Q96T66 · NMNA3_HUMAN

  • Protein
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
  • Gene
    NMNAT3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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. 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.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Divalent metal cations. Mg2+ confers the highest activity.

Activity regulation

Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
209 μMNMN
130 μMNAD+
29 μMATP
390 μMPPi
276 μMGTP
350 μMITP
111 μMNaMN
130 μMNMNH
2.01 μMtriazofurin monophosphate
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
3.6 μmol/min/mgfor NAD synthesis
12.8 μmol/min/mgfor pyrophosphorolytic NAD+ cleavage
2.9 μmol/min/mgfor pyrophosphorolytic NADH cleavage

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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site14NAD+ (UniProtKB | ChEBI)
Binding site15NAD+ (UniProtKB | ChEBI)
Binding site22ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site56ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain
Binding site90NAD+ (UniProtKB | ChEBI)
Binding site93NAD+ (UniProtKB | ChEBI)
Binding site135NAD+ (UniProtKB | ChEBI)
Binding site137NAD+ (UniProtKB | ChEBI)
Binding site140ATP (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site147NAD+ (UniProtKB | ChEBI)
Binding site148NAD+ (UniProtKB | ChEBI)
Binding site167NAD+ (UniProtKB | ChEBI)
Binding site198NAD+ (UniProtKB | ChEBI)
Binding site203-206ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Cellular Componentneuronal cell body
Molecular FunctionATP binding
Molecular Functionnicotinamide-nucleotide adenylyltransferase activity
Molecular Functionnicotinate-nucleotide adenylyltransferase activity
Biological ProcessNAD biosynthetic process
Biological Processnucleotide biosynthetic process
Biological Processresponse to tumor necrosis factor
Biological Processresponse to wounding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
  • Short names
    NMN/NaMN adenylyltransferase 3
  • Alternative names
    • Nicotinamide-nucleotide adenylyltransferase 3 (NMN adenylyltransferase 3)
    • Nicotinate-nucleotide adenylyltransferase 3 (NaMN adenylyltransferase 3) (EC:2.7.7.18
      ) . EC:2.7.7.18 (UniProtKB | ENZYME | Rhea)
    • Pyridine nucleotide adenylyltransferase 3 (PNAT-3) (EC:2.7.7.1
      ) . EC:2.7.7.1 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      NMNAT3
    • ORF names
      FKSG76

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q96T66
  • Secondary accessions
    • B3KVR6
    • D3DNF2
    • D3DNF3
    • Q8N4G1

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 306 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001350161-252Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in lung and spleen with lower levels in placenta and kidney.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q96T66-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    252
  • Mass (Da)
    28,322
  • Last updated
    2006-10-17 v2
  • Checksum
    6402CFB2FE789CF4
MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS

Q96T66-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q96T66-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 10 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R8Y594A0A2R8Y594_HUMANNMNAT3170
A0A2R8YGL3A0A2R8YGL3_HUMANNMNAT3194
A0A2R8YE08A0A2R8YE08_HUMANNMNAT3157
A0A2R8YFG2A0A2R8YFG2_HUMANNMNAT3346
A0A2R8YEU0A0A2R8YEU0_HUMANNMNAT3194
D6REC8D6REC8_HUMANNMNAT363
D6RHV4D6RHV4_HUMANNMNAT3113
D6RGG8D6RGG8_HUMANNMNAT398
D6RGH7D6RGH7_HUMANNMNAT3100
D6R975D6R975_HUMANNMNAT398

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0102671-37in isoform 2
Alternative sequenceVSP_04320337-125in isoform 3
Sequence conflict169in Ref. 1; AAK52726

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF345564
EMBL· GenBank· DDBJ
AAK52726.1
EMBL· GenBank· DDBJ
mRNA
AK123208
EMBL· GenBank· DDBJ
BAG53878.1
EMBL· GenBank· DDBJ
mRNA
AC046134
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC110716
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471052
EMBL· GenBank· DDBJ
EAW79023.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW79024.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW79025.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW79030.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471052
EMBL· GenBank· DDBJ
EAW79031.1
EMBL· GenBank· DDBJ
Genomic DNA
BC034374
EMBL· GenBank· DDBJ
AAH34374.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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