ID NADK1_LISMO Reviewed; 264 AA. AC Q8Y8D7; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 126. 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 {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=nadK1 {ECO:0000255|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=lmo0968; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; 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). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF WILD-TYPE AND MUTANT ASN-45 IN RP COMPLEX WITH NAD AND NAD ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS RP OF ASP-45 AND HIS-223, ACTIVE SITE, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RX PubMed=17686780; DOI=10.1074/jbc.m701394200; RA Poncet-Montange G., Assairi L., Arold S., Pochet S., Labesse G.; RT "NAD kinases use substrate-assisted catalysis for specific recognition of RT NAD."; RL J. Biol. Chem. 282:33925-33934(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF WILD-TYPE AND MUTANT GLU-223 IN RP COMPLEX WITH NAD ANALOGS, FUNCTION, MUTAGENESIS OF HIS-223, AND ACTIVITY RP REGULATION. RX PubMed=22608967; DOI=10.1016/j.str.2012.03.024; RA Gelin M., Poncet-Montange G., Assairi L., Morellato L., Huteau V., RA Dugue L., Dussurget O., Pochet S., Labesse G.; RT "Screening and in situ synthesis using crystals of a NAD kinase lead to a RT potent antistaphylococcal compound."; RL Structure 20:1107-1117(2012). 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, ECO:0000269|PubMed:17686780, CC ECO:0000269|PubMed:22608967}. 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 ECO:0000269|PubMed:17686780}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361}; CC -!- ACTIVITY REGULATION: Competitively inhibited by 5'-thioacetyladenosine CC (TAA) and di-(5'-thioadenosine) (DTA). {ECO:0000269|PubMed:17686780, CC ECO:0000269|PubMed:22608967}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.8 mM for ATP (at pH 7.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:17686780}; CC Vmax=6.67 umol/min/mg enzyme (at pH 7.5 and 30 degrees Celsius) CC {ECO:0000269|PubMed:17686780}; CC Note=kcat is 13.78 sec(-1) for kinase activity with ATP (at pH 7.5 CC and 30 degrees Celsius). kcat is 13.12 sec(-1) for kinase activity CC with NAD (at pH 7.5 and 30 degrees Celsius).; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17686780, CC ECO:0000269|PubMed:22608967}. 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; AL591977; CAC99046.1; -; Genomic_DNA. DR PIR; AH1195; AH1195. DR RefSeq; NP_464493.1; NC_003210.1. DR RefSeq; WP_003729850.1; NZ_CP023861.1. DR PDB; 2I1W; X-ray; 2.34 A; A/B/C/D=1-264. DR PDB; 2I29; X-ray; 2.10 A; A=1-264. DR PDB; 2I2A; X-ray; 2.10 A; A=1-264. DR PDB; 2I2B; X-ray; 2.10 A; A=1-264. DR PDB; 2I2C; X-ray; 1.85 A; A=1-264. DR PDB; 2I2D; X-ray; 2.22 A; A=1-264. DR PDB; 2I2F; X-ray; 1.90 A; A=1-264. DR PDB; 2Q5F; X-ray; 1.90 A; A=1-264. DR PDB; 3V7U; X-ray; 1.97 A; A=1-264. DR PDB; 3V7W; X-ray; 2.01 A; A=1-264. DR PDB; 3V7Y; X-ray; 1.97 A; A=1-264. DR PDB; 3V80; X-ray; 2.03 A; A=1-264. DR PDB; 3V8M; X-ray; 2.48 A; A=1-264. DR PDB; 3V8N; X-ray; 2.38 A; A=1-264. DR PDB; 3V8P; X-ray; 2.29 A; A=1-264. DR PDB; 3V8Q; X-ray; 2.37 A; A=1-264. DR PDB; 3V8R; X-ray; 2.39 A; A=1-264. DR PDB; 4DY6; X-ray; 2.20 A; A=1-264. DR PDB; 5DHP; X-ray; 2.27 A; A/B/C/D=1-264. DR PDB; 5DHQ; X-ray; 2.29 A; A/B/C/D=1-264. DR PDB; 5DHR; X-ray; 2.31 A; A/B/C/D=1-264. DR