ID NADK1_BACLD Reviewed; 267 AA. AC Q65LA2; Q62WP1; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 104. DE RecName: Full=NAD kinase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=BLi01255, BL05111; OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=279010; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15383718; DOI=10.1159/000079829; RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.; RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism RT with great industrial potential."; RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46; RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77; RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.; RT "Complete genome sequence of the industrial bacterium Bacillus RT licheniformis and comparisons with closely related Bacillus species."; RL Genome Biol. 5:R77.1-R77.12(2004). RN [3] RP SEQUENCE REVISION TO 152. RA Berka R.M., Rey M.W., Ramaiya P.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. 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; AE017333; AAU40162.1; -; Genomic_DNA. DR EMBL; CP000002; AAU22817.2; -; Genomic_DNA. DR AlphaFoldDB; Q65LA2; -. DR SMR; Q65LA2; -. DR STRING; 279010.BL05111; -. DR KEGG; bld:BLi01255; -. DR KEGG; bli:BL05111; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_3_9; -. DR Proteomes; UP000000606; 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; 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; 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 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 1" FT /id="PRO_0000229604" FT ACT_SITE 46 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 46..47 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 123..124 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 186 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 267 AA; 29670 MW; 4BBC6CD6CD5EA750 CRC64; MMKFAVSSKG NAVSDSLKSK IQTYLLDFGL ECDEEEPDIV ISVGGDGTLL YAFHKYSGRL DKTAFVGVHT GHLGFYADWV PSEIEKLVIA IAKTPYQIVE YPVLEVIVRY NDGSDEARYL ALNECTIKSI EGTLVTDVEI KGELFETFRG DGLCLSTPSG STAYNKALGG AIIHPSIRAI QLAEMASINN RVFRTVGSPL ILPEHHTCLI KPINDVTFQV AIDHLTLLHK DVKSIQCRVA NENIRFARFR PFPFWKRVQD SFIGKGE //