ID   PPNK_ALCBS              Reviewed;         300 AA.
AC   Q0VQV5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=ABO_0995;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16443.1; -; Genomic_DNA.
DR   RefSeq; YP_692715.1; -.
DR   GeneID; 4211794; -.
DR   GenomeReviews; AM286690_GR; ABO_0995.
DR   KEGG; abo:ABO_0995; -.
DR   NMPDR; fig|393595.12.peg.1002; -.
DR   HOGENOM; Q0VQV5; -.
DR   OMA; Q0VQV5; MEQFRNI.
DR   BioCyc; ABOR393595:ABO_0995-MON; -.
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; 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   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    300       Probable inorganic polyphosphate/ATP-NAD
FT                                kinase.
FT                                /FTId=PRO_1000079479.
SQ   SEQUENCE   300 AA;  32683 MW;  185980257583C98E CRC64;
     MRSLVAQEKF RNIGLIARSE SEQALYSLRQ LIHFLHGRDC TVILDKHIIG HLPEMGLQAA
     SASQMGEACD LVIVVGGDGS LLGAARTLAR YKVPVLGVNR GHLGFLTDIL PSEIESRVGQ
     VLDGEYSTEK RFLLDLEVRR GRTVVGEGSA LNDIVLLSGD SVHMIDFELM IDGHFVYGQR
     SDGLIVSTPT GSTAYALSGG GPIMHPKLDA MVLVPLNPHT LTSRPLVVAG DSEIKIHITT
     EKVRPLVSCD GTEGIRLQVD DVIAIRKKPH RLHLIHPPGH DFYQACRSKL GWSSRPGDNN
//