ID C7MP17_CRYCD Unreviewed; 301 AA. AC C7MP17; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 02-SEP-2026, 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=Ccur_09610 {ECO:0000313|EMBL:ACU94657.1}; OS Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 / OS 12-3). OC Bacteria; Bacillati; Actinomycetota; Coriobacteriia; Eggerthellales; OC Eggerthellaceae; Cryptobacterium. OX NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94657.1, ECO:0000313|Proteomes:UP000000954}; RN [1] {ECO:0000313|EMBL:ACU94657.1, ECO:0000313|Proteomes:UP000000954} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700683 / DSM 15641 / 12-3 RC {ECO:0000313|Proteomes:UP000000954}; RX PubMed=21304644; DOI=10.40456/sigs.12260; RA Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T., RA Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T., RA Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P., RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.; RT "Complete genome sequence of Cryptobacterium curtum type strain (12-3)."; RL Stand. Genomic Sci. 1:93-100(2009). 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=NAD(+) + ATP = ADP + NADP(+) + H(+); 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|ARBA:ARBA00047925, ECO:0000256|HAMAP- CC 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; CP001682; ACU94657.1; -; Genomic_DNA. DR RefSeq; WP_012803343.1; NC_013170.1. DR AlphaFoldDB; C7MP17; -. DR STRING; 469378.Ccur_09610; -. DR KEGG; ccu:Ccur_09610; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_0_11; -. DR OrthoDB; 9774737at2; -. DR Proteomes; UP000000954; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-ARBA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-ARBA. 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; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1. DR Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 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 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:UP000000954}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00361}. FT ACT_SITE 57 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 57..58 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 62 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 153..154 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 181 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 183 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 194..199 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 218 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" SQ SEQUENCE 301 AA; 31868 MW; A4A06358E8948815 CRC64; MRILIMRNAE SPAAIDASLM LGAYLSSQDI EFTLADAADP EGIIASSFDM AVALGGDGTI LRTAKMIRYS RVPILGINYG HLGFLANGNQ GGVVAASAAA LAGDTVAEER TNLRIFVQCE GDDDDQYESM CAGDADASID DDFAISRCLF ALNEAALTRG ALGWMIDCEL SISGSLVGTV RGDGMVISTA TGSTAYALSA GGPLVAPNFR GLVVVPVAPH SLIARAVVTD PHDIVELTLG DTRGDHEAQL FVDGLAVEFP APIKRLRVQR GPEPTILLRY QGESFYTLLR TTFFEHTEPV D //