A0A7J6MNA0 · A0A7J6MNA0_PERCH

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
K+ (UniProtKB | Rhea| CHEBI:29103 )

Note: Binds 1 potassium ion per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site99-103(6S)-NADPHX (UniProtKB | ChEBI)
Binding site100K+ (UniProtKB | ChEBI)
Binding site169K+ (UniProtKB | ChEBI)
Binding site173-179(6S)-NADPHX (UniProtKB | ChEBI)
Binding site204(6S)-NADPHX (UniProtKB | ChEBI)
Binding site207K+ (UniProtKB | ChEBI)
Binding site373(6S)-NADPHX (UniProtKB | ChEBI)
Binding site439-445(6S)-NADPHX (UniProtKB | ChEBI)
Binding site479-483ATP (UniProtKB | ChEBI)
Binding site499-508ATP (UniProtKB | ChEBI)
Binding site509(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionADP-dependent NAD(P)H-hydrate dehydratase activity
Molecular FunctionATP binding
Molecular FunctionATP-dependent NAD(P)H-hydrate dehydratase activity
Molecular Functionmetal ion binding
Molecular FunctionNADHX epimerase activity
Molecular FunctionNADPHX epimerase activity
Biological Processnicotinamide nucleotide metabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    ATP-dependent (S)-NAD(P)H-hydrate dehydratase
  • EC number
  • Alternative names
    • ATP-dependent NAD(P)HX dehydratase
  • Recommended name
    NAD(P)H-hydrate epimerase
  • EC number
  • Alternative names
    • NAD(P)HX epimerase

Gene names

    • ORF names
      FOL47_011061

Organism names

Accessions

  • Primary accession
    A0A7J6MNA0

Proteomes

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_502969513818-1543Multifunctional fusion protein

Keywords

Family & Domains

Features

Showing features for domain, region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Domain46-262YjeF N-terminal
Domain266-573YjeF C-terminal
Region593-625Disordered
Region893-947Disordered
Compositional bias907-925Basic residues
Region1003-1025Disordered
Coiled coil1147-1195
Region1213-1320Disordered
Compositional bias1216-1230Polar residues
Compositional bias1248-1265Polar residues
Compositional bias1276-1294Polar residues
Region1351-1379Disordered
Region1408-1439Disordered
Region1475-1503Disordered

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,543
  • Mass (Da)
    165,858
  • Last updated
    2021-04-07 v1
  • Checksum
    0EF3D5D927C9B159
MNRLLAVSSMVSSSISALTTAAVKGGAAMASAAAAPPMKVSTCEQMRRCDKGATDKYSIPSALLMENAGITSYRCLTELLPDHQVTPQTKVLVVCGPGNNGGDGFVVARYVHSNGGQARVILLNGREKYHGDANTNLNIVDCIPGIPVEIATTEEAITAAVDWAEVLVDGIFGTGLGRPVDPSSPFGIAIAAINRARKPVMSLDIPSGINGDSGRIMGPQAVHATSTATFGLVKVGNLVYPGREMCGDLTVTHIGYPPELYADLDTYVNYFPPLPERNPAGHKGSFGKALFLSGAEGYYGAPMLSSNSFLKAGGGYSRLATVKEVIPVIAAEAPSVVFHQLESTDIGSICSGNYNRVFSLAQEMSDMLVLGPGMSTNGDTARLVRQLVLTLDKPLVIDGDGITAISIPPVDSTDIFTSATQLLQERHRKGLPPVVLTPHLAELSRLTGITMKELTDGSHSLLEVGRQLAQDTNSVVVVKVATSMVCEPSGRVRMNLSGNSGMGTAGSGDVLSGIIPAMYSAYGHDVSSLGDAVAAAVFVHGVAGDIAAIRLGGEDGLTAPDIMNAVPEAVSYTRGGEAFKKYAPQLENVRDSVDGMEQPRDQPPPLLALSPAKPSSTEEEEKELPPSLVAVDRRIKEVTEEICRLERERSLGVRLPAEELAMAKVEITKPLPMRSLSEADLVIRRAKKAQPDEKVVAKKALLQRIEQEVGEEINRQRSEELEKGIELRARYTGKSKLWEIAVPRLRDEQWNEPGPIRRQMEEELTVVEFQMFNEGIIESSCQWRTKDEAGQNRNEVHTAILLLMGKPHSNQSYQEVCRHALLGVLSGVISVTTSALPGRDGSSNGGAVYATVITRRALTEGYKKSLVRALAPHGLQALVLSVDCLKNLVLSQGGPMEGERGGGGAVGSKKKKKGKRGKRGKNRKAKPLPYITEAPRAPEGKDGEVEEDCSEENIPALANIEMEPPVDGPIEECPSETALDACPSPPLKEATSSSHCDHFYISTPSDSEATGPGLEAVDDDDDDDEEDELVDAVGTWLGVDSFDGEQHEDGEYLDQHGSPRARNAAAAMTFFNSAATAFGFSRALGLHEKFAGVVDIVDDNARDGGLNTGRLDPRRQKSEDPAMLGGCELTNLRESDKNRVATLVATLAQQKRRADAEEKARAKAESSAEKAIAEAEKAKETLRRSLQLLNKYHQRAKADLAERARLKACVAMGASGNPRGTSQSQLDRIGQQDTEKPEPPIEPAVTSHAPTGDTSPLTRRTSEASAGHQPTRRRFSEIRPPQTLTGNSPGVSSSDDEVLPEEACCSKTPVAGGSKDGPLNKHQRSLLRRYLQISRDSETVAVLRKFVSNSVEERRPKANGPTPPVETNKATRQPGADELENSAVMRSSISITAHKDGKRVFRLRSPPRFERTEGSSPRINLVDAPKSPERYHKPRSPLTTLTMSPEEKLLSPALGRAEKDSLDIFLRLNKSMGDRLPEAPLPRPGSRQSAPVVDKAENTNNDTSVNLAEVDDVLSALSFADSYSSSHPRMPLVSEHLRYRGMV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias907-925Basic residues
Compositional bias1216-1230Polar residues
Compositional bias1248-1265Polar residues
Compositional bias1276-1294Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAPAO010000092
EMBL· GenBank· DDBJ
KAF4673052.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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