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A0A4D6HPR5 · A0A4D6HPR5_9EURY

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • 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

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 site54-58(6S)-NADPHX (UniProtKB | ChEBI)
Binding site55K+ (UniProtKB | ChEBI)
Binding site120K+ (UniProtKB | ChEBI)
Binding site124-130(6S)-NADPHX (UniProtKB | ChEBI)
Binding site153(6S)-NADPHX (UniProtKB | ChEBI)
Binding site156K+ (UniProtKB | ChEBI)
Binding site235(6S)-NADPHX (UniProtKB | ChEBI)
Binding site304(6S)-NADPHX (UniProtKB | ChEBI)
Binding site414AMP (UniProtKB | ChEBI)
Binding site415(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
      nnrD
    • Synonyms
      nnrE
    • ORF names
      DV706_11580

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JCM 10635
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Natronorubrum

Accessions

  • Primary accession
    A0A4D6HPR5

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain7-205YjeF N-terminal
Domain204-472YjeF 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
    475
  • Mass (Da)
    48,539
  • Last updated
    2019-07-03 v1
  • MD5 Checksum
    1B6B2061157EA8523F6ABDAC1DF8902B
MITGKRMAAVDENAAALGVPRKQLMESSGHAVAREVKDLTEPGARVAIVAGRGNNGGDAFVTARFLDAYDVTTLLLGRAEAIGTRISKENWNALECADYDTREVTDSSAFDLPEADVIVDAMLGTGISGDLREPAATAAEAINAADATVVAVDVPSGFDADEGDHADNGVEADHVVTFHDEKPGLADLEATVAVADIGIPAAAERLVGPGDVALARPDSRTGRAFVIGGGPYTGAPALAAQAALRTGMELSFVAAPESVAGEIQGYSEDLIVQPYEHDILTPAQVDDLVDTAERYDDVVVLGPGLGTADETLEAARKFLESYTGPAVVDADALAIVPGLETDATLVCTPNRRELARMGGPDVDALAPVADEIEAFAAALGHVVLAKGVDDVVTDGNRTHISRSGTPGMAVGGTGDTLAGVTAALLEHAGPLEAAAAAAQVNGLAGERLADRDGNGLLASELCAQLPAVLWGESNE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP031305
EMBL· GenBank· DDBJ
QCC55052.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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