ID NADK_PSESM Reviewed; 296 AA. AC Q87YK2; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 111. 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=PSPTO_3793; OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-871 / DC3000; RX PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C., RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M., RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R., RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R., RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., RA Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). 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; AE016853; AAO57262.1; -; Genomic_DNA. DR RefSeq; NP_793567.1; NC_004578.1. DR RefSeq; WP_003382947.1; NC_004578.1. DR AlphaFoldDB; Q87YK2; -. DR SMR; Q87YK2; -. DR STRING; 223283.PSPTO_3793; -. DR GeneID; 64465004; -. DR KEGG; pst:PSPTO_3793; -. DR PATRIC; fig|223283.9.peg.3888; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_1_6; -. DR OrthoDB; 9774737at2; -. DR PhylomeDB; Q87YK2; -. DR Proteomes; UP000002515; 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..296 FT /note="NAD kinase" FT /id="PRO_0000120648" 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 296 AA; 32255 MW; A43DAC72B7DD1127 CRC64; MEQFRNIGII GRLGSVQVLD TVRRLKRFLL DRHLHVILEE TIAEVLPGHG LQTSSRKMLG EVCDMVIVVG GDGSLLGAAR ALARHNVPVL GINRGSLGFL TDIRPDELEV KCAEVLDGHY LVENRFLLQA EVRRHGEAIG QGDALNDVVL HPGKSTRMIE FEIYIDGQFV CSQKADGLIV ATPTGSTAYA LSAGGPIMHP KLDAIVIVPM YPHTLSGRPI VVDGNSELKI VVSKDMTIYP QVSCDGQNHF TCAPGDTITV SKKPQKLRLI HPLDHNYYEV CRTKLGWGSR LGGGGD //