PDB; 5DHS; X-ray; 2.62 A; A/B/C/D=1-264. DR PDB; 5DHT; X-ray; 2.59 A; A/B/C/D=1-264. DR PDB; 5DHU; X-ray; 2.33 A; A/B/C/D=1-264. DR PDB; 5EJF; X-ray; 2.12 A; A/B/C/D=1-264. DR PDB; 5EJG; X-ray; 2.88 A; A/B/C/D=1-264. DR PDB; 5EJH; X-ray; 2.00 A; A=1-264. DR PDB; 5EJI; X-ray; 2.29 A; A=1-264. DR PDB; 6RBO; X-ray; 1.94 A; A=1-264. DR PDB; 6RBP; X-ray; 2.47 A; A=1-264. DR PDB; 6RBQ; X-ray; 2.24 A; A=1-264. DR PDB; 6RBR; X-ray; 2.06 A; A=1-264. DR PDB; 6RBS; X-ray; 2.32 A; A=1-264. DR PDB; 6RBT; X-ray; 2.55 A; A=1-264. DR PDB; 6RBU; X-ray; 1.97 A; A=1-264. DR PDB; 6RBV; X-ray; 2.29 A; A=1-264. DR PDB; 6RBW; X-ray; 2.50 A; A=1-264. DR PDB; 6RBX; X-ray; 2.47 A; A=1-264. DR PDB; 6RBY; X-ray; 2.31 A; A=1-264. DR PDB; 6RBZ; X-ray; 2.32 A; A=1-264. DR PDB; 6RC0; X-ray; 2.75 A; A=1-264. DR PDB; 6RC1; X-ray; 2.54 A; A=1-264. DR PDB; 6RC2; X-ray; 2.05 A; A=1-264. DR PDB; 6RC3; X-ray; 2.31 A; A=1-264. DR PDB; 6RC4; X-ray; 2.28 A; A=1-264. DR PDB; 6RC5; X-ray; 2.04 A; A=1-264. DR PDB; 6RC6; X-ray; 2.29 A; A=1-264. DR PDB; 6RG6; X-ray; 2.52 A; A=1-264. DR PDB; 6RG7; X-ray; 2.08 A; A=1-264. DR PDB; 6RG8; X-ray; 2.47 A; A=1-264. DR PDB; 6RG9; X-ray; 2.08 A; A=1-264. DR PDB; 6RGA; X-ray; 2.18 A; A=1-264. DR PDB; 6RGB; X-ray; 2.25 A; A=1-264. DR PDB; 6RGC; X-ray; 2.19 A; A=1-264. DR PDB; 6RGD; X-ray; 2.30 A; A=1-264. DR PDB; 6RGE; X-ray; 1.80 A; A=1-264. DR PDB; 6RGF; X-ray; 2.30 A; A=1-264. DR PDB; 6RR2; X-ray; 1.99 A; A=1-264. DR PDB; 6Z61; X-ray; 2.47 A; A=1-264. DR PDB; 6Z64; X-ray; 1.89 A; A=1-264. DR PDB; 6Z65; X-ray; 1.97 A; A=1-264. DR PDB; 7ZZ7; X-ray; 2.00 A; A=1-264. DR PDB; 7ZZ9; X-ray; 1.89 A; A=1-264. DR PDB; 7ZZA; X-ray; 2.05 A; A=1-264. DR PDB; 7ZZB; X-ray; 1.56 A; A=1-264. DR PDB; 7ZZC; X-ray; 2.10 A; A=1-264. DR PDB; 7ZZD; X-ray; 1.79 A; A=1-264. DR PDB; 7ZZE; X-ray; 1.78 A; A=1-264. DR PDB; 7ZZF; X-ray; 2.41 A; A=1-264. DR PDB; 7ZZG; X-ray; 2.30 A; A=1-264. DR PDB; 7ZZH; X-ray; 2.00 A; A=1-264. DR PDB; 7ZZJ; X-ray; 1.99 A; A=1-264. DR PDB; 8A9V; X-ray; 1.98 A; A=1-264. DR PDB; 8B47; X-ray; 2.53 A; A/B=1-264. DR PDBsum; 2I1W; -. DR PDBsum; 2I29; -. DR PDBsum; 2I2A; -. DR PDBsum; 2I2B; -. DR PDBsum; 2I2C; -. DR PDBsum; 2I2D; -. DR PDBsum; 2I2F; -. DR PDBsum; 2Q5F; -. DR PDBsum; 3V7U; -. DR PDBsum; 3V7W; -. DR PDBsum; 3V7Y; -. DR PDBsum; 3V80; -. DR PDBsum; 3V8M; -. DR PDBsum; 3V8N; -. DR PDBsum; 3V8P; -. DR PDBsum; 3V8Q; -. DR PDBsum; 3V8R; -. DR PDBsum; 4DY6; -. DR PDBsum; 5DHP; -. DR PDBsum; 5DHQ; -. DR PDBsum; 5DHR; -. DR PDBsum; 5DHS; -. DR PDBsum; 5DHT; -. DR PDBsum; 5DHU; -. DR PDBsum; 5EJF; -. DR PDBsum; 5EJG; -. DR PDBsum; 5EJH; -. DR PDBsum; 5EJI; -. DR PDBsum; 6RBO; -. DR PDBsum; 6RBP; -. DR PDBsum; 6RBQ; -. DR PDBsum; 6RBR; -. DR PDBsum; 6RBS; -. DR PDBsum; 6RBT; -. DR PDBsum; 6RBU; -. DR PDBsum; 6RBV; -. DR PDBsum; 6RBW; -. DR PDBsum; 6RBX; -. DR PDBsum; 6RBY; -. DR PDBsum; 6RBZ; -. DR PDBsum; 6RC0; -. DR PDBsum; 6RC1; -. DR PDBsum; 6RC2; -. DR PDBsum; 6RC3; -. DR PDBsum; 6RC4; -. DR PDBsum; 6RC5; -. DR PDBsum; 6RC6; -. DR PDBsum; 6RG6; -. DR PDBsum; 6RG7; -. DR PDBsum; 6RG8; -. DR PDBsum; 6RG9; -. DR PDBsum; 6RGA; -. DR PDBsum; 6RGB; -. DR PDBsum; 6RGC; -. DR PDBsum; 6RGD; -. DR PDBsum; 6RGE; -. DR PDBsum; 6RGF; -. DR PDBsum; 6RR2; -. DR PDBsum; 6Z61; -. DR PDBsum; 6Z64; -. DR PDBsum; 6Z65; -. DR PDBsum; 7ZZ7; -. DR PDBsum; 7ZZ9; -. DR PDBsum; 7ZZA; -. DR PDBsum; 7ZZB; -. DR PDBsum; 7ZZC; -. DR PDBsum; 