A0A087AFR4 · A0A087AFR4_9BIFI

  • Protein
    ADP-dependent (S)-NAD(P)H-hydrate dehydratase
  • Gene
    nnrD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

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 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site320(6S)-NADPHX (UniProtKB | ChEBI)
Binding site370(6S)-NADPHX (UniProtKB | ChEBI)
Binding site435(6S)-NADPHX (UniProtKB | ChEBI)
Binding site477-481AMP (UniProtKB | ChEBI)
Binding site510AMP (UniProtKB | ChEBI)
Binding site511(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 Processmetabolite repair
Biological Processnicotinamide nucleotide metabolic process
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      nnrD
    • ORF names
      BCHO_1100

Organism names

  • Taxonomic identifier
  • Strain
    • LMG 10510
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A087AFR4

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-16Polar residues
Region1-25Disordered
Domain39-278YjeF N-terminal
Domain285-601YjeF C-terminal

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    608
  • Mass (Da)
    62,762
  • Last updated
    2014-10-29 v1
  • Checksum
    6C45BE1125FA89F1
MNDQRMNGSGAARTQTMEENEEGARTDMLCSSAYDVATVRALERPLLDDGAPLMRMAAAAAARHILDVVDEQDWDAESLRVCVLAGAGDNGGDGLYCGAMLAGEGLNVTAIAVGRSLHDEAYAAFRKAGGHVFTLDPNAHIPGASVGFSSGEAGARLEQAVRFVSRAHIIVDAMTGIGVNGALHGIPAAIAEAVGTHGVPERVALPDDELDIEFPFVLAIDTPSGIGVDDGTLPGAYIPADATMMFGALKPCAMLPPACYVCGRITLVDFGFDVDDVDPDVEIVDRAFAQSAIRIPRLEDAKYGRGVTGLITGSDAYPGAAVMSTCAAARSNIGMVRYLGPERAQDLVLRALPEAVVGKGHVHSWVVGCGIPDGEHDDGRDLQRTRAKALLAHYSLDGDEEARRAALAMPPVVVDAGALDLLPAHVPAHVVVTPHAGEMASLLTRLGEPTDAADVAARPLTAARRACELTGATVLLKGAMTVIVGADDAGSTRTLVCGRAPAFLATAGAGDVLAGIVGAMLAQQADEVVADPSLAAEVVAGAAYVHGLAAALASHSDQHAWNEPALFTDGDEDTHEAAEAVGHPIVAMDVVDALPDAFDMLNATAHYE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-16Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JGYU01000004
EMBL· GenBank· DDBJ
KFI57614.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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