A0AA38XX18 · A0AA38XX18_9EURO
- ProteinMultifunctional fusion protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids631 (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 ATP, which is converted to ADP. 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 | 61-65 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 62 | K+ (UniProtKB | ChEBI) | |||
Binding site | 124 | K+ (UniProtKB | ChEBI) | |||
Binding site | 128-134 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 157 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 160 | K+ (UniProtKB | ChEBI) | |||
Binding site | 320 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 366-372 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
Binding site | 403-407 | ATP (UniProtKB | ChEBI) | |||
Binding site | 423-432 | ATP (UniProtKB | ChEBI) | |||
Binding site | 433 | (6S)-NADPHX (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | ADP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD(P)HX epimerase activity | |
Biological Process | metabolite repair | |
Biological Process | nicotinamide nucleotide metabolic process | |
Biological Process | tRNA threonylcarbamoyladenosine modification |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameATP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
- Recommended nameNAD(P)H-hydrate epimerase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Trichomeriaceae > Knufia
Accessions
- Primary accessionA0AA38XX18
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 13-214 | YjeF N-terminal | |||
Domain | 224-491 | 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
- Length631
- Mass (Da)64,737
- Last updated2024-01-24 v1
- MD5 Checksum24A3656117FA8ABCD76E546E46338A27
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAPDRN010000089 EMBL· GenBank· DDBJ | KAJ9625316.1 EMBL· GenBank· DDBJ | Genomic DNA |