GCW_03105
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Uniprot: A0A0F6CLQ1
Description: inorganic polyphosphate/ATP-NAD kinase EC number: 2.7.1.23 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00549059}. Cofactor: COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00608905}; Enzyme regulation: Function [CC]: FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. {ECO:0000256|HAMAP-Rule:MF_00361}. Pathway: Active site: ACT_SITE 58 58 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00361}. Binding site: BINDING 63 63 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.; BINDING 150 150 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 58 59 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}.; NP_BIND 125 126 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. Site: Gene names (primary): ppnK Gene names (synonym): nadK Mass: 30,706 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; NAD+ kinase activity [GO:0003951]; NAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741] Gene ontology IDs: GO:0003951; GO:0005524; GO:0005737; GO:0006741; GO:0019674; GO:0046872 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000256|SAAS:SAAS00549087}. Protein families: NAD kinase family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHC00024 UniPathway: K00858 CDD: Gene3D: HAMAP: 2.60.200.30;3.40.50.10330 InterPro: MF_00361 PANTHER: IPR017438;IPR017437;IPR016064;IPR002504 PIRSF: PTHR20275 PRINTS: PROSITE: Pfam: ProDom: PF01513 SMART: SUPFAM: TIGRFAMs: SSF111331 738924-739743(-) >nucleotide sequence ATAATCTGCTTGAGATCTTGTTGCACTAATCTCAATCGTCGTTGAACTAAGTCCTTGTCT AATTACAGCTCCATCAGCCACAATTCTTGGACAAGCATCATGATCGCAGTAATTTTCTTT AATCTCGATTCTAATCTTCGTATCAATCGGTAAGATAATTGGTGATTGAATCGTGGTAAA ACTCGAATGTAATAATGGGTATAGTTCAACCATCTGGATCGCTTTAATCCTAGGGAATAA GATTGCGCCATTTGCTGATTTATTAATCCCAGTAGATCCAGTGGTTGTTGAGATTAATAA CCCCGTGCCCCTAAACTTTTGATAAAACTCATTATCAATAAAGATGTCATAACCATAAGC GGTTGTCGAATTAATATTAAATTCGTTTAGAGCATGATGGATCTGATCATCGATCTGCAA CCTAATAAAATCTAATTGCGTGTATTTTAAATGATCTAAATTATTGGCAATCTGATCAAT GTTGGTTTCATTAAACGTCGTATAAAAACCCAGACTACCACCATTGATCCCAATGATCTT TAAGCCAGCACGGTCATATTTGATTGCATTTTTAATAAAAGTGCCATCACCGCCATTAAT AAATAAGTAGTCTGCTACAGTTGGATCATCAACTTCAACTAACTTTTTATTTAGTTCTTT TTTTATTAACGGTTTTAGTGATTCTGATTTTGGTGCTAATGAAGAGATTAAATAATATGT TTTATTCATCTTCTTTTCTTGAACTTGGTGAACTTTCAT >protein sequence FIKNAIKYDRAGLKIIGINGGSLGFYTTFNETNIDQIANNLDHLKYTQLDFIRLQIDDQI HHALNEFNINSTTAYGYDIFIDNEFYQKFRGTGLLISTTTGSTGINKSANGAILFPRIKA IQMVELYPLLHSSFTTIQSPIILPIDTKIRIEIKENYCDHDACPRIVADGAVIRQGLSST TIEISATRSQADYVATTDLRSYMQRLQKTFIY |
© Fisunov Lab of Proteomics, 2016.