ID A0A2N0UTD6_9FIRM Unreviewed; 285 AA. AC A0A2N0UTD6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 08-NOV-2023, entry version 20. 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=ppnK {ECO:0000313|EMBL:PKD30272.1}; GN Synonyms=nadK {ECO:0000256|HAMAP-Rule:MF_00361}; GN ORFNames=DW802_06625 {ECO:0000313|EMBL:RHD25156.1}, DW960_07090 GN {ECO:0000313|EMBL:RGZ96551.1}, GMC96_01050 GN {ECO:0000313|EMBL:MTR78239.1}, RB5AMG_00677 GN {ECO:0000313|EMBL:PKD30272.1}; OS Ruminococcus bromii. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD30272.1, ECO:0000313|Proteomes:UP000233562}; RN [1] {ECO:0000313|EMBL:PKD30272.1, ECO:0000313|Proteomes:UP000233562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5AMG {ECO:0000313|EMBL:PKD30272.1, RC ECO:0000313|Proteomes:UP000233562}; RX PubMed=29159997; RA Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., Walker A.W., RA Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., Louis P., Koropatkin N., RA Cockburn D., Kibler R., Cooper P.J., Sandoval C., Crost E., Juge N., RA Bayer E.A., Flint H.J.; RT "Sporulation capability and amylosome conservation among diverse human RT colonic and rumen isolates of the keystone starch-degrader Ruminococcus RT bromii."; RL Environ. Microbiol. 0:0-0(2017). RN [2] {ECO:0000313|Proteomes:UP000284544, ECO:0000313|Proteomes:UP000285083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM32-13AC {ECO:0000313|EMBL:RHD25156.1, RC ECO:0000313|Proteomes:UP000284544}, and AM46-2BH RC {ECO:0000313|EMBL:RGZ96551.1, ECO:0000313|Proteomes:UP000285083}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:MTR78239.1, ECO:0000313|Proteomes:UP000432256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIOML-A2 {ECO:0000313|EMBL:MTR78239.1, RC ECO:0000313|Proteomes:UP000432256}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). 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|ARBA:ARBA00001262, 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKD30272.1}. 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; WNAH01000001; MTR78239.1; -; Genomic_DNA. DR EMBL; NNBY01000031; PKD30272.1; -; Genomic_DNA. DR EMBL; QSEV01000005; RGZ96551.1; -; Genomic_DNA. DR EMBL; QSIY01000001; RHD25156.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2N0UTD6; -. DR EnsemblBacteria; PKD30272; PKD30272; RB5AMG_00677. DR Proteomes; UP000233562; Unassembled WGS sequence. DR Proteomes; UP000284544; Unassembled WGS sequence. DR Proteomes; UP000285083; Unassembled WGS sequence. DR Proteomes; UP000432256; Unassembled WGS sequence. 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:0051287; F:NAD binding; IEA:UniProt. 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00361}. FT ACT_SITE 69 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 69..70 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 74 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 141..142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" FT BINDING 169 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 182..187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00361" SQ SEQUENCE 285 AA; 31754 MW; B1156BD2D40B3ADA CRC64; MKFALVVNLS KERAIKYAKK ISLFLLDKNA EIAMIEECSQ YFKGIHIHYS KNITELFEYC DMAITVGGDG TIIHAAKYAA KADKQLIGVN VGRLGFAADV EPHEYEQLER LITGDYTTEE RILLDVEVIK EDGSKHYLAV NDAVVARGQL SKTIDLHLTL DGDEISKYRA DGLLFATPTG STAYSLSAGG PILAPKMECI LMTPVCPHSL FSRSVLFSGE SELSVHVKIP EECCCVLTID GEKNVPVLAT DRVVIRKSDL KLKLALLHNR NFYKLLNEKL KERDF //