A0A430FAP8 · A0A430FAP8_9BIFI

  • Protein
    ADP-dependent (S)-NAD(P)H-hydrate dehydratase
  • 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
K+ (UniProtKB | Rhea| CHEBI:29103 )

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site319(6S)-NADPHX (UniProtKB | ChEBI)
Binding site434(6S)-NADPHX (UniProtKB | ChEBI)
Binding site476-480AMP (UniProtKB | ChEBI)
Binding site509AMP (UniProtKB | ChEBI)
Binding site510(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

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ADP-dependent (S)-NAD(P)H-hydrate dehydratase
  • EC number
  • Alternative names
    • ADP-dependent NAD(P)HX dehydratase

Gene names

    • Name
      nnrD
    • ORF names
      D2E22_0364

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 2020B
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium

Accessions

  • Primary accession
    A0A430FAP8

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-25Disordered
Domain38-277YjeF N-terminal
Domain284-599YjeF C-terminal

Sequence similarities

Belongs to the NnrD/CARKD 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
    606
  • Mass (Da)
    61,981
  • Last updated
    2019-05-08 v1
  • Checksum
    F08F0E056D68A6D8
MNDHGTSGAGMAGTQDIEAEEGPRTDMLRSNAYGVATVKALERPLLDDGAPLMRMAAAAAARRVLDVIDEQDWEADALRVCVLAGAGDNGGDGLYCGAMLAGEGLNVTAIAVGRSLHDEAYAAFREAGGHVFTLDPNASIPGAPVGFSSGEAGARLEQAVRFASRAHIIIDAMTGIGVNGALRGIPAAIAEAVGKRGAPGRPALPDDELDIEFPFVLAIDTPSGIGVEDGALPGAYIPADMTMMFGALKPCAMLPPACYACGRVTLVDFGFDVDDAEPDVEIVDRAFAQSAIRIPRLEDAKYERGVTGLITGSDAYPGAAVLSVCAAARSNIGMVRYLGPGRAQDLVLHALPEAVVGKGHVQSWVVGCGVPDGAHGDERDLQRARAKALLAHYSLDGDEDTRRAALAMPPVVVDAGALDLLPAHVPAHVVITPHAGEMAALLTRLGEAADAADVAARPLAAARRVCELTGATVLLKGAMTVIVGADDAGATRTLVCGRAPAFLATAGAGDVLAGITGAMLAQQADEVVADPSLAAEVVAGAAYVHGLAAALASHSDQRAWKEPALFSDGDEDTLAAESVGHPIIAMDVVDALPAAFDMLNATARYE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QXGI01000001
EMBL· GenBank· DDBJ
RSX49903.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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