A0A1J0VDE7 · A0A1J0VDE7_9GAMM

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrE
  • 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 site68-72(6S)-NADPHX (UniProtKB | ChEBI)
Binding site69K+ (UniProtKB | ChEBI)
Binding site132K+ (UniProtKB | ChEBI)
Binding site136-142(6S)-NADPHX (UniProtKB | ChEBI)
Binding site165(6S)-NADPHX (UniProtKB | ChEBI)
Binding site168K+ (UniProtKB | ChEBI)
Binding site267(6S)-NADPHX (UniProtKB | ChEBI)
Binding site328(6S)-NADPHX (UniProtKB | ChEBI)
Binding site376(6S)-NADPHX (UniProtKB | ChEBI)
Binding site413-417AMP (UniProtKB | ChEBI)
Binding site441AMP (UniProtKB | ChEBI)
Binding site442(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
      nnrE
    • Synonyms
      nnrD
    • ORF names
      BOX17_03195

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Hb3
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Oceanospirillales > Halomonadaceae > Halomonas

Accessions

  • Primary accession
    A0A1J0VDE7

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-222YjeF N-terminal
Domain232-501YjeF 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
    511
  • Mass (Da)
    51,550
  • Last updated
    2017-02-15 v1
  • Checksum
    1FC6D1F436F923D3
MTRPAEPPALSLRPLYRAEQVRELDRRTIAAGCEGFALMQRAAAAAWQDLKARWPHVQSLTVLCGGGNNGGDGHVLAALAAAEGVAVQRILLKPVEELTGDARRAADMATAAGVSAMPWRQDVSLEGELVVDALLGTGLGGEVRGPIREAIEAVNASGLPVLAIDIPSGLQADTGAMLGVAIRATLTVTFIGDKLGLYTGAAPAHVGELAFRALEVDAEAEGDLVPAARLLEAGLIAAWLPPRPRDAHKGDAGHSLVLGGAPGFGGAALLAAEACARLGAGKVSLATAPEHVTASLVRRPEVMVHGVRGAGDLGSLPEHADVLVVGPGLGQGSWGQGMLQAALDASKPLVVDADGLNLLASRFAGRHRDDWILTPHPGEAARLLGLSVGEVEADRPAAALALQRRYGGVVVLKGAGSLVAGPEGLAVCPHGNPGMASGGMGDALSGILGALLAQGLPIEPAAWLGVLVHAMAADMAAGQGGERGLLAGDLASCARILVNPTTGEGDAAATR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP018139
EMBL· GenBank· DDBJ
APE30047.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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