ID   PPNK_BRUSU              Reviewed;         257 AA.
AC   Q8G0Z4;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   16-JUN-2009, entry version 36.
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=BR0937;
OS   Brucella suis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=29461;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330 / Biovar 1;
RX   MEDLINE=22247741; PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
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; AE014291; AAN29863.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_697948.1; -.
DR   GeneID; 1166607; -.
DR   GenomeReviews; AE014291_GR; BR0937.
DR   KEGG; bms:BR0937; -.
DR   NMPDR; fig|204722.1.peg.905; -.
DR   TIGR; BR0937; -.
DR   HOGENOM; Q8G0Z4; -.
DR   BioCyc; BSUI204722:BR_0937-MON; -.
DR   BRENDA; 2.7.1.23; 281610.
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; IPR017438; ATP-NAD_kinase_PpnK-typ_a/b.
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   Gene3D; G3DSA:3.40.50.10330; ATP-NAD_kinase_PpnK-typ_a/b; 1.
DR   PANTHER; PTHR20275; ATP_NADK; 1.
DR   Pfam; PF01513; NAD_kinase; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    257       Probable inorganic polyphosphate/ATP-NAD
FT                                kinase.
FT                                /FTId=PRO_0000120604.
SQ   SEQUENCE   257 AA;  28275 MW;  54ACA8EF3504F74A CRC64;
     MKDTSLALHF VSSGTKESLS AQKDLVERYG HVAAEDADII VALGGDGTML QALRDFMNTG
     KPIYGMNRGS VGFLMNEFVI ENLPERILAA QMETIRPLVM VAETEDAPPV EALAINEVSL
     FRQSYQAARI RITIDGKVRL QELVCDGVMV ATPAGSTAYN LSAQGPILPL EAPLLALTPV
     SPFRPRRWGG ALLPKHVTVR MDLLETEKRP VNAVADNNEV KSVTSVTVRE APNSQVTILF
     DKNHSWDERI LTEQFRH
//