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HMDB Protein ID HMDBP00336
Secondary Accession Numbers
  • 5572
  • HMDBP03898
Name Nicotinamide mononucleotide adenylyltransferase 3
  1. NMN adenylyltransferase 3
  2. NaMN adenylyltransferase 3
  3. Nicotinate-nucleotide adenylyltransferase 3
  4. PNAT-3
  5. Pyridine nucleotide adenylyltransferase 3
Gene Name NMNAT3
Protein Type Unknown
Biological Properties
General Function Involved in nucleotidyltransferase activity
Specific 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.
  • NAD(+) biosynthesis
  • Nicotinate and nicotinamide metabolism
Adenosine triphosphate + Nicotinamide ribotide → Pyrophosphate + NAD details
Adenosine triphosphate + beta-nicotinate-D-ribonucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotide details
Adenosine triphosphate + Nicotinic acid mononucleotide → Pyrophosphate + Nicotinic acid adenine dinucleotide details
GO Classification
Biological Process
NAD biosynthetic process
water-soluble vitamin metabolic process
Cellular Component
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
Molecular Function
ATP binding
nicotinamide-nucleotide adenylyltransferase activity
nicotinate-nucleotide adenylyltransferase activity
metabolic process
coenzyme biosynthetic process
pyridine nucleotide biosynthetic process
nicotinamide nucleotide biosynthetic process
nad biosynthetic process
cellular metabolic process
biosynthetic process
cofactor metabolic process
coenzyme metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 3
Locus 3q23
Gene Sequence
>759 bp
Protein Properties
Number of Residues 252
Molecular Weight 18255.08
Theoretical pI 9.217
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Nicotinamide mononucleotide adenylyltransferase 3
GenBank ID Protein 14029540
UniProtKB/Swiss-Prot ID Q96T66
UniProtKB/Swiss-Prot Entry Name NMNA3_HUMAN
GenBank Gene ID AF345564
GeneCard ID NMNAT3
GenAtlas ID NMNAT3
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Zhang X, Kurnasov OV, Karthikeyan S, Grishin NV, Osterman AL, Zhang H: Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis. J Biol Chem. 2003 Apr 11;278(15):13503-11. Epub 2003 Feb 6. [PubMed:12574164 ]
  3. Berger F, Lau C, Dahlmann M, Ziegler M: Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J Biol Chem. 2005 Oct 28;280(43):36334-41. Epub 2005 Aug 23. [PubMed:16118205 ]
  4. Sorci L, Cimadamore F, Scotti S, Petrelli R, Cappellacci L, Franchetti P, Orsomando G, Magni G: Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis. Biochemistry. 2007 Apr 24;46(16):4912-22. Epub 2007 Apr 3. [PubMed:17402747 ]