Q9UT53 · NMAH_SCHPO
- ProteinNicotinamide/nicotinic acid mononucleotide adenylyltransferase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids368 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 to form deamido-NAD+ (NaAD). Key enzyme in both de novo and salvage pathways for NAD+ biosynthesis.
Catalytic activity
- ATP + beta-nicotinamide D-ribonucleotide + H+ = diphosphate + NAD+
Cofactor
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; deamido-NAD+ from nicotinate D-ribonucleotide: step 1/1.
Cofactor biosynthesis; NAD+ biosynthesis; NAD+ from nicotinamide D-ribonucleotide: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 135 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 136 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 143 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: H | ||||||
Binding site | 215 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 250 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 252 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 263 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 282 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 313 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 318-321 | ATP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: TKVR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | nicotinamide-nucleotide adenylyltransferase activity | |
Molecular Function | nicotinate-nucleotide adenylyltransferase activity | |
Biological Process | NAD biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNicotinamide/nicotinic acid mononucleotide adenylyltransferase
- EC number
- Short namesNMN/NaMN adenylyltransferase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionQ9UT53
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000316624 | 1-368 | Nicotinamide/nicotinic acid mononucleotide adenylyltransferase | |||
Sequence: MHTMNGDNFANSFPKNPLLSRNSSSSNVIQYSDEFSPDEDWLNEHAAKEHEERIRRPSVNRAWQKNSTSGGPSVSLEKREADVASLGEVMDLEEVPRGITRQARQLNEYIFPKHRFRNHLVDEGKIPLVLVACGSFSPITYLHLRMFEMATDTIQEQTNMELVAGYFSPVNDHYKKEGLAPAYHRVRMCELACERTSSWLMVDAWESLQPSYTCTARVLDHFDEEINQKRGGITLSDGTKRPCKIMLLAGGDLIASMGEPGVWSDKDLHHILGKFGCCIVERTGSDVWAFLLAHDIMFAYRGNILVIKQLIYNDISSTKVRLFIRRGMSIRYLLPNSVIQYIERYALYRDAEPVKTIFYQSPFVRMEP | ||||||
Modified residue | 36 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 75 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 85 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MHTMNGDNFANSFPKNPLLSRNSSS | ||||||
Region | 47-78 | Disordered | ||||
Sequence: AKEHEERIRRPSVNRAWQKNSTSGGPSVSLEK | ||||||
Compositional bias | 60-74 | Polar residues | ||||
Sequence: NRAWQKNSTSGGPSV |
Sequence similarities
Belongs to the eukaryotic NMN adenylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length368
- Mass (Da)42,149
- Last updated2012-04-18 v2
- Checksum4EE320D84D917DAE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 60-74 | Polar residues | ||||
Sequence: NRAWQKNSTSGGPSV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAB55285.2 EMBL· GenBank· DDBJ | Genomic DNA |