A0A7J6MNA0 · A0A7J6MNA0_PERCH
- ProteinMultifunctional fusion protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1543 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 | 99-103 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NNGGD | ||||||
Binding site | 100 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 169 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 173-179 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: GTGLGRP | ||||||
Binding site | 204 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 207 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 373 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 439-445 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: HLAELSR | ||||||
Binding site | 479-483 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KVATS | ||||||
Binding site | 499-508 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NSGMGTAGSG | ||||||
Binding site | 509 | (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 | ATP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NADHX epimerase activity | |
Molecular Function | NADPHX epimerase activity | |
Biological Process | nicotinamide nucleotide metabolic process |
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
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Perkinsozoa > Perkinsea > Perkinsida > Perkinsidae > Perkinsus
Accessions
- Primary accessionA0A7J6MNA0
Proteomes
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MNRLLAVSSMVSSSISA | ||||||
Chain | PRO_5029695138 | 18-1543 | Multifunctional fusion protein | |||
Sequence: LTTAAVKGGAAMASAAAAPPMKVSTCEQMRRCDKGATDKYSIPSALLMENAGITSYRCLTELLPDHQVTPQTKVLVVCGPGNNGGDGFVVARYVHSNGGQARVILLNGREKYHGDANTNLNIVDCIPGIPVEIATTEEAITAAVDWAEVLVDGIFGTGLGRPVDPSSPFGIAIAAINRARKPVMSLDIPSGINGDSGRIMGPQAVHATSTATFGLVKVGNLVYPGREMCGDLTVTHIGYPPELYADLDTYVNYFPPLPERNPAGHKGSFGKALFLSGAEGYYGAPMLSSNSFLKAGGGYSRLATVKEVIPVIAAEAPSVVFHQLESTDIGSICSGNYNRVFSLAQEMSDMLVLGPGMSTNGDTARLVRQLVLTLDKPLVIDGDGITAISIPPVDSTDIFTSATQLLQERHRKGLPPVVLTPHLAELSRLTGITMKELTDGSHSLLEVGRQLAQDTNSVVVVKVATSMVCEPSGRVRMNLSGNSGMGTAGSGDVLSGIIPAMYSAYGHDVSSLGDAVAAAVFVHGVAGDIAAIRLGGEDGLTAPDIMNAVPEAVSYTRGGEAFKKYAPQLENVRDSVDGMEQPRDQPPPLLALSPAKPSSTEEEEKELPPSLVAVDRRIKEVTEEICRLERERSLGVRLPAEELAMAKVEITKPLPMRSLSEADLVIRRAKKAQPDEKVVAKKALLQRIEQEVGEEINRQRSEELEKGIELRARYTGKSKLWEIAVPRLRDEQWNEPGPIRRQMEEELTVVEFQMFNEGIIESSCQWRTKDEAGQNRNEVHTAILLLMGKPHSNQSYQEVCRHALLGVLSGVISVTTSALPGRDGSSNGGAVYATVITRRALTEGYKKSLVRALAPHGLQALVLSVDCLKNLVLSQGGPMEGERGGGGAVGSKKKKKGKRGKRGKNRKAKPLPYITEAPRAPEGKDGEVEEDCSEENIPALANIEMEPPVDGPIEECPSETALDACPSPPLKEATSSSHCDHFYISTPSDSEATGPGLEAVDDDDDDDEEDELVDAVGTWLGVDSFDGEQHEDGEYLDQHGSPRARNAAAAMTFFNSAATAFGFSRALGLHEKFAGVVDIVDDNARDGGLNTGRLDPRRQKSEDPAMLGGCELTNLRESDKNRVATLVATLAQQKRRADAEEKARAKAESSAEKAIAEAEKAKETLRRSLQLLNKYHQRAKADLAERARLKACVAMGASGNPRGTSQSQLDRIGQQDTEKPEPPIEPAVTSHAPTGDTSPLTRRTSEASAGHQPTRRRFSEIRPPQTLTGNSPGVSSSDDEVLPEEACCSKTPVAGGSKDGPLNKHQRSLLRRYLQISRDSETVAVLRKFVSNSVEERRPKANGPTPPVETNKATRQPGADELENSAVMRSSISITAHKDGKRVFRLRSPPRFERTEGSSPRINLVDAPKSPERYHKPRSPLTTLTMSPEEKLLSPALGRAEKDSLDIFLRLNKSMGDRLPEAPLPRPGSRQSAPVVDKAENTNNDTSVNLAEVDDVLSALSFADSYSSSHPRMPLVSEHLRYRGMV |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 46-262 | YjeF N-terminal | ||||
