ID   NADK_THEMA              Reviewed;         258 AA.
AC   Q9X255;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 142.
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; OrderedLocusNames=TM_1733;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX   PubMed=16511117; DOI=10.1107/s1744309105019780;
RA   Oganesyan V., Huang C., Adams P.D., Jancarik J., Yokota H.A., Kim R.,
RA   Kim S.H.;
RT   "Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution.";
RL   Acta Crystallogr. F 61:640-646(2005).
CC   -!- FUNCTION: Involved in the regulation of the intracellular balance
CC       between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of
CC       NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the
CC       adenosine moiety of NAD to yield NADP (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16511117}.
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; AE000512; AAD36798.1; -; Genomic_DNA.
DR   PIR; D72217; D72217.
DR   RefSeq; NP_229531.1; NC_000853.1.
DR   RefSeq; WP_004082250.1; NZ_CP011107.1.
DR   PDB; 1YT5; X-ray; 2.30 A; A/B/C/D=1-258.
DR   PDBsum; 1YT5; -.
DR   AlphaFoldDB; Q9X255; -.
DR   SMR; Q9X255; -.
DR   STRING; 243274.TM_1733; -.
DR   PaxDb; 243274-THEMA_05570; -.
DR   EnsemblBacteria; AAD36798; AAD36798; TM_1733.
DR   KEGG; tma:TM1733; -.
DR   eggNOG; COG0061; Bacteria.
DR   InParanoid; Q9X255; -.
DR   OrthoDB; 9774737at2; -.
DR   BRENDA; 2.7.1.23; 6331.
DR   EvolutionaryTrace; Q9X255; -.
DR   Proteomes; UP000008183; 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; IBA:GO_Central.
DR   GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR   GO; GO:0006741; P:NADP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; NAD; NADP;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..258
FT                   /note="NAD kinase"
FT                   /id="PRO_0000120680"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         51..52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         119..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         160..165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00361"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           12..22
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   TURN            23..25
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          26..36
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           51..58
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          66..74
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          99..110
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          113..124
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          144..154
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           157..160
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   TURN            161..167
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          177..184
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          193..196
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          201..213
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   STRAND          216..237
FT                   /evidence="ECO:0007829|PDB:1YT5"
FT   HELIX           243..251
FT                   /evidence="ECO:0007829|PDB:1YT5"
SQ   SEQUENCE   258 AA;  29242 MW;  45EBBCA0B6FD3EAB CRC64;
     MKIAILYREE REKEGEFLKE KISKEHEVIE FGEANAPGRV TADLIVVVGG DGTVLKAAKK
     AADGTPMVGF KAGRLGFLTS YTLDEIDRFL EDLRNWNFRE ETRWFIQIES ELGNHLALND
     VTLERDLSGK MVEIEVEVEH HSSMWFFADG VVISTPTGST AYSLSIGGPI IFPECEVLEI
     SPIAPQFFLT RSVVIPSNFK VVVESQRDIN MLVDGVLTGK TKRIEVKKSR RYVRILRPPE
     YDYVTVIRDK LGYGRRIE
//