G6EHU8 · G6EHU8_9SPHN

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 site68-72(6S)-NADPHX (UniProtKB | ChEBI)
Binding site69K+ (UniProtKB | ChEBI)
Binding site130K+ (UniProtKB | ChEBI)
Binding site134-140(6S)-NADPHX (UniProtKB | ChEBI)
Binding site163(6S)-NADPHX (UniProtKB | ChEBI)
Binding site166K+ (UniProtKB | ChEBI)
Binding site255(6S)-NADPHX (UniProtKB | ChEBI)
Binding site309(6S)-NADPHX (UniProtKB | ChEBI)
Binding site357(6S)-NADPHX (UniProtKB | ChEBI)
Binding site394-398AMP (UniProtKB | ChEBI)
Binding site423AMP (UniProtKB | ChEBI)
Binding site424(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
      NSU_3919

Organism names

Accessions

  • Primary accession
    G6EHU8

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain22-221YjeF N-terminal
Domain222-478YjeF 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
    479
  • Mass (Da)
    48,832
  • Last updated
    2012-01-25 v1
  • Checksum
    396DE4E049A12174
MSSEQTPSDRTRIDQILTVAQMRDAEQALIDAGTSVDELMQVAGRGAADWVWRLAGHHKVTVLCGPGNNGGDGYVIAEAIRERGGHAVVIAATEPKTDAARNARALFKGEVIALDAPGGDVQVEGDVFVDCLFGSGLARPLTGEHAAVVNALAASHRLSIAVDLPSGVQSDNGMLLNEHLPKYDLTIALGAWKFAHFLMPASARMGELRLVPIGVEPVAGAAFAVARPAVAAPSADSHKYKRGLLAVVGGAMPGAAILASIAAQGAGAGYVKLFADSKRNAPADLVVDTGALSDVLADDRNSAVLVGPGLGRDGLARERLAVALADAVPAVVDADALILLAPRHLAERQAATIATPHEGEMVALERAFDLDGSGSRPERALALAAESGMIVVAKGPDTVIAAPDGRLACAPRATAWLSTAGTGDVLAGAIASRVASGVPAFEAACEGVWLHGEAARLCPPAFTAGQLAERIPAALAACV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGFM01000062
EMBL· GenBank· DDBJ
EHJ59082.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help