ID D0KMU6_SACS9 Unreviewed; 249 AA. AC D0KMU6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 26-FEB-2020, entry version 54. DE RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361}; GN Name=nadK {ECO:0000256|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=Ssol_0037 {ECO:0000313|EMBL:ACX90342.1}; OS Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=555311 {ECO:0000313|EMBL:ACX90342.1, ECO:0000313|Proteomes:UP000001493}; RN [1] {ECO:0000313|EMBL:ACX90342.1, ECO:0000313|Proteomes:UP000001493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98/2 {ECO:0000313|EMBL:ACX90342.1, RC ECO:0000313|Proteomes:UP000001493}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Mead D.; RT "Complete sequence of Sulfolobus solfataricus 98/2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_00361}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00361}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00361}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP001800; ACX90342.1; -; Genomic_DNA. DR RefSeq; WP_009992063.1; NZ_ACUK01000288.1. DR SMR; D0KMU6; -. DR EnsemblBacteria; ACX90342; ACX90342; Ssol_0037. DR GeneID; 38466655; -. DR KEGG; sol:Ssol_0037; -. DR HOGENOM; CLU_008831_0_3_2; -. DR KO; K00858; -. DR OMA; VNLGHVG; -. DR OrthoDB; 104144at2157; -. DR BioCyc; SSOL555311:G1GGG-36-MONOMER; -. DR Proteomes; UP000001493; 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: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 Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 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 Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000313|EMBL:ACX90342.1}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00361}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00361}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000313|EMBL:ACX90342.1}. FT NP_BIND 45..46 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT NP_BIND 110..111 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT NP_BIND 149..154 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT ACT_SITE 45 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 50 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 138 FT /note="NAD" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" SQ SEQUENCE 249 AA; 27890 MW; D4AD6A9F7DCD8A49 CRC64; MRVKIVSKPT SQLNYTVEKI KNISNKLGFE VVDIDFDYVI AVGGDGTLLR AVKLGKPVIA IKAGRRGLLM DVPVDKIEDA LLRLKKGDYN EEEYMLLEMV HNDKVELGFN EIGILYDRPE AIKVGISFDT ERVSVEGDGV LVSTPQGSSG WGMSATNSLL YKDLNAIEII FVNPIFYYLR SVVIPPKSLI LRLEDKGYPQ TARVVVDGEV VTLIKTNQEI TVRVSQHKAK ILRFFKLDLI GEVLHAYHI //