(data stored in SCRATCH9089 zone)

SWISSPROT: NADK_PASMU

ID   NADK_PASMU              Reviewed;         305 AA.
AC   Q9CNU2;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   11-DEC-2019, entry version 112.
DE   RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
DE            EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361};
DE   AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361};
GN   Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361}; OrderedLocusNames=PM0333;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance of
CC       NAD and NADP, and is a key enzyme in the biosynthesis of NADP.
CC       Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC       adenosine moiety of NAD to yield NADP. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00361};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00361}.
DR   EMBL; AE004439; AAK02417.1; -; Genomic_DNA.
DR   RefSeq; WP_010906592.1; NC_002663.1.
DR   SMR; Q9CNU2; -.
DR   PRIDE; Q9CNU2; -.
DR   EnsemblBacteria; AAK02417; AAK02417; PM0333.
DR   KEGG; pmu:PM0333; -.
DR   eggNOG; ENOG4105F91; Bacteria.
DR   eggNOG; COG0061; LUCA.
DR   HOGENOM; HOG000227221; -.
DR   KO; K00858; -.
DR   OMA; VNLGHVG; -.
DR   BioCyc; PMUL272843:G1FZ8-351-MONOMER; -.
DR   Proteomes; UP000000809; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule.
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_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CNU2.
DR   SWISS-2DPAGE; Q9CNU2.
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..305
FT                   /note="NAD kinase"
FT                   /id="PRO_0000120644"
FT   NP_BIND         84..85
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   NP_BIND         159..160
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   NP_BIND         200..205
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   ACT_SITE        84
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         170
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         187
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         189
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         260
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   305 AA;  33711 MW;  BD8BC03D93C41BE6 CRC64;
     MKHPNTIDIK ALQSSFQIIG LLGKPRHDVT LQMHKNLFQW LLEKGYQVLV ERPIGEQLGL
     SENYLASVDE IGQQAQLAIV IGGDGNVLGR ARTLAKYDIA LIGINRGNLG FLTDIDPKNA
     YSQLQACLED GDCFVEERFI LEASVERNGK IIARGNAVNE AVVHPAKIAH MIDFHVYIND
     KFAFSQRSDG LIISTPTGST AYSLSAGGPI LTPQLNAIAL VPMFPHTLSS RPLVIDGDSK
     ISIRFAEYNT SQLEVGCDSQ VALEFSPDDI VHIQKSPDKL RLLHLKNYNY YKVLSSKLGW
     LRNSV
//

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