A0AA38XX18 · A0AA38XX18_9EURO

  • Protein
    Multifunctional fusion protein
  • 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 ATP, which is converted to ADP. 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 site61-65(6S)-NADPHX (UniProtKB | ChEBI)
Binding site62K+ (UniProtKB | ChEBI)
Binding site124K+ (UniProtKB | ChEBI)
Binding site128-134(6S)-NADPHX (UniProtKB | ChEBI)
Binding site157(6S)-NADPHX (UniProtKB | ChEBI)
Binding site160K+ (UniProtKB | ChEBI)
Binding site320(6S)-NADPHX (UniProtKB | ChEBI)
Binding site366-372(6S)-NADPHX (UniProtKB | ChEBI)
Binding site403-407ATP (UniProtKB | ChEBI)
Binding site423-432ATP (UniProtKB | ChEBI)
Binding site433(6S)-NADPHX (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular FunctionADP-dependent NAD(P)H-hydrate dehydratase activity
Molecular FunctionATP binding
Molecular FunctionATP-dependent NAD(P)H-hydrate dehydratase activity
Molecular Functionmetal ion binding
Molecular FunctionNAD(P)HX epimerase activity
Biological Processmetabolite repair
Biological Processnicotinamide nucleotide metabolic process
Biological ProcesstRNA threonylcarbamoyladenosine modification

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    ATP-dependent (S)-NAD(P)H-hydrate dehydratase
  • EC number
  • Alternative names
    • ATP-dependent NAD(P)HX dehydratase
  • Recommended name
    NAD(P)H-hydrate epimerase
  • EC number
  • Alternative names
    • NAD(P)HX epimerase

Gene names

    • ORF names
      H2204_010562

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • TK_35
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Trichomeriaceae > Knufia

Accessions

  • Primary accession
    A0AA38XX18

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain13-214YjeF N-terminal
Domain224-491YjeF 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
    631
  • Mass (Da)
    64,737
  • Last updated
    2024-01-24 v1
  • MD5 Checksum
    24A3656117FA8ABCD76E546E46338A27
MANLADLFDSRAARMLDAQASALAGDGGWGLMAQAGQAAWQCLLQHWPQARRIGVVVGSGNNGGDGYVLARHALQAGLLVQVVALPGSPPSTALAQRAAADFKSAGGTVTDFNGELAQADIWVDALFGLGFSRAPAGAALALIEALNAQQAPVLALDVPSGVDADHGCVPGVAVRAALTLQFIVAHRGLYTGDALEYTGRRQLAPLTLPDEAWQGVVAAAECWTQSRLPDLLPPRRANSHKGESGHVLCVGGNHGSGGAIAMAAEAALRTGAGLLSIGTRQDHVGPLLARLPEAMTHALEDGDALPALLAKAKVVAIGPGLGQDEWARALYARVLQSGLPLVIDADALNLLAQDAHAMTDAILTPHPGEAARLLETTTGAIQADRYGSAQALAERYHAVVVLKGAGSVVAAPGRTPRLIAAGNPGMAVGGMGDLLTGIIASLRAQGLPAFDAAAGGALLHALAGDVAAADGARGLLPTDLLAPLRRLANPESTRPPQALVELRGDLGAGKSTTARALLRALGVQGAIRSPTYTLVERYPLSSGGEAWHLDLYRIGQAGELDFLGLDEGSAVLWLVEWPERGAGALPPTDLVVALEIEGQGRRVRLTGISDAGREWLLRLPDGGDLQALSVG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPDRN010000089
EMBL· GenBank· DDBJ
KAJ9625316.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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