P22253 · PNCB_SALTY
- ProteinNicotinate phosphoribosyltransferase
- GenepncB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids400 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.
Catalytic activity
- nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = nicotinate beta-D-ribonucleotide + ADP + phosphate + diphosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.5 μM | nicotinate in the presence of ATP | |||||
0.3 mM | nicotinate in the absence of ATP | |||||
22 μM | 5-phospho-alpha-D-ribose 1-diphosphate in the presence of ATP | |||||
4.5 mM | 5-phospho-alpha-D-ribose 1-diphosphate in the absence of ATP |
Pathway
Cofactor biosynthesis; NAD+ biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | nicotinate phosphoribosyltransferase activity | |
Biological Process | bioluminescence | |
Biological Process | NAD salvage |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNicotinate phosphoribosyltransferase
- EC number
- Short namesNAPRTase
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP22253
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 220 | Loss of ATP hydrolysis and autophosphorylation. | |||
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Initiator methionine | 1 | Removed | |||
Chain | PRO_0000205846 | 2-400 | Nicotinate phosphoribosyltransferase | ||
Modified residue | 220 | Phosphohistidine; by autocatalysis | |||
Post-translational modification
Transiently phosphorylated on a His residue during the reaction cycle (PubMed:9521740).
Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release (PubMed:7503993, PubMed:9521740, PubMed:9521741).
Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release (PubMed:7503993, PubMed:9521740, PubMed:9521741).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length400
- Mass (Da)45,661
- Last updated2007-01-23 v2
- ChecksumBA76FF5EF0D02F3A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55986 EMBL· GenBank· DDBJ | AAA27190.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL19938.1 EMBL· GenBank· DDBJ | Genomic DNA |