A0A2Z3WYK1 · A0A2Z3WYK1_9ENTR

  • 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

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 site71-75(6S)-NADPHX (UniProtKB | ChEBI)
Binding site72K+ (UniProtKB | ChEBI)
Binding site135K+ (UniProtKB | ChEBI)
Binding site139-145(6S)-NADPHX (UniProtKB | ChEBI)
Binding site168(6S)-NADPHX (UniProtKB | ChEBI)
Binding site171K+ (UniProtKB | ChEBI)
Binding site269(6S)-NADPHX (UniProtKB | ChEBI)
Binding site329(6S)-NADPHX (UniProtKB | ChEBI)
Binding site375(6S)-NADPHX (UniProtKB | ChEBI)
Binding site412-416AMP (UniProtKB | ChEBI)
Binding site441AMP (UniProtKB | ChEBI)
Binding site442(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
      AN232_01690

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AR_0157
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter

Accessions

  • Primary accession
    A0A2Z3WYK1

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain23-225YjeF N-terminal
Domain234-501YjeF 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    515
  • Mass (Da)
    54,398
  • Last updated
    2018-10-10 v1
  • Checksum
    F92DE3768F772D4F
MTDHTMKKNPASIPHSIWYADDIRRMEREAADSLGLTLYELMQRAGEAAFQVAREAYPHAQHWLVLCGHGNNGGDGYVVARLAKAQGLEVTLLAQESDKPLPEEAQQARDAWLNAGGVIHAADIAWPGSVDVIIDALSGTGLKHAPREALSVLIERANTYPAPIVAIDIPSGLLAQTGATPGAVINAAHTVTFIALKPGLLTGKARDVTGRLHVNALGLDDWLAGQNAPIQRFDALQLAHWLTPRRPTSHKGSHGRLVIIGGDHGTAGAIRMAGEAALRAGAGLVKVLTRSENIAPILTARPELMVDTLTPQTLDESLAWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSIAEIEDDRLLCAQRLVKRYGGVVVLKGAGTVVAAEPAELGIIATGNAGMASGGMGDVLSGIIGALLGQKLTPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFTTLQRIVNPDVIDVYHDESSNSTT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP029727
EMBL· GenBank· DDBJ
AWS94056.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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