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MGP007053

UniProt Annotations

Entry Information

Gene Name	nicotinamide nucleotide adenylyltransferase 3
Protein Entry	NMNA3_HUMAN
UniProt ID	Q96T66
Species	Human

Comments

Comment type	Description
Alternative Products	Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q96T66-1; Sequence=Displayed; Name=2; IsoId=Q96T66-2; Sequence=VSP_010267; Note=No experimental confirmation available.; Name=3; IsoId=Q96T66-3; Sequence=VSP_043203; Note=No experimental confirmation available.;
Biophysicochemical Properties	Kinetic parameters: KM=209 uM for NMN {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=130 uM for NAD(+) {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=29 uM for ATP {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=390 uM for PPi {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=276 uM for GTP {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=350 uM for ITP {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=111 uM for NaMN {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=130 uM for NMNH {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; KM=2.01 uM for triazofurin monophosphate {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; Vmax=3.6 umol/min/mg enzyme for NAD synthesis {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; Vmax=12.8 umol/min/mg enzyme for pyrophosphorolytic NAD(+) cleavage {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}; Vmax=2.9 umol/min/mg enzyme for pyrophosphorolytic NADH cleavage {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747};
Catalytic Activity	ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+).
Catalytic Activity	ATP + nicotinamide ribonucleotide = diphosphate + NAD(+).
Cofactor	Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:17402747}; Note=Divalent metal cations. Mg(2+) confers the highest activity. {ECO:0000269\|PubMed:17402747};
Enzyme Regulation	Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')- tetraphosphate (Nap4AD). {ECO:0000269\|PubMed:17402747}.
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. {ECO:0000269\|PubMed:16118205, ECO:0000269\|PubMed:17402747}.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Similarity	Belongs to the eukaryotic NMN adenylyltransferase family. {ECO:0000305}.
Subcellular Location	Mitochondrion {ECO:0000269\|PubMed:12574164, ECO:0000269\|PubMed:16118205}.
Subunit	Homotetramer. {ECO:0000269\|PubMed:12574164}.
Tissue Specificity	Expressed in lung and spleen with lower levels in placenta and kidney. {ECO:0000269\|PubMed:12574164, ECO:0000269\|PubMed:16118205}.