ID NADK_PYRAB Reviewed; 277 AA. AC Q9V081; G8ZI77; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 127. 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=PYRAB09100; ORFNames=PAB1756; OS Pyrococcus abyssi (strain GE5 / Orsay). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=272844; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GE5 / Orsay; RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x; RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., RA Weissenbach J., Zivanovic Y., Forterre P.; RT "An integrated analysis of the genome of the hyperthermophilic archaeon RT Pyrococcus abyssi."; RL Mol. Microbiol. 47:1495-1512(2003). RN [2] RP GENOME REANNOTATION. RC STRAIN=GE5 / Orsay; RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x; RA Gao J., Wang J.; RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and RT Pyrococcus furiosus DSM 3638."; RL Curr. Microbiol. 64:118-129(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}. 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; AJ248285; CAB49824.1; -; Genomic_DNA. DR EMBL; HE613800; CCE70318.1; -; Genomic_DNA. DR PIR; G75138; G75138. DR RefSeq; WP_010868033.1; NC_000868.1. DR AlphaFoldDB; Q9V081; -. DR SMR; Q9V081; -. DR STRING; 272844.PAB1756; -. DR GeneID; 1496262; -. DR KEGG; pab:PAB1756; -. DR PATRIC; fig|272844.11.peg.963; -. DR eggNOG; arCOG01348; Archaea. DR HOGENOM; CLU_008831_0_3_2; -. DR OrthoDB; 77798at2157; -. DR PhylomeDB; Q9V081; -. DR Proteomes; UP000000810; Chromosome. DR Proteomes; UP000009139; 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 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:SF43; BIFUNCTIONAL NADP PHOSPHATASE_NAD KINASE; 1. DR PANTHER; PTHR20275; 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; Transferase. FT CHAIN 1..277 FT /note="NAD kinase" FT /id="PRO_0000120705" FT ACT_SITE 67 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 67..68 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 72 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 137..138 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 165 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 167 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 178..183 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 236 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 277 AA; 31673 MW; 1A93BF709D5C5EF4 CRC64; MRFGIVARRD REEALKLAYR VYDYLKVRGY DAIVDSETYE HFPHFKEEDI AKLEEFDVDF IIAIGGDGTI LRIEHKTKKD IPILSINMGT LGFLTEVEPS ETFFAINRLL RGEYYIDERI KLRTYINGEA RIPDALNEVA ILTGIPGKVI HLRYYVDGGL ADEVRADGLV VATPTGSTGY AMSAGGPFVD PRLDTIIIAP LLPLPRTSVP MVVPGYSKIE IEFVTKREVI LAVDGQYYEH LSPDIKIRIE KSPRKTKFVR FTREIYPKYT MRIKERH //