catalytic activity:ATP + nicotinamide ribonucleotide = diphosphate + NAD(+).,catalytic activity:ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD(+).,cofactor:Divalent metal cations. Magnesium confers the highest activity.,enzyme regulation:Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).,function:Catalyzes 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. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following injury.,pathway:Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide ribonucleotide: step 1/1.,similarity:Belongs to the eukaryotic NMN adenylyltransferase family.,subunit:Homotetramer.,tissue specificity:Expressed in lung and spleen with lower levels in placenta and kidney.,
Mitochondrion .
Expressed in lung and spleen with lower levels in placenta and kidney.