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The annotation and conditions in this rule are derived from the following entries: P0A6P9 (ENO_ECOLI), Q8GR70 (ENO_ENTHR), P37869 (ENO_BACSU), Q97QS2 (ENO_STRPN)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 342 - 342 aligns to "K" in entry P0A6P9
    • Subsequence at position 290 - 290 aligns to "E" in entry P0A6P9 Subsequence at position 317 - 317 aligns to "D" in entry P0A6P9 Subsequence at position 246 - 246 aligns to "D" in entry P0A6P9
    • Subsequence at position 342 - 342 aligns to "K" in entry P0A6P9
  • Subsequence at position 290 - 290 aligns to "E" in entry P0A6P9 (applies "Magnesium") Subsequence at position 317 - 317 aligns to "D" in entry P0A6P9 (applies "Magnesium") Subsequence at position 246 - 246 aligns to "D" in entry P0A6P9 (applies "Magnesium")
    • Subsequence at position 159 - 159 aligns to "H" in entry P0A6P9 (individually applies "Substrate")
    • Subsequence at position 209 - 209 aligns to "[ED]" in entry P0A6P9 (individually applies "Proton donor")
    • Subsequence at position 342 - 342 aligns to "K" in entry P0A6P9 (individually applies "Proton acceptor")
    • Subsequence at position 369 - 372 aligns to "S-H-R-S" in entry P0A6P9 (individually applies "Substrate binding")
    • Subsequence at position 317 - 317 aligns to "D" in entry P0A6P9 (individually applies "Substrate")
    • Subsequence at position 393 - 393 aligns to "K" in entry P0A6P9 (individually applies "Substrate")
    • Subsequence at position 168 - 168 aligns to "[ED]" in entry P0A6P9 (individually applies "Substrate")
    • Subsequence at position 290 - 290 aligns to "E" in entry P0A6P9 (individually applies "Substrate")

... then these annotations are applied i

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:
    Enolase (EC:4.2.1.11)
    Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:eno

<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

    • Cytoplasm
    • Secreted
    • Cell surface
    • Note: Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

  • Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation.

<p>This section describes the function(s) of a protein.<p><a href='/help/function' target='_top'>More...</a></p>Functioni

  • Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi

  • Pathwayi: glycolysis

    This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate. This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

<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 describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

  • The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.

<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 ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei

  • Proton donor (to residues corresponding to position 209)
  • Proton acceptor (to residues corresponding to position 342)

<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi

  • Magnesium (to residues corresponding to position 290)
  • Magnesium (to residues corresponding to position 317)
  • Magnesium (to residues corresponding to position 246)

<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

  • Substrate binding (to residues corresponding to positions 369 - 372)

<p>This subsection of the ‘Function’ 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

  • Substrate (covalent); in inhibited form (to residues corresponding to position 342)
  • Substrate (to residues corresponding to position 159)
  • Substrate (to residues corresponding to position 317)
  • Substrate (to residues corresponding to position 393)
  • Substrate (to residues corresponding to position 168)
  • Substrate (to residues corresponding to position 290)

<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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