E1JWD4 · E1JWD4_SOLFR
- ProteinBifunctional NAD(P)H-hydrate repair enzyme
- GenennrE
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids513 (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 | 66-70 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NNGGD | ||||||
Binding site | 67 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 133 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 137-143 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: GTGFTGE | ||||||
Binding site | 168 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 171 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 269 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 338 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 388 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 425-429 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KGPAT | ||||||
Binding site | 454 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 455 | (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 | kinase activity | |
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
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Solidesulfovibrio
Accessions
- Primary accessionE1JWD4
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-225 | YjeF N-terminal | ||||
Sequence: IAGWDAASVAECGMSFLALMENASREAMHALVGEVGEVRGKTVLLLAGPGNNGGDAVALARHLDGLGAKVTIALVRPRGRYKGAAGFNARLAARLGLPMIPLAKADLSGANGPDIIVDGLLGTGFTGELRPDLREVVEAVNRLAGQSYIFALDIPSGLSGATGVASPVAVTADATVTFEAAKTGLVAPQAAPYVGRLLVRPIGIPRPVRE | ||||||
Domain | 234-513 | YjeF C-terminal | ||||
Sequence: MTPRLADALPALDPLLHKGSAGRAVVVGGSRGLTGAPLLAGLGALRAGAGLVSVACPGAVEIALKAGHPDVMTLPVGAGDHFGPDDARAVRDFVSTAGAVALGPGLGRHPDTGAFLRALLPLPSRLVLDADGLFFLATDPELKEKIGSEVVITPHPGEAARLLGTDIPAVEADRLESARALAATYGCVAVLKGPATVVAAPDGSAAVSPVVAPNLAVGGSGDVLSGLAAALACSPLSPLLAACIAVYWHGLAGARLAALYPRRGNLASEIADMLPRALTE |
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
- Length513
- Mass (Da)51,912
- Last updated2010-11-30 v1
- Checksum8D8127FEECE578A1