A0A2D2LU91 · A0A2D2LU91_MOROS
- ProteinADP-dependent (S)-NAD(P)H-hydrate dehydratase
- GenennrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids547 (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.
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 | 295 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 356 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 421 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 458-462 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KGAQT | ||||||
Binding site | 486 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 487 | (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 | metabolite repair | |
Biological Process | nicotinamide nucleotide metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Moraxella
Accessions
- Primary accessionA0A2D2LU91
Proteomes
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-254 | YjeF N-terminal | ||||
Sequence: IYDLEKNWFSKNDSFALMQQAAWQLAHIIKQESSNQKSSYLQKSSHPQKSVLVVAGAGNNGGDAWLVAHYINQLCPHWSVSVVQVAAPSTLASQTAKHLYQSNCANAAKYLTLTAFLQPIHELGLSYHYDVVIDGLLGIGLNRKPTGDYQTIINWINQYRKQVHACQVISIDVPSGLNAATGEVYDDTAVKADKTLCLIGRKVGLHMGGSKDYVGTVIDVPLLPVEPSGM | ||||||
Domain | 254-544 | YjeF C-terminal | ||||
Sequence: MLLHCTLPNLPQRQQVSHKGTYGHVLIIGGNRLQDGHGMAGAAILAASAALSSGAGKVTVACHGDFHAAIVTALPNAMTADLHNVAGIIELINAVDVVAIGMGLGRDKVTLDLFNQYLTAIKQSQKLCVIDADGLYHLADWAGTSDGLTAPIQPRLGQSNQRFYLTPHSAEAGRLLNQPYADIDRDKISAIRALAHQYGGNWLIKGAQTIVLERDSIDICGLGNAGMATAGMGDCLAGLMASLLAQAIAAPMLTAVLIHAKAGDTLAEKMGEYALQANHMASAIGDIIHQI |
Sequence similarities
Belongs to the NnrD/CARKD 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
- Length547
- Mass (Da)58,329
- Last updated2018-01-31 v1
- ChecksumC31EAEE9EF522041