ID NADK_BIFLS Reviewed; 338 AA. AC B7GTM7; E8MLT0; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; GN Name=nadK {ECO:0000255|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=Blon_1862, BLIJ_1928; OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM OS 1222 / NCTC 11817 / S12). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=391904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=19033196; DOI=10.1073/pnas.0809584105; RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., RA Richardson P.M., Mills D.A.; RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals RT adaptations for milk utilization within the infant microbiome."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., RA Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(2011). 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:0000255|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:0000255|HAMAP-Rule:MF_00361}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00361}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000255|HAMAP- CC 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; CP001095; ACJ52936.1; -; Genomic_DNA. DR EMBL; AP010889; BAJ69507.1; -; Genomic_DNA. DR RefSeq; WP_012578151.1; NZ_JDTT01000009.1. DR AlphaFoldDB; B7GTM7; -. DR SMR; B7GTM7; -. DR KEGG; bln:Blon_1862; -. DR KEGG; blon:BLIJ_1928; -. DR PATRIC; fig|391904.8.peg.1932; -. DR HOGENOM; CLU_008831_0_0_11; -. DR Proteomes; UP000001360; 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: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; Cytoplasm; Kinase; NAD; NADP; Nucleotide-binding; Transferase. FT CHAIN 1..338 FT /note="NAD kinase" FT /id="PRO_1000133558" FT REGION 317..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 66 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 66..67 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 71 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 141..142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 152 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 171 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 182..187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" FT BINDING 206 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00361" SQ SEQUENCE 338 AA; 36342 MW; ABB5814631F57D22 CRC64; MAKRNAVVVT HTRLRQTGTV VAEAVSQLRV AGFEVTIIDN TEAPDFGVQP PCVSDDTEIV VVLGGDGTIL RAAELVHCTQ VPILGVNMGH VGFLAEFESF QIDEAIRRVA THDYSIDERM IAHVDVWLPG ATKPIEDWAL NDITLERADR GKMVELSIRV DDVEMNSFGA DGVIVSTPTG STAYAFSAGG PVMWPNVKAL QLIPLAAHAL FARPLIIGSG STFTIDILDD SMSEGWICCD GRRQRALPQG TRVMVRESRD TLRLARLSGM PFTNRLVSKF DLPVVGWREH ARNEASSQPL HHGHTFPAAA YAAGVAGDAG VAGTEPDKPG ERDGKAGA //