ID PPNK_BIFLO Reviewed; 342 AA. AC Q8G5G8; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 32. 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=BL1044; OS Bifidobacterium longum. OC Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=216816; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705; RX MEDLINE=22294977; PubMed=12381787; DOI=10.1073/pnas.212527599; RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., RA Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., RA Pridmore R.D., Arigoni F.; RT "The genome sequence of Bifidobacterium longum reflects its adaptation RT to the human gastrointestinal tract."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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. 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; AE014295; AAN24850.1; -; Genomic_DNA. DR RefSeq; NP_696214.1; -. DR GeneID; 1022572; -. DR GenomeReviews; AE014295_GR; BL1044. DR KEGG; blo:BL1044; -. DR NMPDR; fig|206672.1.peg.981; -. DR HOGENOM; Q8G5G8; -. DR OMA; Q8G5G8; NDGKELA. DR BioCyc; BLON206672:BL1044-MON; -. DR BRENDA; 2.7.1.23; 39917. 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; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD; NADP; KW Nucleotide-binding; Transferase. FT CHAIN 1 342 Probable inorganic polyphosphate/ATP-NAD FT kinase. FT /FTId=PRO_0000120601. SQ SEQUENCE 342 AA; 36613 MW; 3C215EC0045DB211 CRC64; MAKRNAVVVT HTRLRQTGTV VAEAVSQLRV AGFEVAIIDN TEAPDFGVQP PCVSDDTEIV VVLGGDGTIL RAAELVHCTQ VPILGVNMGH VGFLAEFESF QIDEAIRRVS THDYSIDERM IAHVDVWLPG ATKPIEDWAL NDITLERADR GKMVELSIRV DDVEMNSFGA DGVIVSTPTG STAYAFSAGG PVMWPNVKAL QLIPLAAHAL FARPLIIGSG STFTIDILDD SMSEGWICCD GRRQRALPQG TRVMVRESRD TLRLARLSGV PFTNRLVSKF DLPVVGWREH ARNEASSQSL HHGHTFPAAA YAAGVAVAVA GDAGVAGTDP DKPGERDGKA GA //