A0A0D7X645 · A0A0D7X645_9BACL

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrD
  • 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 site131-135(6S)-NADPHX (UniProtKB | ChEBI)
Binding site132K+ (UniProtKB | ChEBI)
Binding site197K+ (UniProtKB | ChEBI)
Binding site201-207(6S)-NADPHX (UniProtKB | ChEBI)
Binding site212(6S)-NADPHX (UniProtKB | ChEBI)
Binding site230(6S)-NADPHX (UniProtKB | ChEBI)
Binding site233K+ (UniProtKB | ChEBI)
Binding site337(6S)-NADPHX (UniProtKB | ChEBI)
Binding site408(6S)-NADPHX (UniProtKB | ChEBI)
Binding site462(6S)-NADPHX (UniProtKB | ChEBI)
Binding site499-503AMP (UniProtKB | ChEBI)
Binding site528AMP (UniProtKB | ChEBI)
Binding site529(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 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
    • ORF names
      QD47_11670

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NRRL B-30644
  • Taxonomic lineage
    Bacteria > Bacillati > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus

Accessions

  • Primary accession
    A0A0D7X645

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-287YjeF N-terminal
Domain302-582YjeF 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
    582
  • Mass (Da)
    60,754
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    E6D938BDCF7BD35672CEEBC5A3F2670D
MYIVTAEEMRQLDRYTIDKLGIPALTLMENAGRAVADEVLKLCAMESGWSHKSFSESHVDSAYGTERRYIVGQDAAKQGYDEGPAYGEQVAHSGPGDTPGHGGVIRTEPWSHGRHAMWEREHWYILVGKGNNGGDGLVAARHLTDAGLRVTVVYAESPDTLRGEAAVQRDTIAALHIPALVYGRDALDLRGASGIVDALLGTGTQGPPREPYASLVREANASGVPLVSVDVPSGLDADTGALYEPCIRARVTVCLAYLKCGLVQYPGAGNAGDVVVRYIGIPPGLAREHGVQLRLLTRDTLREALGVDVSRSRVPDGHKGTYGHVLVAAGSLRMSGAGLLAARAALRIGSGLVTWAVPEALLPRLIGAAPELMLAAAAAGGDGEWNAGSADVLLQLAQARDVLAVGPGLGRFAGDTGWLRRLWEEYSGPLVLDADALNILAAAGPELEAWKPRGAAVVLTPHPGEMARLLGISTAEVQRERIAHARQYARTRGVTLVLKGARTVIACPDGAVYVNTTGHAGMATGGAGDVLTGIIAGLLAQGLNASQAAAFGVYLHGAAGETAARHRQHAASVIAGDIIEAL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JTHP01000019
EMBL· GenBank· DDBJ
KJD45497.1
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.
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