A0A2V4UWN7 · A0A2V4UWN7_9GAMM

  • Protein
    Multifunctional fusion protein
  • Gene
    nnrD
  • 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

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 site89-93(6S)-NADPHX (UniProtKB | ChEBI)
Binding site90K+ (UniProtKB | ChEBI)
Binding site184K+ (UniProtKB | ChEBI)
Binding site188-194(6S)-NADPHX (UniProtKB | ChEBI)
Binding site199(6S)-NADPHX (UniProtKB | ChEBI)
Binding site221(6S)-NADPHX (UniProtKB | ChEBI)
Binding site224K+ (UniProtKB | ChEBI)
Binding site326(6S)-NADPHX (UniProtKB | ChEBI)
Binding site387(6S)-NADPHX (UniProtKB | ChEBI)
Binding site450(6S)-NADPHX (UniProtKB | ChEBI)
Binding site487-491AMP (UniProtKB | ChEBI)
Binding site519AMP (UniProtKB | ChEBI)
Binding site520(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
Biological Processphosphorylation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion 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
  • Alternative names
    • NAD(P)HX epimerase

Gene names

    • Name
      nnrD
    • Synonyms
      nnrE
    • ORF names
      DFP82_109122

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CECT 5889
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Psychrobacter

Accessions

  • Primary accession
    A0A2V4UWN7

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain23-279YjeF N-terminal
Region120-140Disordered
Domain286-596YjeF 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
    599
  • Mass (Da)
    64,777
  • Last updated
    2018-09-12 v1
  • Checksum
    41FDCC0F9D5E0E18
MQIHGHSSIDKKHPISLYSSKQLYAMEQAWFSEGHDSFGLMQQAAWQMAKHIEQLYEKKYLNHHSSASVNFSHRHNHQYRVSIWVGKGNNGGDGWLIAYYLKQAGWQVQIVTVGFEDSDFSNSDSDQVNSDKSDTTAISNSKSSITDAQKALQVARSANCKYERFEDSQNDLRSTALQADVYIDALFGIGLDRTPEGIYKQAIRAFNELTEQNNGLAIAVDIPSGVVASTGEVFDRIAIKADATLCLIARKFGLHTKDGVDYSGQVTDIPLIPYQVDNVAFEPVAKLITTGQAFSPRRQNSYKGSYGHVLVIGGNRIDGSQGMGGAAILSASSSMAAGAGKITVACHEAFHGALLTSLPDAMTINLHDAQGVQHLIKAASVVAIGMGLGRDDKAQALFVNYIQAAMTAKKPIVIDADGLYHLASLQLKNDKLISQLREYSTDNEVCLTPHSGEAAKLLNKKIHEIESDRLSAIKLCAQTYGGNWVLKGAGSLVLERGLDQEQVYVCGVGNAGMATAGMGDVLSGVIAGLLAQQDLEPEMRSLHQAVIIHGLAGDILVSQTNQYNSGKSDRGHLLIGQRGLQAQDMPVAIRHVMQLLVDS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QJSU01000009
EMBL· GenBank· DDBJ
PYE38172.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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