D3SXU2 · D3SXU2_NATMM
- ProteinNAD kinase
- GenenadK
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids607 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- ATP + NAD+ = ADP + H+ + NADP+
Cofactor
Protein has several cofactor binding sites:
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 65 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 65-66 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DG | ||||||
Binding site | 134-135 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ND | ||||||
Binding site | 150 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 410 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 426 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 428 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: L | ||||||
Binding site | 429 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 546 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | inositol monophosphate 1-phosphatase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD+ kinase activity | |
Biological Process | inositol metabolic process | |
Biological Process | NAD metabolic process | |
Biological Process | NADP biosynthetic process | |
Biological Process | phosphatidylinositol phosphate biosynthetic process | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNAD kinase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natrialba
Accessions
- Primary accessionD3SXU2
Proteomes
Subcellular Location
PTM/Processing
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 305-340 | Disordered | ||||
Sequence: ESVGDDHGLPPGPAPTPSPSRAPGSDSTTPALTDGD | ||||||
Compositional bias | 325-340 | Polar residues | ||||
Sequence: RAPGSDSTTPALTDGD |
Sequence similarities
Belongs to the NAD kinase family.
Belongs to the inositol monophosphatase superfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length607
- Mass (Da)64,875
- Last updated2010-04-20 v1
- ChecksumC3D8137CC0499808
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 325-340 | Polar residues | ||||
Sequence: RAPGSDSTTPALTDGD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001932 EMBL· GenBank· DDBJ | ADD03982.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AOHS01000009 EMBL· GenBank· DDBJ | ELY33641.1 EMBL· GenBank· DDBJ | Genomic DNA |