A0A7U9N0C1 · A0A7U9N0C1_9FIRM

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnr
  • 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

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 site64-68(6S)-NADPHX (UniProtKB | ChEBI)
Binding site65K+ (UniProtKB | ChEBI)
Binding site126K+ (UniProtKB | ChEBI)
Binding site130-136(6S)-NADPHX (UniProtKB | ChEBI)
Binding site141(6S)-NADPHX (UniProtKB | ChEBI)
Binding site159(6S)-NADPHX (UniProtKB | ChEBI)
Binding site162K+ (UniProtKB | ChEBI)
Binding site262(6S)-NADPHX (UniProtKB | ChEBI)
Binding site320(6S)-NADPHX (UniProtKB | ChEBI)
Binding site377(6S)-NADPHX (UniProtKB | ChEBI)
Binding site414-418AMP (UniProtKB | ChEBI)
Binding site443AMP (UniProtKB | ChEBI)
Binding site444(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
      nnr
    • Synonyms
      nnrD
      , nnrE
    • ORF names
      IMSAGC003_02402

Organism names

Accessions

  • Primary accession
    A0A7U9N0C1

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-216YjeF N-terminal
Domain227-503YjeF 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
    506
  • Mass (Da)
    54,037
  • Last updated
    2021-06-02 v1
  • Checksum
    4FF7BEC109C61D32
MKYVVDAREMKHYEETVMDILGMPASVLMERAALAVAEEIRGYAAARKLRAEDKSLLVVAGSGNNGADGLAVARILSQEGWQVTVYSAGSRAHCTREWERQYKIMGFYPVRVVSNWPVEEYTVLVDALFGIGLSRQIQGEYGAVIREINRREGYKLSIDVPSGIHASTGRVMGEAVRADLTVTFGWAKKGLLFYPGAEYAGRLAVKEIGINQTCFEAAGNKPGMFYYEEPATALLPPRRPDGHKGSFGKVLLAAGFEQMPGAAVLAARAAYHAGAGMVKVVCPEENRCILQTAVPEVLWAGPEDWRQVCDWADVAAIGPGLGRNAVGKGILTGLLAESRLPLVLDADALNLIAGDMSLQILAAGQGEAGRSMILTPHEGELSRLSGKTMEQVREDREHVSRALARDLHCILVCKGARTLVCREQGEICVNLSGDNGMGTAGSGDVLTGVIAALLAQGAEAFEAASVGVYLHGLAGERAARRYGSHGLTAGRLAEAVGEYAALQVLE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BLLU01000179
EMBL· GenBank· DDBJ
GFH95851.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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