ID NADK_METAC Reviewed; 275 AA. AC Q8TKQ5; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 116. 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=MA_3343; OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / OS C2A). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=188937; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A; RX PubMed=11932238; DOI=10.1101/gr.223902; RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., RA Zinder S.H., Lander E., Metcalf W.W., Birren B.; RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and RT physiological diversity."; RL Genome Res. 12:532-542(2002). 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; AE010299; AAM06712.1; -; Genomic_DNA. DR RefSeq; WP_011023273.1; NC_003552.1. DR AlphaFoldDB; Q8TKQ5; -. DR SMR; Q8TKQ5; -. DR STRING; 188937.MA_3343; -. DR EnsemblBacteria; AAM06712; AAM06712; MA_3343. DR GeneID; 1475236; -. DR KEGG; mac:MA_3343; -. DR HOGENOM; CLU_008831_0_2_2; -. DR InParanoid; Q8TKQ5; -. DR OrthoDB; 77798at2157; -. DR PhylomeDB; Q8TKQ5; -. DR Proteomes; UP000002487; 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; 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: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..275 FT /note="NAD kinase" FT /id="PRO_0000120699" FT ACT_SITE 68 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 68..69 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 73 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 201 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 275 AA; 30499 MW; 1B45C07917BB5CED CRC64; MAIRKIGIAS RCDRPEVLQM VRDIIAHFYS KVQIYVSTAT ADVLDIEGTP VERMRDKGVE LIISVGGDGT VLRNIAKMKD PLPVLGINMG TLGFLVDVEP EDAIETIEEV LYGFSYLERM RVDVFLNGEM LETATNEVAV MSAKPAKIIQ FEVYVNDCLL DEMRADGVVF ATPTGSTAYA MSAGGPIINP RVNAIVVVPV APFKLSARPW VIPSDSEITV KLSDHKKEAV IAIDGQKSYR IRPDDVVKLK KSKYPARFVR ISDTCFYERV QRKLS //