E2Q2G1 · E2Q2G1_STRCL

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrE
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.

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 site118K+ (UniProtKB | ChEBI)
Binding site122-128(6S)-NADPHX (UniProtKB | ChEBI)
Binding site151(6S)-NADPHX (UniProtKB | ChEBI)
Binding site154K+ (UniProtKB | ChEBI)
Binding site251(6S)-NADPHX (UniProtKB | ChEBI)
Binding site305(6S)-NADPHX (UniProtKB | ChEBI)
Binding site350(6S)-NADPHX (UniProtKB | ChEBI)
Binding site387-391AMP (UniProtKB | ChEBI)
Binding site418AMP (UniProtKB | ChEBI)
Binding site419(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

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
      SCLAV_3677

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 / NRRL 3585 / VKM Ac-602
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces

Accessions

  • Primary accession
    E2Q2G1

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain10-208YjeF N-terminal
Domain216-476YjeF 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
    480
  • Mass (Da)
    48,067
  • Last updated
    2010-11-30 v1
  • Checksum
    462E218A070707F0
MRTAHRVEKVRAAEAELMARLPDGALMARAAAGLAAACADLLGRVYGARVVLLVGSGDNGGDTLWAGARLARRGAAVHAVLLAPDRAHAAGLAAFQAAGGRVADDPFAVLSGADLVLDGITGIGGTGGLRPAAVPVARAARGSGAVVVAVDLPSGVEADSGEVRGEALRADATVTFGTDKPGLLIDPAREHAGTVRLVDIGLGPHLPSVPDVESLQHPDVAVLLPEPSGESDKYRRGVVGVAAGSARYPGAAVLTVAGALRGGAGAVRYVGPEGAAVVARFPEALVHAGPPVKAGRVQAWVVGPGLGDDEDTVGQVLASDVPVLVDADGLRLLDPDAVRARTAPTLLTPHAGEAAALLGRDRAEVEAGRLDAVRELSARYGATVLLKGSTTLIAAPDPRLPVRADPMGTPWLATAGSGDVLSGLAGSLLAAGLPPLDAASCAAYLHGLAARRAAAVSTPITSYEVADALGAAWRDIRTPD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000913
EMBL· GenBank· DDBJ
EFG08749.1
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.
FeedbackHelp