ID NADK2_LISMO Reviewed; 267 AA. AC P65770; Q92BC2; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 111. DE RecName: Full=NAD kinase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=nadK2 {ECO:0000255|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=lmo1586; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Listeriaceae; OC Listeria. OX NCBI_TaxID=169963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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=NAD(+) + ATP = ADP + NADP(+) + H(+); 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; AL591979; CAC99664.1; -; Genomic_DNA. DR PIR; AB1273; AB1273. DR RefSeq; WP_003723315.1; NC_003210.1. DR AlphaFoldDB; P65770; -. DR SMR; P65770; -. DR STRING; 169963.gene:17594243; -. DR PaxDb; 169963-gene:17594243; -. DR EnsemblBacteria; CAC99664; CAC99664; CAC99664. DR GeneID; 93235010; -. DR KEGG; lmo:lmo1586; -. DR PATRIC; fig|169963.11.peg.1628; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_3_9; -. DR OrthoDB; 9774737at2; -. DR PhylomeDB; P65770; -. DR BioCyc; LMON169963:LMO1586-MONOMER; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-ARBA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-ARBA. 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 Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1. DR Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 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 NCBIfam; NF002902; PRK03501.1; 1. DR PANTHER; PTHR20275; NAD KINASE; 1. DR PANTHER; PTHR20275:SF9; NAD KINASE 2; 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..267 FT /note="NAD kinase 2" FT /id="PRO_0000120633" FT ACT_SITE 50 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 50..51 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 55 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 122..123 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 151 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 162..167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 186 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 267 AA; 30499 MW; 69512B6100D49F73 CRC64; MAKTIFYFSY RKTEELHAKA KELKKITTDY GYELTDDYQK ANVIISIGGD GAFLKSVRET GFRQDCLYAG IALTEQLGQY CDFHINQLDE IIKAAIEDRW LVRRYPTIYG TVNNTKAFYV LNEFNIRSSI IRTLTMDLYI NDSHFETFRG DGMVISTPTG STAYNKSVNG SIVDPLLPSM QVSELASINN NKFRTLGSSF ILSPKRKLRI EIASEEGNNE FPMIGMDSEA LSIQHVHEVN LEVGDRFINI IKLPKNSFWD KVKRNFL //