Q96T66 · NMNA3_HUMAN
- ProteinNicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- GeneNMNAT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids252 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- ATP + beta-nicotinamide D-ribonucleotide + H+ = diphosphate + NAD+This reaction proceeds in the forward and the backward directions.
Cofactor
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 μM | NMN | |||||
130 μM | NAD+ | |||||
29 μM | ATP | |||||
390 μM | PPi | |||||
276 μM | GTP | |||||
350 μM | ITP | |||||
111 μM | NaMN | |||||
130 μM | NMNH | |||||
2.01 μM | triazofurin monophosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3.6 μmol/min/mg | for NAD synthesis | ||||
12.8 μmol/min/mg | for pyrophosphorolytic NAD+ cleavage | ||||
2.9 μmol/min/mg | for 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 15 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 22 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 56 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: K | ||||||
Binding site | 90 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 93 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 135 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 137 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 140 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: K | ||||||
Binding site | 147 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 148 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 167 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 198 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 203-206 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: TYIR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | neuronal cell body | |
Molecular Function | ATP binding | |
Molecular Function | nicotinamide-nucleotide adenylyltransferase activity | |
Molecular Function | nicotinate-nucleotide adenylyltransferase activity | |
Biological Process | NAD biosynthetic process | |
Biological Process | nucleotide biosynthetic process | |
Biological Process | response to tumor necrosis factor | |
Biological Process | response to wounding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNicotinamide/nicotinic acid mononucleotide adenylyltransferase 3
- Short namesNMN/NaMN adenylyltransferase 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ96T66
- Secondary accessions
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000135016 | 1-252 | Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3 | |||
Sequence: MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS |
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
Structure
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length252
- Mass (Da)28,322
- Last updated2006-10-17 v2
- Checksum6402CFB2FE789CF4
Q96T66-2
- Name2
- Differences from canonical
- 1-37: Missing
Q96T66-3
- Name3
- Differences from canonical
- 37-125: Missing
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y594 | A0A2R8Y594_HUMAN | NMNAT3 | 170 | ||
A0A2R8YGL3 | A0A2R8YGL3_HUMAN | NMNAT3 | 194 | ||
A0A2R8YE08 | A0A2R8YE08_HUMAN | NMNAT3 | 157 | ||
A0A2R8YFG2 | A0A2R8YFG2_HUMAN | NMNAT3 | 346 | ||
A0A2R8YEU0 | A0A2R8YEU0_HUMAN | NMNAT3 | 194 | ||
D6REC8 | D6REC8_HUMAN | NMNAT3 | 63 | ||
D6RHV4 | D6RHV4_HUMAN | NMNAT3 | 113 | ||
D6RGG8 | D6RGG8_HUMAN | NMNAT3 | 98 | ||
D6RGH7 | D6RGH7_HUMAN | NMNAT3 | 100 | ||
D6R975 | D6R975_HUMAN | NMNAT3 | 98 |
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |