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The annotation and conditions in this rule are derived from the following entries: P0A6K1 (DAPF_ECOLI), P44859 (DAPF_HAEIN), Q8NP73 (DAPF_CORGL), P9WP19 (DAPF_MYCTU)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 74 - 75 aligns to "[GI]-N" in entry P44859 (individually applies "Substrate binding")
    • Subsequence at position 159 - 159 aligns to "H" in entry P44859 (individually applies "Could be important to modulate the pK values of the two catalytic cysteine residues")
    • Subsequence at position 157 - 157 aligns to "N" in entry P44859 (individually applies "Substrate")
    • Subsequence at position 44 - 44 aligns to "Q" in entry P44859 (individually applies "Substrate")
    • Subsequence at position 218 - 219 aligns to "G-[ST]" in entry P44859 (individually applies "Substrate binding")
    • Subsequence at position 73 - 73 aligns to "C" in entry P44859 (individually applies "Proton donor")
    • Subsequence at position 64 - 64 aligns to "[NQ]" in entry P44859 (individually applies "Substrate")
    • Subsequence at position 208 - 209 aligns to "E-R" in entry P44859 (individually applies "Substrate binding")
    • Subsequence at position 217 - 217 aligns to "C" in entry P44859 (individually applies "Proton acceptor")
    • Subsequence at position 190 - 190 aligns to "N" in entry P44859 (individually applies "Substrate")
    • Subsequence at position 11 - 11 aligns to "N" in entry P44859 (individually applies "Substrate")
    • Subsequence at position 208 - 208 aligns to "E" in entry P44859 (individually applies "Could be important to modulate the pK values of the two catalytic cysteine residues")

... 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:
    Diaminopimelate epimerase (EC:5.1.1.7)
    Short name:
    DAP epimerase
    Alternative name(s):
    PLP-independent amino acid racemase

<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:dapF

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

  • Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine.
  • Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.

<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

<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

  • 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 ‘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 74 - 75)
  • Substrate binding (to residues corresponding to positions 218 - 219)
  • Substrate binding (to residues corresponding to positions 208 - 209)

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

  • Substrate (to residues corresponding to position 157)
  • Substrate (to residues corresponding to position 44)
  • Substrate (to residues corresponding to position 64)
  • Substrate (to residues corresponding to position 190)
  • Substrate (to residues corresponding to position 11)

<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

  • Could be important to modulate the pK values of the two catalytic cysteine residues (to residues corresponding to position 159)
  • Could be important to modulate the pK values of the two catalytic cysteine residues (to residues corresponding to position 208)
  • Important for dimerization (to residues corresponding to position 268)

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 73)
  • Proton acceptor (to residues corresponding to position 217)

<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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