ID A1RXJ9_THEPD Unreviewed; 292 AA. AC A1RXJ9; DT 06-FEB-2007, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Tpen_0523 {ECO:0000313|EMBL:ABL77929.1}; OS Thermofilum pendens (strain DSM 2475 / Hrk 5). OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae; OC Thermofilum. OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77929.1, ECO:0000313|Proteomes:UP000000641}; RN [1] {ECO:0000313|Proteomes:UP000000641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641}; RX PubMed=18263724; DOI=10.1128/JB.01949-07; RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E., RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M., RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B., RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.; RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of RT biosynthetic pathways without genome reduction."; RL J. Bacteriol. 190:2957-2965(2008). 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; CP000505; ABL77929.1; -; Genomic_DNA. DR AlphaFoldDB; A1RXJ9; -. DR STRING; 368408.Tpen_0523; -. DR EnsemblBacteria; ABL77929; ABL77929; Tpen_0523. DR KEGG; tpe:Tpen_0523; -. DR eggNOG; arCOG01348; Archaea. DR HOGENOM; CLU_008831_0_2_2; -. DR OrthoDB; 77798at2157; -. DR Proteomes; UP000000641; 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; 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 {ECO:0000256|HAMAP-Rule:MF_00361}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00361}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00361}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00361}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361}; KW Reference proteome {ECO:0000313|Proteomes:UP000000641}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00361}. FT ACT_SITE 67 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 67..68 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 72 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 136..137 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 146 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 163 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 165 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 173 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 176..181 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 233 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" SQ SEQUENCE 292 AA; 31982 MW; E251C2D1A4BF2159 CRC64; MSFRKVWMKA RANDPVVLEH ARLLYRYLTD RGLDVYVDPL LGHVIPGRSL SELEAREADL GIVVGGDGTL LRTVQKSNAV LPPILGFSSD SLGYLLPHRV DVAREVLEEV LRGNYSERDV ALGEFIAGER AGVFLNEVCV WSEPGKIVEF EVLLNDESLY RVRGDGVIVA TPAGSTGHAF SYGGPVIIDT GQRALEVVFP GALSPLIRPL IVHGGSIAVK VIAHPANLVV DGQVYSKLQE ASKVTVRPSS KSLRFIYVEK YETPLPEKLA RRVLDRGLSY VVSSLFKQTP KP //