ID A0A2N0UTD6_9FIRM Unreviewed; 285 AA. AC A0A2N0UTD6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 16-JAN-2019, entry version 6. DE RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS01084339}; DE EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS01084342}; 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=RB5AMG_00677 {ECO:0000313|EMBL:PKD30272.1}; OS Ruminococcus bromii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; 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., RA Walker A.W., Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., RA Louis P., Koropatkin N., Cockburn D., Kibler R., Cooper P.J., RA Sandoval C., Crost E., Juge N., 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 RT Ruminococcus bromii."; RL Environ. Microbiol. 0:0-0(2017). CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC of 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, ECO:0000256|SAAS:SAAS01092643}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); CC Xref=Rhea:RHEA:18629, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; CC EC=2.7.1.23; Evidence={ECO:0000256|HAMAP-Rule:MF_00361, CC ECO:0000256|SAAS:SAAS01120179}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00361, CC ECO:0000256|SAAS:SAAS01092646}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361, CC ECO:0000256|SAAS:SAAS01092648}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00361, ECO:0000256|SAAS:SAAS01084379}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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; NNBY01000031; PKD30272.1; -; Genomic_DNA. DR Proteomes; UP000233562; 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: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; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 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 Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000256|SAAS:SAAS01084347}; KW Complete proteome {ECO:0000313|Proteomes:UP000233562}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000256|SAAS:SAAS01092644}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000256|SAAS:SAAS00103427, ECO:0000313|EMBL:PKD30272.1}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00103431}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00103470}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000256|SAAS:SAAS01084333}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000256|SAAS:SAAS00103430, ECO:0000313|EMBL:PKD30272.1}. FT NP_BIND 69 70 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT NP_BIND 141 142 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT NP_BIND 182 187 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT ACT_SITE 69 69 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00361}. FT BINDING 74 74 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT BINDING 152 152 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT BINDING 169 169 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT BINDING 171 171 NAD. {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 //