Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01304
Entry Name
UniProt Accession
Theoretical PI
6.59
Molecular Weight
34438.63
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Nicotinamide mononucleotide adenylyltransferase 2
Protein Synonyms/Alias
NMN adenylyltransferase 2; 2.7.7.1; Nicotinate-nucleotide adenylyltransferase 2; NaMN adenylyltransferase 2; 2.7.7.18;
Gene Name
NMNAT2
Gene Synonyms/Alias
C1orf15; KIAA0479;
Created Date
09-MAY-2003
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
164
Canonical
GESLSRICCVRPPVE
[1][2]
S-Palmitoylation
165
Canonical
ESLSRICCVRPPVER
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Lau C, Dölle C, Gossmann TI, Agledal L, Niere M, Ziegler M. Isoform-specifictargeting and interaction domains in human nicotinamide mononucleotideadenylyltransferases. J Biol Chem. 2010 Jun 11;285(24):18868-76. doi:10.1074/jbc.M110.107631. Epub 2010 Apr 13.[PMID:20388704]
[2] Mayer PR, Huang N, Dewey CM, Dries DR, Zhang H, Yu G. Expression,localization, and biochemical characterization of nicotinamide mononucleotideadenylyltransferase 2. J Biol Chem. 2010 Dec 17;285(51):40387-96. doi:10.1074/jbc.M110.178913. Epub 2010 Oct 13.[PMID:20943658]
Functional Description
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(+).
Sequence Annotation
Nucleotide-binding: 15 24 ATP.
Nucleotide-binding: 269 274 ATP.
Binding site: 16 16 Substrate.
Binding site: 55 55 Substrate.
Binding site: 202 202 Substrate.
Protein Length
307 AA.
Protein Sequence
(Canonical)
MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL  60
VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP  120
SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA  180
NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI  240
MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ  300
LYINASG                                                            307
FASTA
(Canonical)
>LipidDB-9606-01304|Q9BZQ4
MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGL
VSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTP
SMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENA
NLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRI
MNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQ
LYINASG
Gene Ontology
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0000139; C:Golgi membrane; TAS:Reactome
GO:0005770; C:late endosome; IEA:Ensembl
GO:0045202; C:synapse; IEA:Ensembl
GO:0005802; C:trans-Golgi network; IEA:Ensembl
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; TAS:Reactome
GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:UniProtKB
GO:0009435; P:NAD biosynthetic process; IC:UniProtKB
GO:0019674; P:NAD metabolic process; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0006766; P:vitamin metabolic process; TAS:Reactome
GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome
Interpro
InterPro; IPR004821; Cyt_trans-like
InterPro; IPR005248; NAMN_adtrnsfrase
InterPro; IPR014729; Rossmann-like_a/b/a_fold
Pfam
Pfam; PF01467; CTP_transf_2;
SMART
PROSITE
PRINTS