A0A1C5KGV1 · A0A1C5KGV1_9CLOT

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnr
  • 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.
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 site58-62(6S)-NADPHX (UniProtKB | ChEBI)
Binding site59K+ (UniProtKB | ChEBI)
Binding site120K+ (UniProtKB | ChEBI)
Binding site124-130(6S)-NADPHX (UniProtKB | ChEBI)
Binding site135(6S)-NADPHX (UniProtKB | ChEBI)
Binding site153(6S)-NADPHX (UniProtKB | ChEBI)
Binding site156K+ (UniProtKB | ChEBI)
Binding site254(6S)-NADPHX (UniProtKB | ChEBI)
Binding site317(6S)-NADPHX (UniProtKB | ChEBI)
Binding site368(6S)-NADPHX (UniProtKB | ChEBI)
Binding site405-409AMP (UniProtKB | ChEBI)
Binding site433AMP (UniProtKB | ChEBI)
Binding site434(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
      nnr
    • Synonyms
      nnrD
      , nnrE
    • ORF names
      SAMEA3545239_00024

Organism names

  • Taxonomic identifier
  • Strain
    • 2789STDY5608831
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium > environmental samples

Accessions

  • Primary accession
    A0A1C5KGV1

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-210YjeF N-terminal
Domain219-493YjeF 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    493
  • Mass (Da)
    52,924
  • Last updated
    2016-11-02 v1
  • Checksum
    858BD04329015AAA
MEYLVSAEEMRRADRSVIQDYGVPSLVLMERAALSCVELMKKESFDLSRILVAAGSGNNGGDGFAMARILKLQGFSADIWFVGNPEHLSKEAALQKKICENYGMKFVRNLPDGEYTTIVDAIFGSGISREIRGNYREVIEDINRHPAKIFAVDIPSGISSDDGRIQGTAVRADVTGALAFRKLGHVLYPGTEYAGKTVLLDIGITKEGFHQQLPRVQAAGRELLSLLPPREAAGNKGSFGKACLMAGSRNMAGAAYLSGRAAALMGTGLVRVVSEACNREILQTLLPEAVLTTEELFSEKILAESLAWADAIGIGPGLSTGTEAERELFFVLEKNNLPMVLDADALNILAKHPDWLKKSRAPKILTPHMGEMVRLSGFSMEELKKRPLELAAAYAKEQQVILVLKDARTVITDGERLVLNTSGNNGMATGGSGDVLTGIITGLLAQGTAPFDAAVLGVYLHGLAGDRAAENTGVRGMLSTDILKELPQILKEG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FMDP01000001
EMBL· GenBank· DDBJ
SCG86958.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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