ID   PPNK_MYCTU              Reviewed;         307 AA.
AC   P0A5S6; O33196;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Inorganic polyphosphate/ATP-NAD kinase;
DE            Short=Poly(P)/ATP NAD kinase;
DE            EC=2.7.1.23;
GN   Name=ppnK; OrderedLocusNames=Rv1695, MT1734; ORFNames=MTCI125.17;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=20462915; PubMed=11006082; DOI=10.1006/bbrc.2000.3433;
RA   Kawai S., Mori S., Mukai T., Suzuki S., Yamada T., Hashimoto W.,
RA   Murata K.;
RT   "Inorganic polyphosphate / ATP-NAD kinase of Micrococcus flavus and
RT   Mycobacterium tuberculosis H37Rv.";
RL   Biochem. Biophys. Res. Commun. 276:57-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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.
CC   -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+).
CC   -!- COFACTOR: Divalent metal ions.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the NAD kinase family.
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DR   EMBL; AB044336; BAB21478.1; -; Genomic_DNA.
DR   EMBL; BX842577; CAB10952.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK46003.1; -; Genomic_DNA.
DR   PIR; F70502; F70502.
DR   RefSeq; NP_216211.1; -.
DR   RefSeq; NP_336189.1; -.
DR   PDB; 1U0R; X-ray; 2.80 A; A/B/C/D=1-307.
DR   PDB; 1U0T; X-ray; 2.30 A; A/B=1-307.
DR   PDB; 1Y3H; X-ray; 2.80 A; A/B=1-307.
DR   PDB; 1Y3I; X-ray; 2.60 A; A/B=1-307.
DR   PDBsum; 1U0R; -.
DR   PDBsum; 1U0T; -.
DR   PDBsum; 1Y3H; -.
DR   PDBsum; 1Y3I; -.
DR   GeneID; 885660; -.
DR   GeneID; 923972; -.
DR   GenomeReviews; AE000516_GR; MT1734.
DR   GenomeReviews; AL123456_GR; Rv1695.
DR   KEGG; mtc:MT1734; -.
DR   KEGG; mtu:Rv1695; -.
DR   TIGR; MT1734; -.
DR   TubercuList; Rv1695; -.
DR   HOGENOM; P0A5S6; -.
DR   OMA; P0A5S6; NDGKELA.
DR   BRENDA; 2.7.1.23; 809.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; NAD;
KW   NADP; Nucleotide-binding; Transferase.
FT   CHAIN         1    307       Inorganic polyphosphate/ATP-NAD kinase.
FT                                /FTId=PRO_0000120635.
FT   STRAND        6     14
FT   HELIX        15     18
FT   HELIX        20     30
FT   TURN         31     33
FT   STRAND       35     39
FT   STRAND       79     83
FT   HELIX        85     98
FT   STRAND      102    106
FT   STRAND      115    117
FT   HELIX       118    120
FT   HELIX       121    130
FT   STRAND      134    138
FT   STRAND      141    147
FT   STRAND      150    164
FT   STRAND      166    170
FT   STRAND      172    194
FT   HELIX       197    200
FT   HELIX       202    205
FT   STRAND      218    224
FT   STRAND      226    228
FT   STRAND      233    235
FT   STRAND      241    245
FT   STRAND      252    256
FT   TURN        257    259
FT   STRAND      260    264
FT   STRAND      269    274
FT   STRAND      279    283
FT   HELIX       289    297
SQ   SEQUENCE   307 AA;  32904 MW;  68817BE570B6645B CRC64;
     MTAHRSVLLV VHTGRDEATE TARRVEKVLG DNKIALRVLS AEAVDRGSLH LAPDDMRAMG
     VEIEVVDADQ HAADGCELVL VLGGDGTFLR AAELARNASI PVLGVNLGRI GFLAEAEAEA
     IDAVLEHVVA QDYRVEDRLT LDVVVRQGGR IVNRGWALNE VSLEKGPRLG VLGVVVEIDG
     RPVSAFGCDG VLVSTPTGST AYAFSAGGPV LWPDLEAILV VPNNAHALFG RPMVTSPEAT
     IAIEIEADGH DALVFCDGRR EMLIPAGSRL EVTRCVTSVK WARLDSAPFT DRLVRKFRLP
     VTGWRGK
//