ID   A0PPA4_MYCUA            Unreviewed;       307 AA.
AC   A0PPA4;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   01-MAY-2013, entry version 56.
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=MUL_1684;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S.J.A., Frigui W., Reysset G.,
RA   Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M.,
RA   Porter J.L., Ryan J.E., Johnson P.D.R., Davies J.K., Jenkin G.A.,
RA   Small P.L.C., Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J.,
RA   Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL04173.1; -; Genomic_DNA.
DR   RefSeq; YP_905644.1; NC_008611.1.
DR   ProteinModelPortal; A0PPA4; -.
DR   SMR; A0PPA4; 2-305.
DR   STRING; 362242.MUL_1684; -.
DR   EnsemblBacteria; ABL04173; ABL04173; MUL_1684.
DR   GeneID; 4551918; -.
DR   KEGG; mul:MUL_1684; -.
DR   PATRIC; 18170346; VBIMycUlc37413_2025.
DR   GenoList; MUL_1684; -.
DR   eggNOG; COG0061; -.
DR   HOGENOM; HOG000227223; -.
DR   KO; K00858; -.
DR   OMA; GVLWCDG; -.
DR   ProtClustDB; PRK03372; -.
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:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.60.200.30; -; 1.
DR   Gene3D; 3.40.50.10330; -; 1.
DR   HAMAP; MF_00361; NAD_kinase; 1; -.
DR   InterPro; IPR017438; ATP-NAD_kinase_dom_1.
DR   InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; PolyP/ATP_NADK_prd.
DR   PANTHER; PTHR20275; PTHR20275; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; ATP-NAD_kinase_PpnK-typ; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Transferase.
SQ   SEQUENCE   307 AA;  32972 MW;  4E1FCBCD2F208801 CRC64;
     MTATRTVLLV VHTGRDEATE TARRVEKVLG DNGIALRVLS AEAVDRGSLH LAPDDMRALG
     IDIEVVDADP RAADGCELVL VLGGDGTFLR AAELARNAQI PVLGVNLGRI GFLAEAEAEA
     IDRVLDHVVA RDYRVEERLT LDVVVRKAGC DLERGWALNE VSLEKGPRLG VLGVVVEIDG
     RSVSAFGCDG VLVSTPTGST AYAFSAGGPV LWPDLEAILV VPNNAHALFG RPMVTSPEAT
     IAVEIEPDGH DAMVFCDGRR EMLMPAGSRL EVTRCDTPVK WARLDSAPFT DRLVHKFRLP
     VTGWRGK
//