U1GHJ6 · U1GHJ6_9ACTN

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.

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 site258(6S)-NADPHX (UniProtKB | ChEBI)
Binding site308(6S)-NADPHX (UniProtKB | ChEBI)
Binding site354(6S)-NADPHX (UniProtKB | ChEBI)
Binding site447AMP (UniProtKB | ChEBI)
Binding site448(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

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      nnrD
    • ORF names
      H641_06068

Organism names

Accessions

  • Primary accession
    U1GHJ6

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-209YjeF N-terminal
Domain223-502YjeF C-terminal

Sequence similarities

Belongs to the NnrD/CARKD 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
    508
  • Mass (Da)
    51,586
  • Last updated
    2013-11-13 v1
  • Checksum
    6495CC59CA633BA1
MTQYVCTAAAMRAAEQKLFDAHPGTDLMAVAAGQVAAQARGMLADLGCGVRGGSVLVLVGGGNNGGDGLLAAAELADEGCHVRVCPVLGTPHAAGWQVALRAGCEVVTMEQAGQVVPDLVIDAVLGIGGRPGIPDDLARLGEQLSAASWLAVDLPSGLDANSGAVTTSLRADVTVTFAARKWCHVAPPAAERCGRVDVVDIGVEPGGSDGVPKCADGWTSVVDEDDLARLWPVPGPGDDKYSRGVVGMDTGSSQYPGAALLGTLGALRTGAGMVRYVGPRRPADLVLAAMPSVVLADGRVQAWVVGSGWGQDDPAANGRRLQQRCVDGVPMVIDADALSLLPAELPDGCLLTPHAGELARMLGVDRDEVRENPRESAAEAARRFGATVLLKGAIQWMADPNGHVVEPTPSEILDVADHPGAGQMPAGQAGCAAALPGPAWTGQAGSGDVLAGVCGTLLAAGVSAGWAGLLGASLQALTACRHPGPWSPDQLAGFFPEIIGACRRPSFP

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOSS01000229
EMBL· GenBank· DDBJ
ERF56339.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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