ID NADK_AZOVD Reviewed; 295 AA. AC C1DPY6; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 02-SEP-2026, entry version 78. 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=Avin_34070; OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=322710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ / ATCC BAA-1303; RX PubMed=19429624; DOI=10.1128/jb.00504-09; RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G., RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L., RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A., RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S., RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I., RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L., RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., RA Dean D.R., Dixon R., Wood D.; RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized RT to support diverse anaerobic metabolic processes."; RL J. Bacteriol. 191:4534-4545(2009). 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; CP001157; ACO79557.1; -; Genomic_DNA. DR RefSeq; WP_012701937.1; NC_012560.1. DR AlphaFoldDB; C1DPY6; -. DR SMR; C1DPY6; -. DR STRING; 322710.Avin_34070; -. DR EnsemblBacteria; ACO79557; ACO79557; Avin_34070. DR GeneID; 309096496; -. DR KEGG; avn:Avin_34070; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_1_6; -. DR OrthoDB; 9774737at2; -. DR Proteomes; UP000002424; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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 FunFam; 2.60.200.30:FF:000001; NAD kinase; 1. 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; NF002306; PRK01231.1; 1. 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..295 FT /note="NAD kinase" FT /id="PRO_1000205411" FT ACT_SITE 72 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 72..73 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 146..147 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 157 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 174 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 187..192 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 247 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 295 AA; 32299 MW; 1CAEF6CE5CF0DE33 CRC64; MEHFRNIGII GRLGSTQVVD TIRRLKRFLL DRHLHVILDE GIAELLPGHG LQVSSRKQLG EVCDMVVVVG GDGSMLGAAR ALARYKVPVL GINRGSLGFL TDIRPDELET RVAEVLDGQY TVESRFLLET QVRRKLEPIG QGDALNDVVL HPGKSTRMIE FELYIDGQFV CSQKSDGLIV STPTGSTAYA LSAGGPIMHP KLDAIVIVPM YPHTLSSRPI VVAGNSELKI VVSPKMDIYP QVSCDGQNHF TCSPGDIVTI SKKPQRLQLI HPLDHNYYEV CRTKLGWGSR LGGGS //