Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A1H1PFZ1 · A0A1H1PFZ1_9BRAD

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrD
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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 site61-65(6S)-NADPHX (UniProtKB | ChEBI)
Binding site62K+ (UniProtKB | ChEBI)
Binding site122K+ (UniProtKB | ChEBI)
Binding site126-132(6S)-NADPHX (UniProtKB | ChEBI)
Binding site155(6S)-NADPHX (UniProtKB | ChEBI)
Binding site158K+ (UniProtKB | ChEBI)
Binding site257(6S)-NADPHX (UniProtKB | ChEBI)
Binding site320(6S)-NADPHX (UniProtKB | ChEBI)
Binding site375(6S)-NADPHX (UniProtKB | ChEBI)
Binding site413-417AMP (UniProtKB | ChEBI)
Binding site442AMP (UniProtKB | ChEBI)
Binding site443(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
    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
      SAMN05444158_1002

Organism names

  • Taxonomic identifier
  • Strain
    • GAS369
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0A1H1PFZ1

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-212YjeF N-terminal
Domain222-497YjeF 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
    505
  • Mass (Da)
    52,785
  • Last updated
    2017-01-18 v1
  • MD5 Checksum
    9C3371CA7E5804424F0AF78174645B86
MYREFGMEVLTTAEMERADRLAIAAGTPGFALMLSAGQAVAQAAIELVEEGPILVVAGRGNNGGDGFVAAAELAARGREVSVILLCERDSLQGDAASAARGWKHPVLPFNPQAIGKPALIVDALFGAGLNRPVKGEPYDMIEAINANGAPVLSIDLPSGINGTTGAVMGIAVRATETVTFFRSKPAHLLLPGRIYCGRIRVADIGIDAQVLSEIAPQTFENVPPFWRSHFPVPQVDGHKYARGHAVVVSGDITATGAARMSARGALRTGAGLVTLATPRDALAVNAAALTAVMVRPTDTVVEFAELLNDKRFNACVIGPGAGVSERTRDFVLTALAAQRDLVLDADALTSFADAPDRLFEAIKASPDPKVVLTPHEGEFPRLFSDISNKHPFRSKLERVRAAAERSGAVVLLKGADTVVASPDGRATIAANAPPWLATAGAGDVLSGMIAGLLAQGAPAFEAACIGVWMHGEAAQEAGPGLIAEDLPETLPAVFRRLYDEFGVEY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LT629750
EMBL· GenBank· DDBJ
SDS10000.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help