Names & Taxonomy
- Uniprot ID:
- Q9HAN9
- Entry Name:
- NMNA1_HUMAN
- Status:
- reviewed
- Protein Names:
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide-nucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1)
- Gene Names:
- NMNAT1 NMNAT
- Gene Names Primary:
- NMNAT1
- Organism:
- Homo sapiens (Human)
Structure
- Length:
- 279
- Sequence:
- MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT
- Proteomes:
- UP000005640
Subcellular location
- Subcellular Location:
- Nucleus
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. 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.
- 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(+).
- Cofactor:
- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
- Kinetics:
- BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=34 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:
- nucleoplasm
nucleus
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:
- nucleoplasm
nucleus - Keywords:
- 3D-structure
ATP-binding
Complete proteome
Direct protein sequencing
Disease mutation
Leber congenital amaurosis
Magnesium
NAD
Nucleotide-binding
Nucleotidyltransferase
Nucleus
Phosphoprotein
Pyridine nucleotide biosynthesis
Reference proteome
Transferase
Zinc - Interacts With:
- P24863; Q6NVW7; Q96EB6