Q8DGC3 · NNR_THEVB
- ProteinBifunctional NAD(P)H-hydrate repair enzyme Nnr
- Genennr
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids505 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity).
Catalytic activity
- (6S)-NADHX + ADP = AMP + H+ + NADH + phosphate
Cofactor
Note: Binds 1 potassium ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 124 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 157 | (6S)-NADPHX 1 (UniProtKB | ChEBI); for epimerase activity | ||||
Sequence: D | ||||||
Binding site | 160 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 330 | (6S)-NADPHX 2 (UniProtKB | ChEBI); for dehydratase activity | ||||
Sequence: G | ||||||
Binding site | 412-416 | ADP (UniProtKB | ChEBI) | ||||
Sequence: KGART | ||||||
Binding site | 432-441 | ADP (UniProtKB | ChEBI) | ||||
Sequence: TPALARGGSG | ||||||
Binding site | 442 | (6S)-NADPHX 2 (UniProtKB | ChEBI); for dehydratase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ADP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | NADHX epimerase activity | |
Molecular Function | NADPHX epimerase activity | |
Biological Process | metabolite repair | |
Biological Process | nicotinamide nucleotide metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional NAD(P)H-hydrate repair enzyme Nnr
- Alternative names
Including 2 domains:
- Recommended nameADP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
- Recommended nameNAD(P)H-hydrate epimerase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Acaryochloridales > Thermosynechococcaceae > Thermosynechococcus
Accessions
- Primary accessionQ8DGC3
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000416423 | 1-505 | Bifunctional NAD(P)H-hydrate repair enzyme Nnr | |||
Sequence: MKPTFPAIVTTAEMQAIEGAMFNGGLPIPALMEKVGQRLSHYLQAHFPTSQYPRVAVLAGPGHNGGDALVVARELWHRGYQVKLWQPFERLKPLTADHARYARFLGLPFVERVEALQEVDVIVDGLFGFGLERELTGELAHAIDEINTWPQPRVSIDVPSGLHSDTGAVLGTAIRADRTLCLGLWKRGLLVEEAQPWVGQGVLIPFDIPSVVIETALASAPRRYCLDDSCWQALPLSRSPITHKYQQGQLLLIGGSGQFGGSILLSALAARCTGVGMLVVAVPQSLKSLVLSRVPDAIVVGCPETPRGAIARLPEGLELGKFSAIACGPGLTPEAVSVVATVLRAETSLVLDADALNILATLSPWPLPSGTILTPHYGEFRRLFPDLVGTAGDRLDQVIAAARWSNAIVLLKGARTAIASARGDLWINPHSTPALARGGSGDVLTGLIGGLLAQQEALRATYGGVWWHAQAALEAEQQATSLGVYPEQLIAHLLPTLRRALAARV |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-219 | NAD(P)H-hydrate epimerase | ||||
Sequence: MKPTFPAIVTTAEMQAIEGAMFNGGLPIPALMEKVGQRLSHYLQAHFPTSQYPRVAVLAGPGHNGGDALVVARELWHRGYQVKLWQPFERLKPLTADHARYARFLGLPFVERVEALQEVDVIVDGLFGFGLERELTGELAHAIDEINTWPQPRVSIDVPSGLHSDTGAVLGTAIRADRTLCLGLWKRGLLVEEAQPWVGQGVLIPFDIPSVVIETALAS | ||||||
Domain | 14-214 | YjeF N-terminal | ||||
Sequence: MQAIEGAMFNGGLPIPALMEKVGQRLSHYLQAHFPTSQYPRVAVLAGPGHNGGDALVVARELWHRGYQVKLWQPFERLKPLTADHARYARFLGLPFVERVEALQEVDVIVDGLFGFGLERELTGELAHAIDEINTWPQPRVSIDVPSGLHSDTGAVLGTAIRADRTLCLGLWKRGLLVEEAQPWVGQGVLIPFDIPSVVIE | ||||||
Region | 63-67 | NADPHX 1; for epimerase activity | ||||
Sequence: HNGGD | ||||||
Region | 128-134 | NADPHX 1; for epimerase activity | ||||
Sequence: GFGLERE | ||||||
Domain | 226-500 | YjeF C-terminal | ||||
Sequence: LDDSCWQALPLSRSPITHKYQQGQLLLIGGSGQFGGSILLSALAARCTGVGMLVVAVPQSLKSLVLSRVPDAIVVGCPETPRGAIARLPEGLELGKFSAIACGPGLTPEAVSVVATVLRAETSLVLDADALNILATLSPWPLPSGTILTPHYGEFRRLFPDLVGTAGDRLDQVIAAARWSNAIVLLKGARTAIASARGDLWINPHSTPALARGGSGDVLTGLIGGLLAQQEALRATYGGVWWHAQAALEAEQQATSLGVYPEQLIAHLLPTLRRA | ||||||
Region | 227-505 | ADP-dependent (S)-NAD(P)H-hydrate dehydratase | ||||
Sequence: DDSCWQALPLSRSPITHKYQQGQLLLIGGSGQFGGSILLSALAARCTGVGMLVVAVPQSLKSLVLSRVPDAIVVGCPETPRGAIARLPEGLELGKFSAIACGPGLTPEAVSVVATVLRAETSLVLDADALNILATLSPWPLPSGTILTPHYGEFRRLFPDLVGTAGDRLDQVIAAARWSNAIVLLKGARTAIASARGDLWINPHSTPALARGGSGDVLTGLIGGLLAQQEALRATYGGVWWHAQAALEAEQQATSLGVYPEQLIAHLLPTLRRALAARV | ||||||
Region | 376-382 | NADPHX 2; for dehydratase activity | ||||
Sequence: HYGEFRR |
Sequence similarities
In the N-terminal section; belongs to the NnrE/AIBP family.
In the C-terminal section; belongs to the NnrD/CARKD family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length505
- Mass (Da)53,934
- Last updated2003-03-01 v1
- Checksum503588EDBFF6BCF0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000039 EMBL· GenBank· DDBJ | BAC09947.1 EMBL· GenBank· DDBJ | Genomic DNA |