M0M2I0 · M0M2I0_9EURY

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.

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 site54-58(6S)-NADPHX (UniProtKB | ChEBI)
Binding site55K+ (UniProtKB | ChEBI)
Binding site120K+ (UniProtKB | ChEBI)
Binding site124-130(6S)-NADPHX (UniProtKB | ChEBI)
Binding site153(6S)-NADPHX (UniProtKB | ChEBI)
Binding site156K+ (UniProtKB | ChEBI)
Binding site239(6S)-NADPHX (UniProtKB | ChEBI)
Binding site308(6S)-NADPHX (UniProtKB | ChEBI)
Binding site418AMP (UniProtKB | ChEBI)
Binding site419(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionADP-dependent NAD(P)H-hydrate dehydratase activity
Molecular FunctionATP binding
Molecular Functionkinase 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
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Alternative names
    • Nicotinamide nucleotide repair protein

Including 2 domains:

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

Gene names

    • Name
      nnrE
    • Synonyms
      nnrD
    • ORF names
      C447_06436

Organism names

  • Taxonomic identifier
  • Strain
    • 100A6
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Halococcaceae > Halococcus

Accessions

  • Primary accession
    M0M2I0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-205YjeF N-terminal
Domain205-474YjeF C-terminal

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 status
    Complete
  • Length
    475
  • Mass (Da)
    49,049
  • Last updated
    2013-04-03 v1
  • Checksum
    D511730969B1E5BD
MITTDRMAAVDANAAALGVPQKQLMESSGNAVARAVRDLVDPGSRIAIVAGRGNNGGDALVAARFLDEFDTHTLLLGRAETISTDIARENWDALDEAKYDVEEVQDSRAIGLGDPDLVVDAMLGTGISGDLREPEATAAREMNESDATVLSVDVPSGVDADTGEGGAGAVEADHVVTFHDSKPGLDSLDADVRVEDIGIPAAAERFVGPGDLAVETDPRARKGDSGRVMVIGGGPYTGAPALAAQSSLRAGADLAFVSIPERVFDPIAGYAEDLIVQPYDAPRLGPDQVDDLLDTATRHDDIVVLGPGLGTADETLDAVAEFLSGFDGRAVVDADALSVVPEVDTDATLVCTPNRHELAEMGGPDVDDLAAHADEIEAFAADLGHIVLAKAKDDVISNGKRTRISRVGTPGMTVGGTGDLLAGITAAQLGTREAFDAACVAPYVNGRAAEALDRGSGLMASDLLDAIPEAMRVDR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOMB01000017
EMBL· GenBank· DDBJ
EMA39593.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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