Q6LX63 · NPPNK_METMP
- ProteinBifunctional NADP phosphatase/NAD kinase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids566 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in the regulation of the intracellular balance between NAD(H) and NADP(H), and is a key enzyme in the biosynthesis of NADP. Catalyzes the phosphorylation and dephosphorylation of NAD and NADP, respectively. Although it shows conflicting dual activities and is able to supply NADP, it seems that its physiological role is to prevent excess accumulation of NADP.
Catalytic activity
- ATP + NAD+ = ADP + H+ + NADP+This reaction proceeds in the forward direction.
- H2O + NADP+ = NAD+ + phosphateThis reaction proceeds in the forward direction.
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 66 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 85 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 85 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 87 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 88 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 229 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 355 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 355-356 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DG | ||||||
Binding site | 360 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 430-431 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: NE | ||||||
Binding site | 441 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 458 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 460 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 471-476 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TAYSLS | ||||||
Binding site | 528 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
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 | |
Molecular Function | NADP phosphatase activity | |
Biological Process | lysine metabolic process | |
Biological Process | NAD metabolic process | |
Biological Process | NADP biosynthetic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional NADP phosphatase/NAD kinase
Including 2 domains:
- Recommended nameNAD kinase
- EC number
- Alternative names
- Recommended nameNADP phosphatase
- EC number
- Short namesNADPase ; pNPPase
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Methanomada group > Methanococci > Methanococcales > Methanococcaceae > Methanococcus
Accessions
- Primary accessionQ6LX63
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000229718 | 1-566 | Bifunctional NADP phosphatase/NAD kinase | |||
Sequence: MDMLEMALNIAKDIEKSVKPLIGWEKSNEVVKIGADGTPTKRIDLIAENVAINSIEKVCSAILISEEIGFKRIGKNKPEYVIVLDPVDGTYNSLKDIPFYSAAVAIGRIDKFADNLEELINNLKMKDLEVGVVRNIATGDTYYAEKGKGAHFLRKGEKKSISISNSSNLKDSSIGLFAHDISIDTLKFIKDRRFRRIRLFGSIALEMCYVAKGALDAFINVNETTRLCDIAAGYVIIKEAGGIVTDKNGQEVNLDLDVNSKVSVICSNEMLHKKLVGIFGNRWRIKPTNFGIISRIDNEESIEVADNVIKYLDSKGIKYELDSSTYNALKNRLTKKCDIISNIEEISHMISIGGDGTVLRASKMIEGNEIPMVCINMGTVGFLTEFNKDEIFSAIDSIICGSYKVEKRTKLMGFAKLSDGKQHILNDSLNEVVITTKNPAKMMHFEVYIDGSLVEDVRADGIIVSTPNGSTAYSLSSGGPIIEPTVEGFVIVPICPFKLSSRPLVVNANSEIKIKLLKKSTYVVIDGNTEFEAKKGDEIILRKSESNAYFVKGDNFYNKLKKLSLM |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-283 | NADP phosphatase | ||||
Sequence: MDMLEMALNIAKDIEKSVKPLIGWEKSNEVVKIGADGTPTKRIDLIAENVAINSIEKVCSAILISEEIGFKRIGKNKPEYVIVLDPVDGTYNSLKDIPFYSAAVAIGRIDKFADNLEELINNLKMKDLEVGVVRNIATGDTYYAEKGKGAHFLRKGEKKSISISNSSNLKDSSIGLFAHDISIDTLKFIKDRRFRRIRLFGSIALEMCYVAKGALDAFINVNETTRLCDIAAGYVIIKEAGGIVTDKNGQEVNLDLDVNSKVSVICSNEMLHKKLVGIFGNRW | ||||||
Region | 275-566 | NAD kinase | ||||
Sequence: LVGIFGNRWRIKPTNFGIISRIDNEESIEVADNVIKYLDSKGIKYELDSSTYNALKNRLTKKCDIISNIEEISHMISIGGDGTVLRASKMIEGNEIPMVCINMGTVGFLTEFNKDEIFSAIDSIICGSYKVEKRTKLMGFAKLSDGKQHILNDSLNEVVITTKNPAKMMHFEVYIDGSLVEDVRADGIIVSTPNGSTAYSLSSGGPIIEPTVEGFVIVPICPFKLSSRPLVVNANSEIKIKLLKKSTYVVIDGNTEFEAKKGDEIILRKSESNAYFVKGDNFYNKLKKLSLM |
Sequence similarities
In the N-terminal section; belongs to the inositol monophosphatase superfamily.
In the C-terminal section; belongs to the NAD kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length566
- Mass (Da)62,594
- Last updated2004-07-05 v1
- Checksum1BE5DAC1288E60B0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX950229 EMBL· GenBank· DDBJ | CAF31045.1 EMBL· GenBank· DDBJ | Genomic DNA |