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MGP005793

UniProt Annotations

Entry Information
Gene Namenicotinamide nucleotide adenylyltransferase 1
Protein EntryNMNA1_HUMAN
UniProt IDQ9HAN9
SpeciesHuman
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=34 uM for NMN {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; KM=40 uM for ATP {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; KM=937 uM for PPi {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; KM=59 uM for NAD(+) {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; Vmax=25 umol/min/mg enzyme for NAD synthesis {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; Vmax=60.5 umol/min/ug enzyme for NAD(+) cleavage {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}; Vmax=8.5 umol/min/ug enzyme for NADH cleavage {ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747};
Catalytic ActivityATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+).
Catalytic ActivityATP + nicotinamide ribonucleotide = diphosphate + NAD(+). {ECO:0000269|PubMed:11027696}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:17402747}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:17402747}; Note=Divalent metal cations. Zn(2+) confers higher activity as compared to Mg(2+). {ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:17402747};
DiseaseLeber congenital amaurosis 9 (LCA9) [MIM:608553]: A severe dystrophy of the retina, typically becoming evident in the first years of life. Visual function is usually poor and often accompanied by nystagmus, sluggish or near-absent pupillary responses, photophobia, high hyperopia and keratoconus. {ECO:0000269|PubMed:22842227, ECO:0000269|PubMed:22842229, ECO:0000269|PubMed:22842230, ECO:0000269|PubMed:22842231}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Enzyme RegulationActivity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')- tetraphosphate (Nap4AD). {ECO:0000269|PubMed:17402747}.
FunctionCatalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following mechanical or toxic insults. {ECO:0000269|PubMed:17402747}.
InteractionQ96EB6:SIRT1; NbExp=3; IntAct=EBI-3917542, EBI-1802965;
PathwayCofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
SimilarityBelongs to the eukaryotic NMN adenylyltransferase family. {ECO:0000305}.
Subcellular LocationNucleus {ECO:0000269|PubMed:11248244, ECO:0000269|PubMed:12574164, ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:22842230}.
SubunitHomohexamer. Interacts with ADPRT/PARP1. {ECO:0000269|PubMed:11248244, ECO:0000269|PubMed:11751893}.
Tissue SpecificityWidely expressed with highest levels in skeletal muscle, heart and kidney. Also expressed in the liver pancreas and placenta. Widely expressed throughout the brain. {ECO:0000269|PubMed:11027696, ECO:0000269|PubMed:11891043}.
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