A0A0Q4EPY7 · A0A0Q4EPY7_9SPHN

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.
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 site61-65(6S)-NADPHX (UniProtKB | ChEBI)
Binding site62K+ (UniProtKB | ChEBI)
Binding site118K+ (UniProtKB | ChEBI)
Binding site122-128(6S)-NADPHX (UniProtKB | ChEBI)
Binding site187(6S)-NADPHX (UniProtKB | ChEBI)
Binding site190K+ (UniProtKB | ChEBI)
Binding site277(6S)-NADPHX (UniProtKB | ChEBI)
Binding site329(6S)-NADPHX (UniProtKB | ChEBI)
Binding site377(6S)-NADPHX (UniProtKB | ChEBI)
Binding site410-414AMP (UniProtKB | ChEBI)
Binding site439AMP (UniProtKB | ChEBI)
Binding site440(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

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
      ASE69_07000

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Leaf208
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingomonas

Accessions

  • Primary accession
    A0A0Q4EPY7

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, compositional bias, region.

TypeIDPosition(s)Description
Domain15-244YjeF N-terminal
Compositional bias128-158Polar residues
Region128-160Disordered
Domain244-494YjeF 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
    494
  • Mass (Da)
    50,099
  • Last updated
    2016-01-20 v1
  • Checksum
    640F617DC5E7ADEE
MIGIEGQPVLTAAEMRAAEDAVIATGVSVDTLMERAGTAIAGVVRRLAGTNEVLILCGPGNNGGDGYVAARVLAEMGVPVRVAALSEPKTDAAKSARAGWLGPVETLAEAKPAPILVDALFGTGLTRPLDASTTPTPNRSPADAGAQLNTNGSPSGLSWAPASAGERSVVKCLHFLANAAQLRVAVDLPSGLATDSGEVLSTPPVFNLTLALGAVKPAHLLQPAARYCGQIRLLDIGVPTASQAEVLKAPSLPTPGPDSHKYTRGMVAIIAGTMSGAADLAALAAMRAGAGYVTLLGDSQGPPHALVRTPFSDHALANDRIGALVIGPGLGRDDTATARLEAALTSGHPLIIDGDALRLLDPDRIKVLKVPVILTPHAGEFDALFGKSDADKITRARDAATRANVIVVFKGADTVIAAPDGRVRIAQGSSDWLSTAGTGDVLAGAIGAMLAAKLDPLDAACAGVWLQGDAARRLGAAFIADDLAEALRSARASL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias128-158Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMKH01000023
EMBL· GenBank· DDBJ
KQM51082.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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