A0A228QIQ5 · A0A228QIQ5_9BURK
- ProteinBifunctional NAD(P)H-hydrate repair enzyme
- GenennrE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids514 (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 | 68-72 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NNGGD | ||||||
Binding site | 69 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 130 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 134-140 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: GIGLGRA | ||||||
Binding site | 166 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 266 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 322 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 378 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 415-419 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KGSGT | ||||||
Binding site | 444 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 445 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
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 | 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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia
Accessions
- Primary accessionA0A228QIQ5
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-225 | YjeF N-terminal | ||||
Sequence: LRVADLRAAEADATAALPPHTLMGRAGAAAARWLSERVAGDDRPVWFAVGPGNNGGDALVAAAQLQQLGVATHAWMPVPVKPDDAQWALGVARTAGVPLSAAPPASLEGYAWVVDGLFGIGLGRALDGTFAEQAARIAAHARDGGRVLALDVPSGLDSDTGRIVGAGVAVAATHTLTFIGAKPGLYTGDGRDLAGEIHVASLDVAPPAAP | ||||||
Domain | 231-505 | YjeF C-terminal | ||||
Sequence: APSLFAAALPARAFASHKGTYGSLAVLGGDTGMCGAPILAARAALFAGAGKVHVGFLGAGAPPYDPPFPELMLHPADTLGLGTMTAIAAGCGLGTREAAATLVRDVLAQDIATLLDADALNLVATHADLAAAVVRRGARGNPCVLTPHPLEAARLLGGDTAAVQRDRVAAAQALAARYAGVVVLKGSGTVIAAPDGRVAINPTGNAALATGGTGDVLGGLIGALLAQRVAPYEAALAGVYLHGLAADTLTANGTGPAGLTAGELAPMVRTLINRL |
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
- Length514
- Mass (Da)51,195
- Last updated2017-10-25 v1
- Checksum9F17BF8E7A8E10C3