A0A0D7X645 · A0A0D7X645_9BACL
- ProteinBifunctional NAD(P)H-hydrate repair enzyme
- GenennrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids582 (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 | 131-135 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 132 | K+ (UniProtKB | ChEBI) | |||
Binding site | 197 | K+ (UniProtKB | ChEBI) | |||
Binding site | 201-207 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 212 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 230 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 233 | K+ (UniProtKB | ChEBI) | |||
Binding site | 337 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 408 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 462 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 499-503 | AMP (UniProtKB | ChEBI) | |||
Binding site | 528 | AMP (UniProtKB | ChEBI) | |||
Binding site | 529 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ADP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD(P)HX 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 > Bacillati > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus
Accessions
- Primary accessionA0A0D7X645
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-287 | YjeF N-terminal | |||
Domain | 302-582 | 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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length582
- Mass (Da)60,754
- Last updated2015-05-27 v1
- MD5 ChecksumE6D938BDCF7BD35672CEEBC5A3F2670D
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JTHP01000019 EMBL· GenBank· DDBJ | KJD45497.1 EMBL· GenBank· DDBJ | Genomic DNA |