ID   NADK_THEGJ              Reviewed;         278 AA.
AC   C5A3H8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=TGAM_0288;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(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=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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001398; ACS32790.1; -; Genomic_DNA.
DR   RefSeq; WP_015857909.1; NC_012804.1.
DR   AlphaFoldDB; C5A3H8; -.
DR   SMR; C5A3H8; -.
DR   STRING; 593117.TGAM_0288; -.
DR   PaxDb; C5A3H8; -.
DR   EnsemblBacteria; ACS32790; ACS32790; TGAM_0288.
DR   GeneID; 7988944; -.
DR   KEGG; tga:TGAM_0288; -.
DR   PATRIC; fig|593117.10.peg.290; -.
DR   eggNOG; arCOG01348; Archaea.
DR   HOGENOM; CLU_008831_0_3_2; -.
DR   OMA; VNLGHVG; -.
DR   OrthoDB; 104144at2157; -.
DR   Proteomes; UP000001488; 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   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   Pfam; PF01513; NAD_kinase; 1.
DR   SUPFAM; SSF111331; SSF111331; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase.
FT   CHAIN           1..278
FT                   /note="NAD kinase"
FT                   /id="PRO_1000205432"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         67..68
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         137..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         148
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         178..183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         237
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
SQ   SEQUENCE   278 AA;  31338 MW;  C988DD46C5518704 CRC64;
     MRFGIVARRD REAALKLAYR VYDFLKVSGY DVLVDRETFE NLPEFEEGDV VPLEEFDVDF
     IIAIGGDGTI LRIEHKTKKD FPILGINMGT LGFLTEVEPH ETFFALSRLL EGDYWIDERM
     KLRTYLNGEN SVPDALNEDA ILTGVPGKIV HLKYYVDGGL ADEVRSDGVI VSTPTGSTGY
     ALSAGGPFVD PRLELFVIAP INPIALSSRP MVVPSSSEIE IVPLPPERGL ILTVDGQFYT
     HLSPDTEIKI KKSPRKARFV RFSHEIYPRY PFRLKKRF