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The annotation and conditions in this rule are derived from the following entries: P33160 (FDH_PSESR), O13437 (FDH_CANBO), Q08911 (FDH1_YEAST), G0SGU4 (FDH_CHATD), Q07511 (FDH_SOLTU), Q9S7E4 (FDH_ARATH)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 202 - 203 aligns to "R-I" in entry P33160 (individually applies "NAD")
    • Subsequence at position 381 - 381 aligns to "S" in entry P33160 (individually applies "NAD")
    • Subsequence at position 147 - 147 aligns to "N" in entry P33160 (individually applies "Substrate")
    • Subsequence at position 333 - 336 aligns to "H-x-S-G" in entry P33160 (individually applies "NAD")
    • Subsequence at position 148 - 148 aligns to "[ST]" in entry P33160 (individually applies "NAD")
    • Subsequence at position 148 - 334 aligns to entry P33160 (individually applies "Coenzyme-binding")
    • Subsequence at position 333 - 333 aligns to "H" in entry P33160 (individually applies "Important for catalytic activity")
    • Subsequence at position 335 - 382 aligns to entry P33160 (individually applies "Catalytic")
    • Subsequence at position 309 - 309 aligns to "D" in entry P33160 (individually applies "NAD")
    • Subsequence at position 283 - 283 aligns to "[TN]" in entry P33160 (individually applies "NAD; via carbonyl oxygen")
    • Subsequence at position 3 - 147 aligns to entry P33160 (individually applies "Catalytic")
    • Subsequence at position 285 - 285 aligns to "R" in entry P33160 (individually applies "Important for catalytic activity")
    • Subsequence at position 123 - 123 aligns to "[IV]" in entry P33160 (individually applies "Substrate; via amide nitrogen")
    • Subsequence at position 257 - 261 aligns to "P-L-[HTY]-x(2)" in entry P33160 (individually applies "NAD")
    • Subsequence at position 222 - 222 aligns to "D" in entry P33160 (individually applies "NAD")

... 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 namesi

  • Recommended name:
    Formate dehydrogenase, mitochondrial (EC:1.17.1.9)
    Short name:
    FDH
    Alternative name(s):
    NAD-dependent formate dehydrogenase
  • Recommended name:
    Formate dehydrogenase (EC:1.17.1.9)
    Short name:
    FDH
    Alternative name(s):
    NAD-dependent formate dehydrogenase

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<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 NAD+-dependent oxidation of formate to carbon dioxide. Involved in the cell stress response.
  • Catalyzes the NAD+-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.

<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

  • Homodimer.

<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 <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> 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 (to residues corresponding to position 381)
  • Substrate (to residues corresponding to position 147)
  • NAD (to residues corresponding to position 148)
  • NAD (to residues corresponding to position 309)
  • NAD; via carbonyl oxygen (to residues corresponding to position 283)
  • Substrate; via amide nitrogen (to residues corresponding to position 123)
  • NAD (to residues corresponding to position 222)

<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

  • Coenzyme-binding (to residues corresponding to positions 148 - 334)
  • Catalytic (to residues corresponding to positions 335 - 382)
  • Catalytic (to residues corresponding to positions 3 - 147)

<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

  • NAD (to residues corresponding to positions 202 - 203)
  • NAD (to residues corresponding to positions 333 - 336)
  • NAD (to residues corresponding to positions 257 - 261)

<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei

  • Important for catalytic activity (to residues corresponding to position 333)
  • Important for catalytic activity (to residues corresponding to position 285)

<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

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