A0A5E5R102 · A0A5E5R102_PSEAI

  • 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 site68K+ (UniProtKB | ChEBI)
Binding site130K+ (UniProtKB | ChEBI)
Binding site134-140(6S)-NADPHX (UniProtKB | ChEBI)
Binding site163(6S)-NADPHX (UniProtKB | ChEBI)
Binding site166K+ (UniProtKB | ChEBI)
Binding site264(6S)-NADPHX (UniProtKB | ChEBI)
Binding site325(6S)-NADPHX (UniProtKB | ChEBI)
Binding site373(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 Functionmetal ion binding
Molecular FunctionNADHX epimerase activity
Molecular FunctionNADPHX 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
      TUEID40_02908

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ID40
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A5E5R102

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain20-220YjeF N-terminal
Domain229-497YjeF 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
    502
  • Mass (Da)
    51,641
  • Last updated
    2019-11-13 v1
  • Checksum
    336FC0AE9E118756
MTMTFQHDDLPLALYSAAQVRDLDARLIAAGTPGFELMQRAAHAAWRALRRRWPEAAALTVLAGHGNNAGDGYLIAALAQRAGWRVRVLAVAAPQRLAGDAAQAHAAALATGVVVEPWSECAVLEGVVVDALLGTGLAGAVREPFAQAIRLANAADLPVLAVDIPSGLSADTGAVLGEAIRADLTVTFIGLKIGLFTGEAPARVGELVFDELGSDAVVLQGLQPRAHRLARNALPSLAARPRTAHKGLFGHLLVVGGDTGMGGAVLLAAESALRCGAGLVSVATRVEHVPALLSRCPEVMAHGVASANQLLALAERASVLMLGPGLGQRAWGRSLLSAVRSRPLPQVWDADALNLLALEPVGAGPRTWILTPHPGEAARLLGRSTTEVQADRPAAALELARRYQAVVVLKGAGSLVAAPDGRLAVCSQGHPAMAGAGLGDVLSGITGALLAQRVEAFEAACLAVWLHAAAGERLGAQGRGLAATDLIPTVRQLLEECSPCLK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR700248
EMBL· GenBank· DDBJ
VVH81727.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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