A6IWP7 · A6IWP7_RAT
- ProteinATP-dependent (S)-NAD(P)H-hydrate dehydratase
- GeneNaxd
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids365 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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.
Catalytic activity
- (6S)-NADHX + ATP = ADP + phosphate + NADH + H+
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 171 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 224-230 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NHVEFSR | ||||||
Binding site | 264-268 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KGEQD | ||||||
Binding site | 283-292 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSSRRCGGQG | ||||||
Binding site | 293 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent NAD(P)H-hydrate dehydratase activity | |
Biological Process | nicotinamide nucleotide metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameATP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionA6IWP7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 28-53 | Helical | ||||
Sequence: YGAAAVVMALLSAAIAFHCSPLLAVL |
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 71-362 | YjeF C-terminal | ||||
Sequence: LFQLVRNIVPALTSKKHKGQDGRIGIVGGCQEYTGAPYFAGISALKVGADLTHVFCAREAAPVIKSYSPELIVHPVLDSSDAVEEVEKWLPRLHALVVGPGLGRDDLLLNNVRGILESTKARDIPVVIDADGLWLIAQRPALVHGYQKAVLTPNHVEFSRLWDAVLSSPMDTSNHSGSVLKLSQALGNITIVQKGEQDLISNGQQVLVCNQEGSSRRCGGQGDLLSGSLGVMAHWALRAGPEKTNGSSPLLVAAWGACTLTRECNHLAFQKYGRSTTTTDMIAEVGAAFSKL |
Sequence similarities
Belongs to the NnrD/CARKD family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length365
- Mass (Da)38,731
- Last updated2023-06-28 v1
- Checksum357007FF5852CF82
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH473970 EMBL· GenBank· DDBJ | EDM08823.1 EMBL· GenBank· DDBJ | Genomic DNA |