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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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
//