ID   PDXY_GRABC              Reviewed;         286 AA.
AC   Q0BSF0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=GbCGDNIH1_1354;
OS   Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Granulibacter.
OX   NCBI_TaxID=391165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17827295; DOI=10.1128/JB.00793-07;
RA   Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K.,
RA   Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W.,
RA   Holland S.M.;
RT   "Genome sequence analysis of the emerging human pathogenic acetic acid
RT   bacterium Granulibacter bethesdensis.";
RL   J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI62252.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_745175.1; -.
DR   GeneID; 4275222; -.
DR   GenomeReviews; CP000394_GR; GbCGDNIH1_1354.
DR   KEGG; gbe:GbCGDNIH1_1354; -.
DR   NMPDR; fig|391165.8.peg.1341; -.
DR   HOGENOM; Q0BSF0; -.
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    286       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269811.
FT   BINDING       8      8       Substrate (By similarity).
FT   BINDING      43     43       Substrate (By similarity).
FT   BINDING     223    223       Substrate (By similarity).
SQ   SEQUENCE   286 AA;  30628 MW;  83674D0AC0B48A01 CRC64;
     MNILSIQSWV CYGHVGNASA VFPLQLLGAE VWAVNTVQFS NHTGYGDWTG QVFGGDDIAA
     LMKGIADRGV LPRCDAVLSG YMGSDAIGGA ILDAVASVRA ANPEALYCCD PVIGDTGRGI
     FVRPGLPELF RDRAVPTANI LTPNQFELEW LTGHHCRTLA DARAAVKVLA ESMIRQGPRI
     ILVTSLHVAE TPSGSLDMLV YENGRFYLLR TPLLPVSING AGDAIAALFL FHRLDTGDAR
     QALEKAASSV YGLLKRTAEA GSMEILTVAA RQEFLTPSTC FYAQIC
//