A0A0R2HMF5 · A0A0R2HMF5_9FIRM
- ProteinBifunctional NAD(P)H-hydrate repair enzyme
- GenennrE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids491 (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.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
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 | 52-56 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 53 | K+ (UniProtKB | ChEBI) | |||
Binding site | 120 | K+ (UniProtKB | ChEBI) | |||
Binding site | 124-130 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 135 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 154 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 157 | K+ (UniProtKB | ChEBI) | |||
Binding site | 254 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 314 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 365 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 399-403 | AMP (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
Names & Taxonomy
Protein names
- Recommended nameBifunctional NAD(P)H-hydrate repair enzyme
- 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
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Erysipelotrichia > Erysipelotrichales > Coprobacillaceae > Kandleria
Accessions
- Primary accessionA0A0R2HMF5
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-211 | YjeF N-terminal | |||
Domain | 219-485 | YjeF C-terminal | |||
Sequence similarities
Belongs to the NnrD/CARKD family.
Belongs to the NnrE/AIBP 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
- Length491
- Mass (Da)53,945
- Last updated2016-01-20 v1
- Checksum6DF665794014E1F4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JQBL01000003 EMBL· GenBank· DDBJ | KRN51031.1 EMBL· GenBank· DDBJ | Genomic DNA |