A0A2V7LJM4 · A0A2V7LJM4_UNCGE

  • 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.
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 )

Note: Binds 1 potassium ion per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site110-114(6S)-NADPHX (UniProtKB | ChEBI)
Binding site111K+ (UniProtKB | ChEBI)
Binding site170K+ (UniProtKB | ChEBI)
Binding site174-180(6S)-NADPHX (UniProtKB | ChEBI)
Binding site203(6S)-NADPHX (UniProtKB | ChEBI)
Binding site206K+ (UniProtKB | ChEBI)
Binding site298(6S)-NADPHX (UniProtKB | ChEBI)
Binding site363(6S)-NADPHX (UniProtKB | ChEBI)
Binding site408(6S)-NADPHX (UniProtKB | ChEBI)
Binding site446-450AMP (UniProtKB | ChEBI)
Binding site475AMP (UniProtKB | ChEBI)
Binding site476(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
      DMD60_02695

Organism names

Accessions

  • Primary accession
    A0A2V7LJM4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-26Basic residues
Region1-51Disordered
Domain60-257YjeF N-terminal
Domain263-535YjeF 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
    555
  • Mass (Da)
    57,311
  • Last updated
    2018-09-12 v1
  • Checksum
    7A30A1F8A0815236
MRPGARRHGPGGRSRAGRRARRHRALQPLRHGDGGRRRRGGIRRGGHPVNPIPVLSATEAAAWDSAARTQYRIPSRVLMEAAGRAVAYLIVRDYPAILARGALVVAGAGNNGGDGWVVARALHASGIPVWVAALDPKTDDAIDNRALARVDGVRETGREEPWPAAAVVIDALLGTGAAGPARGDVLALAQRLVAYAAPVIAIDGPTGLDLSSGEAHGPVRAELSITFGGPRRGHLLAREWCGKIVVIDIGLPPADPVWPLLVTDVWAGVRLPKLTPTMHKGDRGRVTVVGGGSGMTGAALHAARGALAAGAGLVKLVAATETIEAARASLPDVLTVESTLGPELEPEAAEALEWADALVVGPGLGREPPRAQFLQAVLARRPIPTVLDADALILFHGSAERPVVLTPHLGEFRAQFGDELADAAANDRWAAAAKAAQKVKGTVLLKGVPTVIADLRGPIHVVASGNPGLATGGSGDLLAGFIGAFLARGSAGPEAAALGAHALGRAAEHGARQWTARSLRPADVLAALPEIWRAWTNTQPVGPPVLTVLEPPETA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-26Basic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QHUD01000045
EMBL· GenBank· DDBJ
PYO99023.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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