A0A1W1ZB13 · A0A1W1ZB13_9FIRM

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 site58-62(6S)-NADPHX (UniProtKB | ChEBI)
Binding site59K+ (UniProtKB | ChEBI)
Binding site128K+ (UniProtKB | ChEBI)
Binding site132-138(6S)-NADPHX (UniProtKB | ChEBI)
Binding site161(6S)-NADPHX (UniProtKB | ChEBI)
Binding site164K+ (UniProtKB | ChEBI)
Binding site263(6S)-NADPHX (UniProtKB | ChEBI)
Binding site333(6S)-NADPHX (UniProtKB | ChEBI)
Binding site383(6S)-NADPHX (UniProtKB | ChEBI)
Binding site417-421AMP (UniProtKB | ChEBI)
Binding site446AMP (UniProtKB | ChEBI)
Binding site447(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
      nnrE
    • Synonyms
      nnrD
    • ORF names
      SAMN02745168_0930

Organism names

Accessions

  • Primary accession
    A0A1W1ZB13

Proteomes

Interaction

Subunit

Homotetramer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-218YjeF N-terminal
Domain228-506YjeF 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
    506
  • Mass (Da)
    53,234
  • Last updated
    2017-06-07 v1
  • Checksum
    4A9C101BDD6FC36F
MKLATARQMKELDGYAIHTLGISSLLLMENAAAALAEEAAGCLMNPGERIAVFCGGGNNGGDGAAAARILARNGAEVRLFLTGDREKFTPDLKEMLARYETAGGEPEEFIPGDPECEAWCAGASVLIDALFGIGLNSPLRGRPLAAVELMNRLKVPVVAADIASGVESDTGQILGAAPKCVKTITFTYPKIGHFCGEGGLLCGDLRVAGIGIPEEALSRIPDKIFAVDDEDTRELLPRRRRDSHKGDYGRVLLVCGSRDYTGAPAFSARAAVRTGSGLVFLGVPASIHGIEAEKNDEAMVISLPEEEGKLSPGAVPVILEQLRGCDACLIGPGLGRSEGVSAAVRAVLETCRVPLVIDADGINALAGNIDIWKRNCPVILTPHEGEFQRLLGRPMKADRISQAREFAQASGCILILKGYRTVTALPDGRVYINTTGNPGMAKGGSGDVLSGMLVSLLGQGLSPERAAWGAVWLHGRAGDTTASEKGEYGMTPTDMIEAIPKATMQY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FWXW01000002
EMBL· GenBank· DDBJ
SMC45607.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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