Q9HQ90 · Q9HQ90_HALSA

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 site48-52(6S)-NADPHX (UniProtKB | ChEBI)
Binding site49K+ (UniProtKB | ChEBI)
Binding site114K+ (UniProtKB | ChEBI)
Binding site118-124(6S)-NADPHX (UniProtKB | ChEBI)
Binding site147(6S)-NADPHX (UniProtKB | ChEBI)
Binding site150K+ (UniProtKB | ChEBI)
Binding site233(6S)-NADPHX (UniProtKB | ChEBI)
Binding site301(6S)-NADPHX (UniProtKB | ChEBI)
Binding site347(6S)-NADPHX (UniProtKB | ChEBI)
Binding site411AMP (UniProtKB | ChEBI)
Binding site412(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
    • Ordered locus names
      VNG_1272C

Organism names

Accessions

  • Primary accession
    Q9HQ90

Proteomes

PTM/Processing

Proteomic databases

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-198YjeF N-terminal
Domain200-469YjeF 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
    472
  • Mass (Da)
    47,080
  • Last updated
    2001-03-01 v1
  • Checksum
    DBFDC5231D4FFEA4
MAAVDRNAAALGVPRAQLMESSGHAVGRAVKRVADPGASVAIVAGRGNNGGDAFAAARFLDDYAVSVSLLGRPESINDRISRANWDALQAGGYDTTTVRDAHALALDDPDVVVDALLGTGISGPPREPEATAIERINATDAPTVAVDVPSGLDADTGATPGSAVDADRVVTFHDTTPGLADHDHVTVADIGIPEAAETVVGPGDLLGVDRDPHGHKGDAGSVLVIGGGPYTGAPALCAQAALRAGADLVRLAVPDAVAAEVQGFDETFIVDSVVGTRLVEEHVPDLLARAEDADAVVIGPGLGDADTTQAAVAAFLAAFEGRAVVDADALTAVPDVETDATLVCTPHRGELQAMGGPTVDGSQPSRDAVEGFAAELGQTLLVTGARDVLSDGDTTRVNRSGTPGMTVGGTGDVLAGTAAAMLATQPPIQAASAAAYATGGAGERAAEARGHGLLATDICDALPAAIWGGQDA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE004437
EMBL· GenBank· DDBJ
AAG19626.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp