A0A0R0M9D4 · A0A0R0M9D4_9CYAN

  • Protein
    Bifunctional NAD(P)H-hydrate repair enzyme
  • Gene
    nnrE
  • 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.
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 site67-71(6S)-NADPHX (UniProtKB | ChEBI)
Binding site68K+ (UniProtKB | ChEBI)
Binding site128K+ (UniProtKB | ChEBI)
Binding site132-138(6S)-NADPHX (UniProtKB | ChEBI)
Binding site161(6S)-NADPHX (UniProtKB | ChEBI)
Binding site164K+ (UniProtKB | ChEBI)
Binding site337(6S)-NADPHX (UniProtKB | ChEBI)
Binding site387(6S)-NADPHX (UniProtKB | ChEBI)
Binding site421-425AMP (UniProtKB | ChEBI)
Binding site450AMP (UniProtKB | ChEBI)
Binding site451(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
      ASL19_13435

Organism names

  • Taxonomic identifier
  • Strain
    • CR12
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Aphanizomenonaceae > Cylindrospermopsis

Accessions

  • Primary accession
    A0A0R0M9D4

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain20-218YjeF N-terminal
Domain231-514YjeF 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
    528
  • Mass (Da)
    57,082
  • Last updated
    2016-01-20 v1
  • Checksum
    A40B592AED1509C9
MNNQDLKHLKEIFVVTAAQMRDVESRVFAAGMPIPALMEKVGRLICDRLLFMKLKGSRVGILAGPGHNGGDALVVGRELHFRGYNVWIYQPFGQLKELTNQHFHYAQSLGIPCFSQLAELPDCDFLIDGLFGFGLEREITGNIAEAINHLNLWNKPIFSIDLPSGIHTDTGAVLGTAICASHTFCLGLWKQGLLQEQAIQYTGKTELIDFDIPLADIQAVLGEVPTIKRITQSLVINTLPLPLSPIVHKYKSGHLLLICGSKRYAGGAILTGLGARASGIGMLSIAVPESLKPLLVSHLPEALIIGCPETNNGAISHLQLPGETTLNSFTVIACGPGLTTEATPIVEQVIKSEVPIILDADALNILAQLGTITTLKNRHQPTILTPHGGEFHRLFPEIDITNRVKGVQTAASQTRAIVLLKGARTAIAKHQGVTWINSESTPALARGGSGDVLTGLMGGILGQVVNRQVNMEDVVATAAWWHSQAGILAAKERTELGVDAFTLTQYLNRVLAQIQTDEISKWVELNIR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMVE01000012
EMBL· GenBank· DDBJ
KRH98130.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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