A0A8B6LIY2 · A0A8B6LIY2_9BURK

  • 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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 site64-68(6S)-NADPHX (UniProtKB | ChEBI)
Binding site65K+ (UniProtKB | ChEBI)
Binding site125K+ (UniProtKB | ChEBI)
Binding site129-135(6S)-NADPHX (UniProtKB | ChEBI)
Binding site158(6S)-NADPHX (UniProtKB | ChEBI)
Binding site161K+ (UniProtKB | ChEBI)
Binding site256(6S)-NADPHX (UniProtKB | ChEBI)
Binding site309(6S)-NADPHX (UniProtKB | ChEBI)
Binding site365(6S)-NADPHX (UniProtKB | ChEBI)
Binding site402-406AMP (UniProtKB | ChEBI)
Binding site431AMP (UniProtKB | ChEBI)
Binding site432(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
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
      SRS16CHR_02452

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SRS16
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Variovorax

Accessions

  • Primary accession
    A0A8B6LIY2

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain18-218YjeF N-terminal
Region217-238Disordered
Domain221-486YjeF 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
    486
  • Mass (Da)
    49,217
  • Last updated
    2021-09-29 v1
  • Checksum
    56392589645D2701
MHCITSATAADLFDIAASRRIEQAAAAKLPPHALMQRAGLAVARLAMAVAPHARTVWIACGPGNNGGDGFEAAARLQRRGFMTVLTRIGDEGRLPADALASLQRARAAGVTLADAPPQYFDLAIDALLGIGNLRPPTGAMADWMQRMYGGPAPVLGVDTPSGLNTDTGTLSLELPAHGGPRVCLSLLTLKPGLFTAQGRDAAGDVWFDDLGVGTGAEPPSARLAGTPATPPRSHASHKGSYGDVAVIGGAPGMAGAVLLAASAAASAGAGRVFVAALDTAMMALDPLQPELMFRRPDTLDLAAMTVVCGCGGGSAVRELLPQVLQTARALVLDADALNAVAADGALQGLLEARARRRTATVLTPHPLEAARLLNTSAADIQGDRLHAARRLAERFGAVVVLKGSGTVIASAGETPMINASGNARLATAGTGDVLAGMVGAALAAGRPAMAAACGAVWRHGDLADRWPAEVPLTAGALARGLPQARS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR594666
EMBL· GenBank· DDBJ
VTU19503.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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