ID C7MC96_BRAFD Unreviewed; 314 AA. AC C7MC96; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 02-SEP-2026, entry version 88. 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=Bfae_13660 {ECO:0000313|EMBL:ACU85203.1}; OS Brachybacterium faecium (strain ATCC 43885 / DSM 4810 / JCM 11609 / LMG OS 19847 / NBRC 14762 / NCIMB 9860 / 6-10). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Dermabacteraceae; Brachybacterium. OX NCBI_TaxID=446465 {ECO:0000313|EMBL:ACU85203.1, ECO:0000313|Proteomes:UP000001919}; RN [1] {ECO:0000313|EMBL:ACU85203.1, ECO:0000313|Proteomes:UP000001919} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43885 / DSM 4810 / JCM 11609 / LMG 19847 / NBRC 14762 / RC NCIMB 9860 / 6-10 {ECO:0000313|Proteomes:UP000001919}; RX PubMed=21304631; DOI=10.4056/sigs.492; RA Lapidus A., Pukall R., Labuttii K., Copeland A., Del Rio T.G., Nolan M., RA Chen F., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., RA Rohde M., Goker M., Pati A., Ivanova N., Mavrommatis K., Chen A., RA Palaniappan K., D'haeseleer P., Chain P., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Brachybacterium faecium type strain RT (Schefferle 6-10)."; RL Stand. Genomic Sci. 1:3-11(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; CP001643; ACU85203.1; -; Genomic_DNA. DR AlphaFoldDB; C7MC96; -. DR STRING; 446465.Bfae_13660; -. DR KEGG; bfa:Bfae_13660; -. DR PATRIC; fig|446465.5.peg.1364; -. DR eggNOG; COG0061; Bacteria. DR HOGENOM; CLU_008831_0_0_11; -. DR OrthoDB; 9774737at2; -. DR Proteomes; UP000001919; 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 NCBIfam; NF002892; PRK03372.1; 1. 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:UP000001919}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00361}. FT ACT_SITE 85 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 85..86 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 90 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 160..161 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 171 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 190 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 201..206 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 225 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" SQ SEQUENCE 314 AA; 34122 MW; 3A978911650A0BE7 CRC64; MRRFLLYVHT GRRAALRAML SVLEELRLRN VRAVVVDEQV EEILALPEDM APPKLITFLT NGAVDVRAAV SAADVVELGI VLGGDGTILR ALEAVREADI PVHGVNLGHV GFLAESEVED LSITVARLLD GDYDIEKRST LDITVLDSED ELVDHHWALN EASLEKADRQ KMINVAIEID GRPVSSFGAD GVLLSTSTGS TAYAFSAGGP VIWPEVDAMM LIPLAAHALF ARPLVLGRSS EAAVEMTLDN REDGILTLDG RRGADITAGM RIEARLSPRS VRLARLAPTP FADRLVEKFQ LPVVGWRGRG PRTR //