ID NADK_METTH Reviewed; 283 AA. AC O26958; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 134. 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=MTH_872; OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=187420; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H; RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997; RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., RA Reeve J.N.; RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: RT functional analysis and comparative genomics."; RL J. Bacteriol. 179:7135-7155(1997). 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; AE000666; AAB85370.1; -; Genomic_DNA. DR PIR; E69216; E69216. DR AlphaFoldDB; O26958; -. DR SMR; O26958; -. DR STRING; 187420.MTH_872; -. DR PaxDb; 187420-MTH_872; -. DR EnsemblBacteria; AAB85370; AAB85370; MTH_872. DR KEGG; mth:MTH_872; -. DR PATRIC; fig|187420.15.peg.856; -. DR HOGENOM; CLU_008831_0_2_2; -. DR InParanoid; O26958; -. DR Proteomes; UP000005223; 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 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:SF43; BIFUNCTIONAL NADP PHOSPHATASE_NAD KINASE; 1. DR PANTHER; PTHR20275; 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; KW Reference proteome; Transferase. FT CHAIN 1..283 FT /note="NAD kinase" FT /id="PRO_0000120703" 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 136..137 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 147 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 166 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 177..182 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 236 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 283 AA; 31604 MW; A8E67DC1D603561C CRC64; MMRIGIIARF DVAEAVEIAE RVASFLLNRG VEITVDLKLT EELPQLREYG EDIRNMDADM ILTIGGDGTI LRTRSLIEDK EIPILGINMG TVGFLTEVDP ENVFSALEAV LRGEYAVEKR TLLSVYHNDE LPSALNEVVL MTRRPAKMLH IEISVDDEVV EELRADGIII ATPSGSTAYS MSAGGPIVDP RVEAFLIVPI CPFKLSARPL VVSNKSVIRV KLLRKGKKAI AVIDGQYEEE INHMDEVIFR KSERKAHFVR LSKDFYRKVR EKLIEGGIDS IKG //