NADK_THEMA
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 03-AUG-2022, entry version 135.
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; Thermotogae; Thermotogales; Thermotogaceae; 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.THEMA_05570; -.
DR EnsemblBacteria; AAD36798; AAD36798; TM_1733.
DR KEGG; tma:TM1733; -.
DR eggNOG; COG0061; Bacteria.
DR InParanoid; Q9X255; -.
DR OMA; VNLGHVG; -.
DR OrthoDB; 1463423at2; -.
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 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 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
