A0A2W1A7A3 · A0A2W1A7A3_UNCCH

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrE
  • 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.
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 site58-62(6S)-NADPHX (UniProtKB | ChEBI)
Binding site59K+ (UniProtKB | ChEBI)
Binding site125K+ (UniProtKB | ChEBI)
Binding site165(6S)-NADPHX (UniProtKB | ChEBI)
Binding site168K+ (UniProtKB | ChEBI)
Binding site265(6S)-NADPHX (UniProtKB | ChEBI)
Binding site334(6S)-NADPHX (UniProtKB | ChEBI)
Binding site390(6S)-NADPHX (UniProtKB | ChEBI)
Binding site427-431AMP (UniProtKB | ChEBI)
Binding site455AMP (UniProtKB | ChEBI)
Binding site456(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
      nnrE
    • Synonyms
      nnrD
    • ORF names
      DK305_000652

Organism names

Accessions

  • Primary accession
    A0A2W1A7A3

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-222YjeF N-terminal
Domain230-515YjeF 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
    521
  • Mass (Da)
    57,193
  • Last updated
    2018-09-12 v1
  • Checksum
    BB1C1FEF81773806
MIVITKEEMQDAEKRAFASNLNQENIIEKAGVIIAQEAWVNTTASKNTKIIILVGPGNNGSDGLVAARFLSSWKATVTILLISKRNDLNKYLKDEQKNIKCIEMIKNHEARTITKKIKESECIIDALYGIGWDINRKQKTDEYNLKKLLDKIQLHRDRQFILCVDIPTGVDANTGQCIKNTLTADMTITFGAIKIGMTQQPGSSKVGNIIIEGLGIDHFIKERSSAHIISKNDFHKNIIKRKSASNKGHFGKILVIAGSRIYPGAAILTCEAAAIAGAGIITLASSKFVQQINITKQPELTLFDTGNSEYLDESIFPQLIRQVDNFNAIVIGPGISQNKRTVLLINKIIEFLKKNKHSIPLILDADGLNILAKMENWPFKLSKNVILTPHPGEMARLLKKSITEIQSNRIKYASILAKKTEATVILKGPGTIIVSENNIMISDVSVPALATPGTGDILSGLIGGFLSQKLLPIDAACFGVYAHALAGQEVEKNIGNISSKASDLFKYLPKTIKEIVYAKDK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QGNP01000006
EMBL· GenBank· DDBJ
PZC40537.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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