A0A378IW12 · A0A378IW12_9GAMM

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    yjeF
  • 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 site63K+ (UniProtKB | ChEBI)
Binding site126K+ (UniProtKB | ChEBI)
Binding site130-136(6S)-NADPHX (UniProtKB | ChEBI)
Binding site159(6S)-NADPHX (UniProtKB | ChEBI)
Binding site162K+ (UniProtKB | ChEBI)
Binding site321(6S)-NADPHX (UniProtKB | ChEBI)
Binding site367(6S)-NADPHX (UniProtKB | ChEBI)
Binding site404-408AMP (UniProtKB | ChEBI)
Binding site433AMP (UniProtKB | ChEBI)
Binding site434(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
      yjeF
    • Synonyms
      nnrD
      , nnrE
    • ORF names
      NCTC11978_02615

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NCTC11978
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Legionellales > Legionellaceae > Legionella

Accessions

  • Primary accession
    A0A378IW12

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain14-216YjeF N-terminal
Domain225-493YjeF 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
    497
  • Mass (Da)
    51,931
  • Last updated
    2018-11-07 v1
  • Checksum
    CC74836070C35B03
MTTSKVALYQAKHIRLCEEMATDDLGLSEDELMLRAGTSAFSTLSMLYPTVRTLAIFCGSGNNAGDGYVLARLAHKKGYSVVVNQHKTIEDLPPPAARAAAAAIAAGVSCQCLDDAIDPEAELIVDALLGIGLQGDVHGPIATAINQINDSGLPVLALDVPSGLNADTGCVKGVAVKANVTVTFIACKLGLMTLDGPDHCGELVCHSLQLESCLLKIKPAAYLLDENLGHALLPRRLKNSHKGHFGHVLVIGGGHGMPGSVYLAANAALRVGAGLVTIATRPEYAGQVLPLLPEAMIYGIEESVELLPLIARATVCIIGPGLGEDEWAKVLFNQAIASQLPMVIDASALRLLAQNPQHDDNWILTPHPGEAASLLQCSNAEIQKDRYQTILALQQQYGGNVVLKGVGSMVCTDEPGVYLCADGNPGMASAGMGDALSGVIAGLIAQGLALAEAVKLGVWIHASAADAAAAVMGERGLLASDLMPYLRRQVNYLSRIK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UGNY01000001
EMBL· GenBank· DDBJ
STX39417.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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