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Database: UniProt/TrEMBL
Entry: A6T230_JANMA
LinkDB: A6T230_JANMA
Original site: A6T230_JANMA 
ID   A6T230_JANMA            Unreviewed;       305 AA.
AC   A6T230;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   01-MAY-2013, entry version 49.
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=mma_2887;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M.,
RA   Raoult D., Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the
RT   convergent evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(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; CP000269; ABR89472.1; -; Genomic_DNA.
DR   RefSeq; YP_001354577.1; NC_009659.1.
DR   ProteinModelPortal; A6T230; -.
DR   STRING; 375286.mma_2887; -.
DR   EnsemblBacteria; ABR89472; ABR89472; mma_2887.
DR   GeneID; 5351992; -.
DR   KEGG; mms:mma_2887; -.
DR   PATRIC; 22158293; VBIJanSp106498_2909.
DR   eggNOG; COG0061; -.
DR   HOGENOM; HOG000227221; -.
DR   KO; K00858; -.
DR   OMA; KLHWAGS; -.
DR   ProtClustDB; CLSK967402; -.
DR   BioCyc; JSP375286:GJ8U-2932-MONOMER; -.
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   305 AA;  32990 MW;  AEC66157BD995A5F CRC64;
     MSLTPHSPHP SSFNTIAIVG KHMAGGIAKS LTDIADCLGS TGRKVIFEAE TALNFSLTDY
     DSMTLPEIGE CADAAIVVGG DGTMLGIARQ LAPYNVPLIG VNQGRLGFMT DISLDQMMPL
     LKEMLSGKVR SEQRTLLKGS IEREGEPMYS TLAFNDVVLS RGSGAGMVEL RVEVDGHFMY
     NQRSDGLIVA TPTGSSAYAL SAGGPILHPS LTGIGLVPIA PHALSNRPIV VPDSSVIVIE
     VMSGRNASVN FDMQSVARLL KHDRITVQRS EHTITFLHPE GWNYYDTLRE KLHWNEYPSV
     EGRLK
//
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