P65774 · NADK_SALTY
- ProteinNAD kinase
- GenenadK
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids292 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates as a source of phosphorus. NADH cannot replace NAD as a substrate.
Catalytic activity
- ATP + NAD+ = ADP + H+ + NADP+
Cofactor
Activity regulation
Allosterically inhibited by NADPH and NADH. NADPH is the primary inhibitor during aerobic growth and NADH during anaerobic growth.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
2.1 mM | NAD | |||||
2.7 mM | ATP |
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 73 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 73-74 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DG | ||||||
Binding site | 147-148 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NE | ||||||
Binding site | 158 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 175 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Site | 175 | Responsible for conferring strict specificity to NAD | ||||
Sequence: R | ||||||
Binding site | 177 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 185 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 188-193 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TAYSLS | ||||||
Binding site | 247 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | NAD binding | |
Molecular Function | NAD+ kinase activity | |
Biological Process | NAD metabolic process | |
Biological Process | NADP biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD kinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP65774
- Secondary accessions
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120655 | 1-292 | NAD kinase | |||
Sequence: MNNHFKCIGIVGHPRHPTALTTHEMLYRWLCDQGYEVIVEQQIAHELQLKNVPTGTLAEIGQQADLAVVVGGDGNMLGAARTLARYDINVIGINRGNLGFLTDLDPDNALQQLSDVLEGRYISEKRFLLEAQVCQQDRQKRISTAINEVVLHPGKVAHMIEFEVYIDETFAFSQRSDGLIISTPTGSTAYSLSAGGPILTPSLDAITLVPMFPHTLSARPLVINSSSTIRLRFSHRRSDLEISCDSQIALPIQEGEDVLIRRCDYHLNLIHPKDYSYFNTLSTKLGWSKKLF |
Proteomic databases
Interaction
Subunit
Equilibrium mixture of dimer and tetramer. It is converted entirely to tetramer in the presence of the inhibitor NADPH.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length292
- Mass (Da)32,584
- Last updated2004-10-11 v1
- Checksum93585C83A2EEF41C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE006468 EMBL· GenBank· DDBJ | AAL21572.1 EMBL· GenBank· DDBJ | Genomic DNA |