A0A1T4K1T0 · A0A1T4K1T0_9FIRM

  • 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 site59-63(6S)-NADPHX (UniProtKB | ChEBI)
Binding site60K+ (UniProtKB | ChEBI)
Binding site128K+ (UniProtKB | ChEBI)
Binding site132-138(6S)-NADPHX (UniProtKB | ChEBI)
Binding site167(6S)-NADPHX (UniProtKB | ChEBI)
Binding site170K+ (UniProtKB | ChEBI)
Binding site269(6S)-NADPHX (UniProtKB | ChEBI)
Binding site365(6S)-NADPHX (UniProtKB | ChEBI)
Binding site422(6S)-NADPHX (UniProtKB | ChEBI)
Binding site466-470AMP (UniProtKB | ChEBI)
Binding site495AMP (UniProtKB | ChEBI)
Binding site496(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
      SAMN02745110_00099

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ATCC 17233
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Eubacteriales > Eubacteriaceae > Eubacterium

Accessions

  • Primary accession
    A0A1T4K1T0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain10-224YjeF N-terminal
Domain234-553YjeF C-terminal
Region316-341Disordered

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
    553
  • Mass (Da)
    58,790
  • Last updated
    2017-05-10 v1
  • Checksum
    1B7070190618FF8C
MKYFTTGAKSALIDKISIEEVGMPQMVLMERASLGVAGAAAEFIKDKKQKILTVVEGGNNGGDGVAAARILKERGFNVDIFYIGGIKKTSEAFLEQIKIAENCGVKIYKASDDYSLKSLLVGYDIVIDGIFGVGLSREIGGVQAEAINIINDAKEERQNDLAVISIDIPSGVSADNGELLGVAVKADVTVTFGFTKVGMLFGKGREYSGKIILKDIGFPACAVEKTAPEYYGLDIDDIKKILPVRKDDSNKGNFGRLLIVAGNDSIAGAAVIAGQAAFKAGAGLVKIFTHKDNRNIIGAALPEALLDVYEYNSDSEESSDGTNHSAGKCSGKITSPGGEQSGEIISSTDIESLVKWATAIAIGPGLGTSEKSKYLLKAVLKAAYENDKPVVMDADAINIISEDRSILKNLRFEEKKWIITPHMLEMARLIKTEDENAKDALGRIFKDRFEVAKYVSNEYNIISVLKDARTVVSDGSSRCFINTNGNSGMSKGGSGDSLTGIIGALLAEGMKPQDAARAGVFIHGAAGDIAALKCGRTSMTVTDLNGVIDMIKR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FUXA01000003
EMBL· GenBank· DDBJ
SJZ36391.1
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