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H6R0W8 · H6R0W8_NOCCG

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.

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 site246(6S)-NADPHX (UniProtKB | ChEBI)
Binding site299(6S)-NADPHX (UniProtKB | ChEBI)
Binding site349(6S)-NADPHX (UniProtKB | ChEBI)
Binding site383-387AMP (UniProtKB | ChEBI)
Binding site412AMP (UniProtKB | ChEBI)
Binding site413(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
    • Ordered locus names
      NOCYR_0931

Organism names

Accessions

  • Primary accession
    H6R0W8

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-206YjeF N-terminal
Domain211-473YjeF 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    478
  • Mass (Da)
    48,237
  • Last updated
    2012-04-18 v1
  • MD5 Checksum
    617274EB47328CEF15128B005D6B7505
MCSQRGYYSVDAVREAEAELFTRVAAGVPMRRAAYGLANVVAGELRARTGGVAGRSVTLLVGSGDNGGDALWAGSFLRRRGVSVDAVLLNPDRAHAEGLAALRKAGGRVRAEVGRPDLVIDGIVGISGRGSLRPEAAEIVSRIEAPIVAADLPSGVDPDNGAVDGPAVRAQVTVAFGACKPVHALAADRCGRIELVPIGLQLPEPGLAALEPSEIGARWPVPGATDDKYSQGVTGVCAGSAAYPGAAVLCTGGAVAATSGMVRYAGSGADQVLAQFPEVIAARNIASTGRVQAWVFGPGSGTDDGAWARMAQILSTDLPVVIDADGLTLLAEHPAMVRDRTAPTVLTPHAGEFARLTGESLGVDRVTAVRELAESWGATVLLKGRATLVAEPGKPVLVNEAGGSWAATAGAGDVLSGVIGSLLAAGREPGWSAAAAARAHALAANLAAAEGPAAAPISATPLLNHLRPAIRTLRALAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FO082843
EMBL· GenBank· DDBJ
CCF61742.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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