Sequence: MRRCDKGATDKYSIPSALLMENAGITSYRCLTELLPDHQVTPQTKVLVVCGPGNNGGDGFVVARYVHSNGGQARVILLNGREKYHGDANTNLNIVDCIPGIPVEIATTEEAITAAVDWAEVLVDGIFGTGLGRPVDPSSPFGIAIAAINRARKPVMSLDIPSGINGDSGRIMGPQAVHATSTATFGLVKVGNLVYPGREMCGDLTVTHIGYPPELYA | ||||||
Domain | 266-573 | YjeF C-terminal | ||||
Sequence: TYVNYFPPLPERNPAGHKGSFGKALFLSGAEGYYGAPMLSSNSFLKAGGGYSRLATVKEVIPVIAAEAPSVVFHQLESTDIGSICSGNYNRVFSLAQEMSDMLVLGPGMSTNGDTARLVRQLVLTLDKPLVIDGDGITAISIPPVDSTDIFTSATQLLQERHRKGLPPVVLTPHLAELSRLTGITMKELTDGSHSLLEVGRQLAQDTNSVVVVKVATSMVCEPSGRVRMNLSGNSGMGTAGSGDVLSGIIPAMYSAYGHDVSSLGDAVAAAVFVHGVAGDIAAIRLGGEDGLTAPDIMNAVPEAVSYT | ||||||
Region | 593-625 | Disordered | ||||
Sequence: VDGMEQPRDQPPPLLALSPAKPSSTEEEEKELP | ||||||
Region | 893-947 | Disordered | ||||
Sequence: GGPMEGERGGGGAVGSKKKKKGKRGKRGKNRKAKPLPYITEAPRAPEGKDGEVEE | ||||||
Compositional bias | 907-925 | Basic residues | ||||
Sequence: GSKKKKKGKRGKRGKNRKA | ||||||
Region | 1003-1025 | Disordered | ||||
Sequence: TPSDSEATGPGLEAVDDDDDDDE | ||||||
Coiled coil | 1147-1195 | |||||
Sequence: LAQQKRRADAEEKARAKAESSAEKAIAEAEKAKETLRRSLQLLNKYHQR | ||||||
Region | 1213-1320 | Disordered | ||||
Sequence: GASGNPRGTSQSQLDRIGQQDTEKPEPPIEPAVTSHAPTGDTSPLTRRTSEASAGHQPTRRRFSEIRPPQTLTGNSPGVSSSDDEVLPEEACCSKTPVAGGSKDGPLN | ||||||
Compositional bias | 1216-1230 | Polar residues | ||||
Sequence: GNPRGTSQSQLDRIG | ||||||
Compositional bias | 1248-1265 | Polar residues | ||||
Sequence: HAPTGDTSPLTRRTSEAS | ||||||
Compositional bias | 1276-1294 | Polar residues | ||||
Sequence: SEIRPPQTLTGNSPGVSSS | ||||||
Region | 1351-1379 | Disordered | ||||
Sequence: VEERRPKANGPTPPVETNKATRQPGADEL | ||||||
Region | 1408-1439 | Disordered | ||||
Sequence: RFERTEGSSPRINLVDAPKSPERYHKPRSPLT | ||||||
Region | 1475-1503 | Disordered | ||||
Sequence: RLPEAPLPRPGSRQSAPVVDKAENTNNDT |
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.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,543
- Mass (Da)165,858
- Last updated2021-04-07 v1
- Checksum0EF3D5D927C9B159
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 907-925 | Basic residues | ||||
Sequence: GSKKKKKGKRGKRGKNRKA | ||||||
Compositional bias | 1216-1230 | Polar residues | ||||
Sequence: GNPRGTSQSQLDRIG | ||||||
Compositional bias | 1248-1265 | Polar residues | ||||
Sequence: HAPTGDTSPLTRRTSEAS | ||||||
Compositional bias | 1276-1294 | Polar residues | ||||
Sequence: SEIRPPQTLTGNSPGVSSS |
Keywords
- Technical term