ID   PPNK_BORBU              Reviewed;         279 AA.
AC   O51291;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Probable inorganic polyphosphate/ATP-NAD kinase;
DE            Short=Poly(P)/ATP NAD kinase;
DE            EC=2.7.1.23;
GN   Name=ppnK; OrderedLocusNames=BB_0311;
OS   Borrelia burgdorferi (Lyme disease spirochete).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=139;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680;
RX   MEDLINE=98065943; PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- FUNCTION: Catalyzes the phosphorylation of NAD to NADP. Utilizes
CC       ATP and other nucleoside triphosphates as well as inorganic
CC       polyphosphate as a source of phosphorus (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
CC   -!- COFACTOR: Divalent metal ions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
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DR   EMBL; AE000783; AAC66699.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_212445.1; -.
DR   GeneID; 1195148; -.
DR   GenomeReviews; AE000783_GR; BB_0311.
DR   KEGG; bbu:BB0311; -.
DR   NMPDR; fig|224326.1.peg.695; -.
DR   TIGR; BB_0311; -.
DR   HOGENOM; O51291; -.
DR   BioCyc; BBUR224326:BB_0311-MON; -.
DR   BRENDA; 2.7.1.23; 142596.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:HAMAP.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:HAMAP.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   HAMAP; MF_00361; -; 1.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; ATP_NADK.
DR   Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 1.
DR   PANTHER; PTHR20275; ATP_NADK; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    279       Probable inorganic polyphosphate/ATP-NAD
FT                                kinase.
FT                                /FTId=PRO_0000120602.
SQ   SEQUENCE   279 AA;  30967 MW;  1592FC198FAFE96C CRC64;
     MKNKVLLCIN TLKSGASILG NDVKVYLETK YFVEVVLIDV GRPLFSFPKE NFLFLITLGG
     DGTVLLAVNL LLENENIDIP IISINMGNVG FLADIKIEDF KKVIDRFFNN SLVINKKFLL
     HVTVSQHGKD LISKYALNDI IIRSSVLNKM IYVDLMVNSE SFLSYKSDGI IVSTPTGSTG
     YSFSAGGPIL EADLEGFXLT PISPHSVYNR SFVFSKLSKL SISFSKEYFI AAASIFLDGI
     NFGSFGVDVV FEFKISSQSL NFVSFCTDTF VKRLKNKLL
//