A0A6A9UY37 · A0A6A9UY37_9ACTN
- ProteinADP-dependent (S)-NAD(P)H-hydrate dehydratase
- GenennrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids504 (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.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme 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.
Catalytic activity
- (6R)-NADHX = (6S)-NADHX
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 potassium ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 256 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 304 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 360 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 427 | AMP (UniProtKB | ChEBI) | |||
Binding site | 428 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
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
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Auraticoccus
Accessions
- Primary accessionA0A6A9UY37
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 13-216 | YjeF N-terminal | |||
Domain | 221-482 | YjeF C-terminal | |||
Region | 482-504 | Disordered | |||
Sequence similarities
Belongs to the NnrD/CARKD family.
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length504
- Mass (Da)50,830
- Last updated2020-06-17 v1
- Checksum0A099511855094B0
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
WPCU01000006 EMBL· GenBank· DDBJ | MVA76347.1 EMBL· GenBank· DDBJ | Genomic DNA |