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The annotation and conditions in this rule are derived from the following entries: P94368 (NNRD_BACSU), P31806 (NNR_ECOLI), Q9X024 (NNR_THEMA)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_01965
    • taxon = Bacteria
    • fragment ≠ the sequence is fragmented
    • Matches HAMAP signature MF_01965
    • taxon = Archaea
    • fragment ≠ the sequence is fragmented

Special conditions

    • Subsequence at position 216 - 216 aligns to "D" in entry P94368 (individually applies "NAD(P)HX")
    • Subsequence at position 149 - 155 aligns to "x(3)-E-x(3)" in entry P94368 (individually applies "NAD(P)HX")
    • Subsequence at position 186 - 190 aligns to "K-x(4)" in entry P94368 (individually applies "ADP")
    • Subsequence at position 104 - 104 aligns to entry P94368 (individually applies "NAD(P)HX; via amide nitrogen")
    • Subsequence at position 206 - 215 aligns to "x(7)-G-x-G" in entry P94368 (individually applies "ADP")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namei

  • Recommended name:
    ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC:4.2.1.136)
    Alternative name(s):
    ADP-dependent NAD(P)HX dehydratase

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namei

  • Name:nnrD

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Homotetramer.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • 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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei

  • NAD(P)HX (to residues corresponding to position 216)
  • NAD(P)HX; via amide nitrogen (to residues corresponding to position 104)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi

  • ADP (to residues corresponding to positions 186 - 190)
  • ADP (to residues corresponding to positions 206 - 215)

<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni

  • NAD(P)HX (to residues corresponding to positions 149 - 155)

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO (Gene Ontology) termsi

  • GO:0046496 nicotinamide nucleotide metabolic process
  • GO:0052855 ADP-dependent NAD(P)H-hydrate dehydratase activity
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