A0A1V5LZL4 · A0A1V5LZL4_UNCXX

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnr
  • 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.
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 site58-62(6S)-NADPHX (UniProtKB | ChEBI)
Binding site59K+ (UniProtKB | ChEBI)
Binding site95K+ (UniProtKB | ChEBI)
Binding site99-105(6S)-NADPHX (UniProtKB | ChEBI)
Binding site130(6S)-NADPHX (UniProtKB | ChEBI)
Binding site133K+ (UniProtKB | ChEBI)
Binding site232(6S)-NADPHX (UniProtKB | ChEBI)
Binding site303(6S)-NADPHX (UniProtKB | ChEBI)
Binding site354(6S)-NADPHX (UniProtKB | ChEBI)
Binding site420AMP (UniProtKB | ChEBI)
Binding site421(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
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
      nnr
    • Synonyms
      nnrD
      , nnrE
    • ORF names
      BWY76_00977

Organism names

Accessions

  • Primary accession
    A0A1V5LZL4

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane217-241Helical

Keywords

  • Cellular component

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-187YjeF N-terminal
Domain197-480YjeF 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.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    483
  • Mass (Da)
    50,267
  • Last updated
    2017-06-07 v1
  • Checksum
    34844637EC0059B7
MKLVTAEQMRALDRYAIEELGIPGLTLMERAGEAVASETARLLDAYPGMVLVLCGKGNNGGPDARANYDRAVEARVTILSEVTDADLREAGVIVDALLGTGVSGAVRGELASLIERVNALRAGCGVLAVDVPSGVETNTGQVPGTAMRAELTVTMGLPKPCLLLYPAAEFAGEWAVADIGFPPEVVDGWNAVAEMTELEQVSEWVPARRPTAHKMDVGAVLVIAGSFGMTGAAAMAATAAYRAGAGLVRLALPASLTAALNAQLTEVVFRPMSETRAGTLSFHGFQRLLDEVEGTRAVLLGPGLSRHPATAHLIRRLVPLIHAPLVVDADALTAMVGHDRLWRQREKPTVITPHPGEMSRLLGQPATVLEEDRIAAAKEAARRFNATVVFKGSPVVIAAPDGRTFVNPTGTPALAVVGTGDVLAGMIAALIAQRVEVAHAAALACFTGGLAAQRMTAQLGLRGFTALDLIAAIPHGLAEVAGE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MWAH01000159
EMBL· GenBank· DDBJ
OPZ86379.1
EMBL· GenBank· DDBJ
Genomic DNA

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