A0A2V4UWN7 · A0A2V4UWN7_9GAMM
- ProteinMultifunctional fusion protein
- GenennrD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids599 (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 | 89-93 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NNGGD | ||||||
Binding site | 90 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 184 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 188-194 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: GIGLDRT | ||||||
Binding site | 199 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 221 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 326 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 387 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 450 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 487-491 | AMP (UniProtKB | ChEBI) | ||||
Sequence: KGAGS | ||||||
Binding site | 519 | AMP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 520 | (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 | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameADP-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 lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Psychrobacter
Accessions
- Primary accessionA0A2V4UWN7
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-279 | YjeF N-terminal | ||||
Sequence: LYAMEQAWFSEGHDSFGLMQQAAWQMAKHIEQLYEKKYLNHHSSASVNFSHRHNHQYRVSIWVGKGNNGGDGWLIAYYLKQAGWQVQIVTVGFEDSDFSNSDSDQVNSDKSDTTAISNSKSSITDAQKALQVARSANCKYERFEDSQNDLRSTALQADVYIDALFGIGLDRTPEGIYKQAIRAFNELTEQNNGLAIAVDIPSGVVASTGEVFDRIAIKADATLCLIARKFGLHTKDGVDYSGQVTDIPLIPYQVDNV | ||||||
Region | 120-140 | Disordered | ||||
Sequence: FSNSDSDQVNSDKSDTTAISN | ||||||
Domain | 286-596 | YjeF C-terminal | ||||
Sequence: KLITTGQAFSPRRQNSYKGSYGHVLVIGGNRIDGSQGMGGAAILSASSSMAAGAGKITVACHEAFHGALLTSLPDAMTINLHDAQGVQHLIKAASVVAIGMGLGRDDKAQALFVNYIQAAMTAKKPIVIDADGLYHLASLQLKNDKLISQLREYSTDNEVCLTPHSGEAAKLLNKKIHEIESDRLSAIKLCAQTYGGNWVLKGAGSLVLERGLDQEQVYVCGVGNAGMATAGMGDVLSGVIAGLLAQQDLEPEMRSLHQAVIIHGLAGDILVSQTNQYNSGKSDRGHLLIGQRGLQAQDMPVAIRHVMQLL |
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
- Length599
- Mass (Da)64,777
- Last updated2018-09-12 v1
- Checksum41FDCC0F9D5E0E18