Names & Taxonomy
- Uniprot ID:
- Q96T66
- Entry Name:
- NMNA3_HUMAN
- Status:
- reviewed
- Protein Names:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 (NMN/NaMN adenylyltransferase 3) (Nicotinamide-nucleotide adenylyltransferase 3) (NMN adenylyltransferase 3) (Nicotinate-nucleotide adenylyltransferase 3) (NaMN adenylyltransferase 3) (EC 2.7.7.18) (Pyridine nucleotide adenylyltransferase 3) (PNAT-3) (EC 2.7.7.1)
- Gene Names:
- NMNAT3 FKSG76
- Gene Names Orf:
- FKSG76
- Gene Names Primary:
- NMNAT3
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 252
- Sequence:
- MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Mitochondrion
Function
- 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 D-ribonucleotide: step 1/1.; Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
- Catalytic Activity:
- ATP + nicotinamide ribonucleotide = diphosphate + NAD(+).; ATP + beta-nicotinate-D-ribonucleotide = diphosphate + deamido-NAD(+).
- Cofactor:
- COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
- Kinetics:
- BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=209 uM for NMN
- Enzyme Regulation:
- ENZYME REGULATION: Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).
- Gene Ontology Go:
- cytosol
mitochondrion
ATP binding
nicotinamide-nucleotide adenylyltransferase activity
nicotinate-nucleotide adenylyltransferase activity
'de novo' NAD biosynthetic process from aspartate
NAD biosynthetic process
NAD metabolic process
response to wounding
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process - Gene Ontology Biological Process:
- 'de novo' NAD biosynthetic process from aspartate
NAD biosynthetic process
NAD metabolic process
response to wounding
small molecule metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process - Gene Ontology Molecular Function:
- ATP binding
nicotinamide-nucleotide adenylyltransferase activity
nicotinate-nucleotide adenylyltransferase activity - Gene Ontology Cellular Component:
- cytosol
mitochondrion - Keywords:
- 3D-structure
ATP-binding
Alternative splicing
Complete proteome
Magnesium
Mitochondrion
NAD
Nucleotide-binding
Nucleotidyltransferase
Pyridine nucleotide biosynthesis
Reference proteome
Transferase