ID NADK1_OCEIH Reviewed; 267 AA. AC Q8ERS9; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 111. 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=OB1221; OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / OS KCTC 3954 / HTE831). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=221109; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831; RX PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge RT and its unexpected adaptive capabilities to extreme environments."; RL Nucleic Acids Res. 30:3927-3935(2002). 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; BA000028; BAC13177.1; -; Genomic_DNA. DR RefSeq; WP_011065620.1; NC_004193.1. DR AlphaFoldDB; Q8ERS9; -. DR SMR; Q8ERS9; -. DR STRING; 221109.gene:10733460; -. DR KEGG; oih:OB1221; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_3_9; -. DR OMA; NGIERMS; -. DR OrthoDB; 9774737at2; -. DR PhylomeDB; Q8ERS9; -. DR Proteomes; UP000000822; 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_0000120642" 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 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; 30240 MW; A76087334F01B60A CRC64; MNFKIVSKGD DRSEKIKAMM RQYLSEFGLT YDKETPDLVI SVGGDGTFLE AFHRYVHRLE DTAFIGIHTG HLGFYTDWTP KDVERLIIEI AKTPFQTVEY PLLEVIIRAK AGGKEDRILA LNEAMIKTAD GSSVVFDVEI KGEHFETFRG DGICISTPSG STAYNKALGG AILHPSLEAI QITENASINN RVFRTIGSPL ILPKHHTCFL KPMVDSSFLI QIDHFTKNYQ NVKSIQCRVA KEKVRFARFK QFPFWNRVRD SFVSEEG //