F2NU31 · F2NU31_TRES6

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.

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 site63-67(6S)-NADPHX (UniProtKB | ChEBI)
Binding site64K+ (UniProtKB | ChEBI)
Binding site131K+ (UniProtKB | ChEBI)
Binding site135-141(6S)-NADPHX (UniProtKB | ChEBI)
Binding site164(6S)-NADPHX (UniProtKB | ChEBI)
Binding site167K+ (UniProtKB | ChEBI)
Binding site262(6S)-NADPHX (UniProtKB | ChEBI)
Binding site309(6S)-NADPHX (UniProtKB | ChEBI)
Binding site359(6S)-NADPHX (UniProtKB | ChEBI)
Binding site437AMP (UniProtKB | ChEBI)
Binding site438(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionADP-dependent NAD(P)H-hydrate dehydratase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular FunctionNAD(P)HX 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
    • Ordered locus names
      Tresu_0025

Organism names

Accessions

  • Primary accession
    F2NU31

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain8-219YjeF N-terminal
Domain229-490YjeF 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    490
  • Mass (Da)
    53,831
  • Last updated
    2011-05-31 v1
  • MD5 Checksum
    3F076CC161BDAAF5D79D4D5DAB139098
MQNIFFDTRILDKKSREKFYLTEELMMENAAQELESCVMPHVFHESSRYINRPCVLILAGRGNNGADGYVLARRLSCHDFCVAVCCIGEPSSEIAKVQKKRAELLGVSFISPYDLDSFVEEKSFDISVVVDCVYDSGFHLPLDAESEAVIQSANKIEAFKVSCDVPSGLDSDGNGKIVFRADETVAMGALKLSLFSDKAKDFCGKVKVCNLGISRNNFEFLETPDAFLLEKEEMKLPFRKMQNVHKGTFGHVALAAGEKTGAAKIAANSAFAFGAGLVTLVGIEDSGFMNIMASLELPENTTALVLGCGFGRKNPSFQKYFDFFKENKNIPCVLDADIFYYKEILNLLTERGNFVLTPHPKEFSALLENCGFGKFSVQEIVEKRIELIKLFCGKFKDSVLVLKGAVVLIGTWSKNEGRVKIYLNPYGNNSLAKGGTGDILSGLIASLLAQGYDCVNAAVTASLAHSFASEKVKNNFALTPQLLIEKISEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002631
EMBL· GenBank· DDBJ
AEB12995.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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