGQRIETVA EAVEACRSII RRGPRLILVK
     HLHDRNSPAD RFNMLVVTET EAWIGQRPLY AFPRHPVGVG DLTSAIFVAR RLRGDSVRAA
     FEHTLAAVHA VVKATYDARR YELELVAAQD EIAQPSEWFG AWVTGAD
//