ID   NADK_STRPI              Reviewed;         272 AA.
AC   B1IBN7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SPH_1189;
OS   Streptococcus pneumoniae (strain Hungary19A-6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=487214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hungary19A-6;
RX   PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA   Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA   Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA   Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA   Rappuoli R., Moxon E.R., Masignani V.;
RT   "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT   closely related species.";
RL   Genome Biol. 11:R107.1-R107.19(2010).
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}.
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DR   EMBL; CP000936; ACA36304.1; -; Genomic_DNA.
DR   RefSeq; WP_000799059.1; NC_010380.1.
DR   AlphaFoldDB; B1IBN7; -.
DR   SMR; B1IBN7; -.
DR   EnsemblBacteria; ACA36304; ACA36304; SPH_1189.
DR   GeneID; 66806203; -.
DR   KEGG; spv:SPH_1189; -.
DR   HOGENOM; CLU_008831_0_3_9; -.
DR   OMA; NGIERMS; -.
DR   Proteomes; UP000002163; 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:0051287; F:NAD binding; IEA:UniProt.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   SUPFAM; SSF111331; SSF111331; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase.
FT   CHAIN           1..272
FT                   /note="NAD kinase"
FT                   /id="PRO_1000120891"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         50..51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         126..127
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         154
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         165..170
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         189
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   272 AA;  31005 MW;  3272461E3DBB941A CRC64;
     MKNTGKRIDL IANRKPQSQR VLYELRDRLK RNQFILNDTN PDIVISIGGD GMLLSAFHKY
     ENQLEKVRFI GLHTGHLGFY TDYRDFELDK LVTNLQLDTG ARVSYPVLNV KVFLENGEVK
     IFRALNEASI RRSDRTMVAD IVINGVPFER FRGDGLTVST PTGSTAYNKS LGGAVLHPTI
     EALQLTEIAS LNNRVYRTLG SSIIVPKKDK IELIPTRNDY HTISVDNSVY SFRNIERIEY
     QIAHHKIHFV ATPSHTSFWN RVKDAFIGEV DE