ID NADK_LEVBA Reviewed; 267 AA. AC Q03QF3; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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=LVIS_1472; OS Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM OS 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Levilactobacillus. OX NCBI_TaxID=387344; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / RC NCIMB 947 / NCTC 947; RX PubMed=17030793; DOI=10.1073/pnas.0607117103; RA Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., RA Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., RA O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., RA Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.; RT "Comparative genomics of the lactic acid bacteria."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006). 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; CP000416; ABJ64569.1; -; Genomic_DNA. DR RefSeq; WP_011668197.1; NC_008497.1. DR AlphaFoldDB; Q03QF3; -. DR SMR; Q03QF3; -. DR STRING; 387344.LVIS_1472; -. DR KEGG; lbr:LVIS_1472; -. DR PATRIC; fig|387344.15.peg.1407; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_3_9; -. DR Proteomes; UP000001652; 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" FT /id="PRO_1000059869" FT ACT_SITE 45 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 45..46 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 148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 150 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 161..166 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 185 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 223 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 267 AA; 29407 MW; 57EFB61058F46539 CRC64; MKVSIFSNNG LSSQKVATAL QKGLTAAGVP IDSLDPDVVV TVGGDGTLLS AFHHYNDRLD KVRFVGIHTG HLGFYTDWRD YEVQELIDSL AQDNGQSVSY PLLTIQVEYA DGTHPDQALA LNESTIKKVS GTMVADVYIK DELFESFRGD GLCISTPTGS TAYNKSVGGA VLNPRFNAVQ MAEIASINNL VFRTLGSPLI IPADEWIRIE PADPTDNVLM CDQLGIEGRP IKAIMYRIAR QRIAFAEYRH THFWQRVESS FIGRENA //