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Showing Protein Nicotinamide mononucleotide adenylyltransferase 2 (HMDBP00338)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 9 metabolites
Identification
HMDB Protein ID HMDBP00338
Secondary Accession Numbers
  • 5574
Name Nicotinamide mononucleotide adenylyltransferase 2
Synonyms
  1. NMN adenylyltransferase 2
  2. NaMN adenylyltransferase 2
  3. Nicotinate-nucleotide adenylyltransferase 2
Gene Name NMNAT2
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 but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+).
Pathways
  • NAD(+) biosynthesis
  • Nicotinate and nicotinamide metabolism
  • Nicotinate and nicotinamide metabolism
Reactions
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
nucleus
trans-Golgi network
late endosome
Golgi membrane
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. Cytoplasm
  2. Golgi apparatus
Gene Properties
Chromosome Location 1
Locus 1q25
SNPs NMNAT2
Gene Sequence 
>924 bp
ATGACCGAGACCACCAAGACCCACGTTATCTTGCTCGCCTGCGGCAGCTTCAATCCCATC
ACCAAAGGGCACATTCAGATGTTTGAAAGAGCCAGGGATTATCTGCACAAAACTGGAAGG
TTTATTGTGATTGGCGGGATTGTCTCCCCTGTCCACGACTCCTATGGAAAACAGGGCCTC
GTGTCAAGCCGGCACCGTCTCATCATGTGTCAGCTGGCCGTCCAGAATTCTGATTGGATC
AGGGTGGACCCTTGGGAGTGCTACCAGGACACCTGGCAGACGACCTGCAGCGTGTTGGAA
CACCACCGGGACCTCATGAAGAGGGTGACTGGCTGCATCCTCTCCAATGTCAACACACCT
TCCATGACACCTGTGATCGGACAGCCACAAAACGAGACCCCCCAGCCCATTTACCAGAAC
AGCAACGTGGCCACCAAGCCCACTGCAGCCAAGATCTTGGGGAAGGTGGGAGAAAGCCTC
AGCCGGATCTGCTGTGTCCGCCCGCCGGTGGAGCGTTTCACCTTTGTAGATGAGAATGCC
AATCTGGGCACGGTGATGCGGTATGAAGAGATTGAGCTACGGATCCTGCTGCTGTGTGGT
AGTGACCTGCTGGAGTCCTTCTGCATCCCAGGGCTCTGGAACGAGGCAGATATGGAGGTG
ATTGTTGGTGACTTTGGGATTGTGGTGGTGCCCCGGGATGCAGCCGACACAGACCGAATC
ATGAATCACTCCTCAATACTCCGCAAATACAAAAACAACATCATGGTGGTGAAGGATGAC
ATCAACCATCCCATGTCTGTTGTCAGCTCAACCAAGAGCAGGCTGGCCCTGCAGCATGGG
GACGGCCATGTTGTGGATTACCTGTCCCAGCCGGTCATCGACTACATCCTCAAAAGCCAG
CTGTACATCAATGCCTCCGGCTAG
Protein Properties
Number of Residues 307
Molecular Weight 34438.38
Theoretical pI 7.06
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Nicotinamide mononucleotide adenylyltransferase 2
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG
GenBank ID Protein 24307989
UniProtKB/Swiss-Prot ID Q9BZQ4
UniProtKB/Swiss-Prot Entry Name NMNA2_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_015039.2
GeneCard ID NMNAT2
GenAtlas ID NMNAT2
HGNC ID HGNC:16789
References
General References
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  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 ]
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