A0A066RIA0 · A0A066RIA0_ECOLX

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnr
  • 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 site66-70(6S)-NADPHX (UniProtKB | ChEBI)
Binding site67K+ (UniProtKB | ChEBI)
Binding site130K+ (UniProtKB | ChEBI)
Binding site134-140(6S)-NADPHX (UniProtKB | ChEBI)
Binding site163(6S)-NADPHX (UniProtKB | ChEBI)
Binding site166K+ (UniProtKB | ChEBI)
Binding site264(6S)-NADPHX (UniProtKB | ChEBI)
Binding site324(6S)-NADPHX (UniProtKB | ChEBI)
Binding site370(6S)-NADPHX (UniProtKB | ChEBI)
Binding site407-411AMP (UniProtKB | ChEBI)
Binding site436AMP (UniProtKB | ChEBI)
Binding site437(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
      nnr
    • Synonyms
      nnrD
      , nnrE
    • ORF names
      BANRA_00171
      , BK300_13050
      , E2863_05047
      , NCTC10865_05623
      , NCTC8179_00936
      , NCTC8333_05225
      , NCTC8622_02054
      , NCTC8960_02023

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • 574
    • NCTC10865
    • NCTC8179
    • NCTC8333
    • NCTC8622
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A066RIA0

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-220YjeF N-terminal
Domain229-496YjeF 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
    510
  • Mass (Da)
    53,927
  • Last updated
    2014-09-03 v1
  • MD5 Checksum
    3BBDCE8A6BBA6F38C5B5F5C94848F63C
MKKNPVSIPHTVWHADDIRRGEREAADALGLTLYELMLRAGEAAFQVCRSAYPDARHWLVLCGHGNNGGDGYVVARLATAVGIEVTLLAQESDKPLPEEAALAREAWLNAGGEIHASNIVWPESVDLIVDALLGTGLQQAPRESISQLIDHANSHPAPIAAVDIPSGLLAETGATPGAVINADHTITFIALKPGLLTGKARDVTGQLHFDSLGLDSWLAGQETKIQRFSAEQLSHWLKPRRPTSHKGDHGRLVIIGGDHGTAGAIRMTGEAALRAGAGLVRVLTRSENIAPLLTARPELMVHELTMDSLTESLEWADVVVIGPGLGQQEWGKKALQKVENFRKPMLWDADALNLLAINPDKRHNRVITPHPGEAARLLGCSVAEIESDRLHCAKRLVQRYGGVAVLKGAGTVVAAHPDALGIIDAGNAGMASGGMGDVLSGIIGALLGQKLSPYDAACAGCVAHGAAADVLAARFGTRGMLATDLFSTLQRIVNPEVTDKNHDESSNSAP

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP018802
EMBL· GenBank· DDBJ
BBF56460.1
EMBL· GenBank· DDBJ
Genomic DNA
MOHC01000021
EMBL· GenBank· DDBJ
OJN37231.1
EMBL· GenBank· DDBJ
Genomic DNA
UGCD01000002
EMBL· GenBank· DDBJ
STI20225.1
EMBL· GenBank· DDBJ
Genomic DNA
UGCP01000002
EMBL· GenBank· DDBJ
STI83041.1
EMBL· GenBank· DDBJ
Genomic DNA
UGEB01000001
EMBL· GenBank· DDBJ
STK56954.1
EMBL· GenBank· DDBJ
Genomic DNA
UGFE01000002
EMBL· GenBank· DDBJ
STM26167.1
EMBL· GenBank· DDBJ
Genomic DNA
UGFO01000006
EMBL· GenBank· DDBJ
STN11793.1
EMBL· GenBank· DDBJ
Genomic DNA
UWXJ01000001
EMBL· GenBank· DDBJ
VCY81548.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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