ID   NADK_CLOB1              Reviewed;         281 AA.
AC   A7FUT5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   02-SEP-2026, entry version 97.
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};
GN   OrderedLocusNames=CLB_1816;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium; Clostridium botulinum group.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT   and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(2007).
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=NAD(+) + ATP = ADP + NADP(+) + H(+); 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; CP000726; ABS32452.1; -; Genomic_DNA.
DR   RefSeq; WP_011986440.1; NC_009697.1.
DR   AlphaFoldDB; A7FUT5; -.
DR   SMR; A7FUT5; -.
DR   KEGG; cba:CLB_1816; -.
DR   HOGENOM; CLU_008831_0_1_9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-ARBA.
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   FunFam; 2.60.200.30:FF:000011; NAD kinase; 1.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 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   PANTHER; PTHR20275; NAD KINASE; 1.
DR   PANTHER; PTHR20275:SF0; NAD KINASE; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   Pfam; PF20143; NAD_kinase_C; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase.
FT   CHAIN           1..281
FT                   /note="NAD kinase"
FT                   /id="PRO_1000120843"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         61..62
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         134..135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         145
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         175..180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   281 AA;  31690 MW;  0014EA8B8EE1A1A2 CRC64;
     MKNIGININT DKDISRNILD KIFQYIHEEC SEAKIKVFYD SKGLDNEESR ALDAVMVLGG
     DGTILGTARA LAKYDVPIFG INRGHLGFLA EIELEDCKKA IKNLFKGQYK IEDRIMLKCD
     LKGIDKKDDF LALNDIVLTK GNLSRIVKYS IYVDDVWYTT FVADGVIVAT PTGSTAYSLS
     AGGPIVYPDL DVLEIAPICP HSLGIRPILL NGNSKINIRV LKKYEDPVLT IDGQRYKKVT
     VNEVTISKSE YKCRLIKFKD KDYFKILRTK ISYRSRECEG E
//