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A0A1Y0LB73 · A0A1Y0LB73_TATCI

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

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 site69-73(6S)-NADPHX (UniProtKB | ChEBI)
Binding site70K+ (UniProtKB | ChEBI)
Binding site132K+ (UniProtKB | ChEBI)
Binding site136-142(6S)-NADPHX (UniProtKB | ChEBI)
Binding site147(6S)-NADPHX (UniProtKB | ChEBI)
Binding site165(6S)-NADPHX (UniProtKB | ChEBI)
Binding site168K+ (UniProtKB | ChEBI)
Binding site266(6S)-NADPHX (UniProtKB | ChEBI)
Binding site326(6S)-NADPHX (UniProtKB | ChEBI)
Binding site372(6S)-NADPHX (UniProtKB | ChEBI)
Binding site409-413AMP (UniProtKB | ChEBI)
Binding site438AMP (UniProtKB | ChEBI)
Binding site439(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionADP-dependent NAD(P)H-hydrate dehydratase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular FunctionNADHX epimerase activity
Molecular FunctionNADPHX epimerase activity
Biological Processmetabolite repair
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
      nnrD
    • Synonyms
      nnrE
    • ORF names
      A7K98_17185

Organism names

Accessions

  • Primary accession
    A0A1Y0LB73

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-222YjeF N-terminal
Domain231-498YjeF 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
    498
  • Mass (Da)
    52,644
  • Last updated
    2017-08-30 v1
  • MD5 Checksum
    2B219A9B0678264F365CDA440D17F012
MSANNFSLSSLSGAVWPASQFPSLEQQLCSICGISTRTLMERAGHAAFQHICRLWPQAEHWRILCGSGNNGGDGYVVARLAKEAGFRVTVIACDAARLPAEALQAREQWLACGGECLPADSDWIGEEHLIVDALLGIGLNRAPEDPYRQLIEKAEERSVPIIALDIPSGVMADSGTVPGVAIKADVTLTFIALKAGLLTGKARDYCGTILLDPLGPELAGNYADPPVWRKDVSHLAGWLPARKATAHKGDHGKLVLIGGDDGTGGAIRLAGEAALRSGAGLVRVLTHPDNVNALVTARPELMAAAMSEQWLEESLEWADTVMIGPGLGQQAWGKWVFNQVKKSKKQTLWDADALNLLAISPDTRQNRILTPHPGEAARLLGTSVQKVENDRLLAARQLVQRYGGVVVLKGAGTVISSSTGETVIADVGNPGMATGGMGDVLSGVITALAGQKLSLYDAACAGVVAHGGAADWVAREHGMRGMLASDLFEPLRRLVNPE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP015579
EMBL· GenBank· DDBJ
ARU95321.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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