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Identification
HMDB Protein ID HMDBP00335
Secondary Accession Numbers
  • 5571
  • HMDBP10464
Name Nicotinamide mononucleotide adenylyltransferase 1
Synonyms
  1. NMN adenylyltransferase 1
  2. NaMN adenylyltransferase 1
  3. Nicotinate-nucleotide adenylyltransferase 1
  4. SubName: Nicotinamide nucleotide adenylyltransferase 1, isoform CRA_a
  5. SubName: cDNA, FLJ96727, Homo sapiens nicotinamide nucleotide adenylyltransferase 1(NMNAT1), mRNA
Gene Name NMNAT1
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. 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.
Pathways
  • NAD(+) biosynthesis
  • Nicotinate and nicotinamide metabolism
Reactions
Adenosine triphosphate + beta-nicotinamide D-ribonucleotide → 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
nucleoplasm
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
nucleotidyltransferase activity
Molecular Function
ATP binding
nicotinamide-nucleotide adenylyltransferase activity
nicotinate-nucleotide adenylyltransferase activity
Process
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. Nucleus
Gene Properties
Chromosome Location 1
Locus 1p36.22
SNPs NMNAT1
Gene Sequence
>840 bp
ATGGAAAATTCCGAGAAGACTGAAGTGGTTCTCCTTGCTTGTGGTTCATTCAATCCCATC
ACCAACATGCACCTCAGGTTGTTTGAGCTGGCCAAGGACTACATGAATGGAACAGGAAGG
TACACAGTTGTCAAAGGCATCATCTCTCCTGTTGGTGATGCCTACAAGAAGAAAGGACTC
ATTCCTGCCTATCACCGGGTCATCATGGCAGAACTTGCTACCAAGAATTCTAAATGGGTG
GAAGTTGATACATGGGAAAGTCTTCAGAAGGAGTGGAAAGAGACTCTGAAGGTGCTAAGA
CACCATCAAGAGAAATTGGAGGCTAGTGACTGTGATCACCAGCAGAACTCACCTACTCTA
GAAAGGCCTGGAAGGAAGAGGAAGTGGACTGAAACACAAGATTCTAGTCAAAAGAAATCC
CTAGAGCCAAAAACAAAAGCTGTGCCAAAGGTCAAGCTGCTGTGTGGGGCAGATTTATTG
GAGTCCTTTGCTGTTCCCAATTTGTGGAAGAGTGAAGACATCACCCAAATCGTGGCCAAC
TATGGGCTCATATGTGTTACTCGGGCTGGAAATGATGCTCAGAAGTTTATCTATGAATCG
GATGTGCTGTGGAAACACCGGAGCAACATTCACGTGGTGAATGAATGGATCGCTAATGAC
ATCTCATCCACAAAAATCCGGAGAGCCCTCAGAAGGGGCCAGAGCATTCGCTACTTGGTA
CCAGATCTTGTCCAAGAATACATTGAAAAGCATAATTTGTACAGCTCTGAGAGTGAAGAC
AGGAATGCTGGGGTCATCCTGGCCCCTTTGCAGAGAAACACTGCAGAAGCTAAGACATAG
Protein Properties
Number of Residues 279
Molecular Weight 31932.22
Theoretical pI 8.86
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Nicotinamide mononucleotide adenylyltransferase 1
MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGL
IPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTL
ERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVAN
YGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLV
PDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT
GenBank ID Protein 189055023
UniProtKB/Swiss-Prot ID Q9HAN9
UniProtKB/Swiss-Prot Entry Name NMNA1_HUMAN
PDB IDs
GenBank Gene ID AF314163
GeneCard ID NMNAT1
GenAtlas ID NMNAT1
HGNC ID HGNC:17877
References
General References
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  3. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Schweiger M, Hennig K, Lerner F, Niere M, Hirsch-Kauffmann M, Specht T, Weise C, Oei SL, Ziegler M: Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis. FEBS Lett. 2001 Mar 9;492(1-2):95-100. [PubMed:11248244 ]
  6. Emanuelli M, Carnevali F, Saccucci F, Pierella F, Amici A, Raffaelli N, Magni G: Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase. J Biol Chem. 2001 Jan 5;276(1):406-12. [PubMed:11027696 ]
  7. Fernando FS, Conforti L, Tosi S, Smith AD, Coleman MP: Human homologue of a gene mutated in the slow Wallerian degeneration (C57BL/Wld(s)) mouse. Gene. 2002 Feb 6;284(1-2):23-9. [PubMed:11891043 ]
  8. 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 ]
  9. 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 ]
  10. 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 ]
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  12. Garavaglia S, D'Angelo I, Emanuelli M, Carnevali F, Pierella F, Magni G, Rizzi M: Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis. J Biol Chem. 2002 Mar 8;277(10):8524-30. Epub 2001 Dec 19. [PubMed:11751893 ]
  13. Zhou T, Kurnasov O, Tomchick DR, Binns DD, Grishin NV, Marquez VE, Osterman AL, Zhang H: Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin. J Biol Chem. 2002 Apr 12;277(15):13148-54. Epub 2002 Jan 11. [PubMed:11788603 ]