7ZZD; -. DR PDBsum; 7ZZE; -. DR PDBsum; 7ZZF; -. DR PDBsum; 7ZZG; -. DR PDBsum; 7ZZH; -. DR PDBsum; 7ZZJ; -. DR PDBsum; 8A9V; -. DR PDBsum; 8B47; -. DR AlphaFoldDB; Q8Y8D7; -. DR SMR; Q8Y8D7; -. DR STRING; 169963.gene:17593624; -. DR BindingDB; Q8Y8D7; -. DR ChEMBL; CHEMBL4523411; -. DR PaxDb; 169963-lmo0968; -. DR EnsemblBacteria; CAC99046; CAC99046; CAC99046. DR GeneID; 986453; -. DR KEGG; lmo:lmo0968; -. DR PATRIC; fig|169963.11.peg.995; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_3_9; -. DR OrthoDB; 9774737at2; -. DR PhylomeDB; Q8Y8D7; -. DR BioCyc; LMON169963:LMO0968-MONOMER; -. DR BRENDA; 2.7.1.23; 3045. DR EvolutionaryTrace; Q8Y8D7; -. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB. DR GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Kinase; NAD; NADP; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..264 FT /note="NAD kinase 1" FT /id="PRO_0000120632" FT ACT_SITE 45 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT BINDING 45..46 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT BINDING 46 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT BINDING 122..123 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" 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:0000305|PubMed:17686780" FT BINDING 158 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT BINDING 161..166 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT BINDING 223 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361, FT ECO:0000269|PubMed:17686780" FT MUTAGEN 45 FT /note="D->N: Only minor changes in the structure and a FT 10-fold decrease in the kinase activity." FT /evidence="ECO:0000269|PubMed:17686780" FT MUTAGEN 223 FT /note="H->E: Twice less active than the wild-type. Its FT activity toward DTA is increased 2-fold." FT /evidence="ECO:0000269|PubMed:17686780, FT ECO:0000269|PubMed:22608967" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:7ZZB" FT TURN 25..28 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 45..54 FT /evidence="ECO:0007829|PDB:7ZZB" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 63..71 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:6RGE" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 83..91 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 96..110 FT /evidence="ECO:0007829|PDB:7ZZB" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:8B47" FT STRAND 115..131 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 133..139 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 142..155 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 158..161 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 178..186 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 189..191 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 207..213 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 217..221 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 224..228 FT /evidence="ECO:0007829|PDB:7ZZB" FT STRAND 230..249 FT /evidence="ECO:0007829|PDB:7ZZB" FT HELIX 253..261 FT /evidence="ECO:0007829|PDB:7ZZB" SQ SEQUENCE 264 AA; 29933 MW; 00E0BCC4CAD30653 CRC64; MKYMITSKGD EKSDLLRLNM IAGFGEYDME YDDVEPEIVI SIGGDGTFLS AFHQYEERLD EIAFIGIHTG HLGFYADWRP AEADKLVKLL AKGEYQKVSY PLLKTTVKYG IGKKEATYLA LNESTVKSSG GPFVVDVVIN DIHFERFRGD GLCMSTPSGT TAYNKSLGGA LMHPSIEAMQ LTEMASINNR VYRTIGSPLV FPKHHVVSLQ PVNDKDFQIS VDHLSILHRD VQEIRYEVSA KKIHFARFRS FPFWRRVHDS FIED //