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The annotation and conditions in this rule are derived from the following entries: P23908 (ARGE_ECOLI)

If a protein meets these conditions... i

Common conditions

Special conditions

    • Subsequence at position 145 - 145 aligns to "E" in entry P23908 (individually applies "Cobalt or zinc 2")
    • Subsequence at position 112 - 112 aligns to "D" in entry P23908 (individually applies "Cobalt or zinc 1")
    • Subsequence at position 112 - 112 aligns to "D" in entry P23908 (individually applies "Cobalt or zinc 2")
    • Subsequence at position 82 - 82 aligns to "D" in entry P23908 (individually applies "")
    • Subsequence at position 169 - 169 aligns to "E" in entry P23908 (individually applies "Cobalt or zinc 1")
    • Subsequence at position 355 - 355 aligns to "H" in entry P23908 (individually applies "Cobalt or zinc 2")
    • Subsequence at position 80 - 80 aligns to "H" in entry P23908 (individually applies "Cobalt or zinc 1")
    • Subsequence at position 144 - 144 aligns to "E" in entry P23908 (individually applies "")

... 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:
    Acetylornithine deacetylase (EC:3.5.1.16)
    Short name:
    AO
    Short name:
    Acetylornithinase
    Alternative name(s):
    N-acetylornithinase
    Short name:
    NAO

<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:argE

<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 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 '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

  • Homodimer.

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

  • Pathwayi: L-arginine biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes L-ornithine from N(2)-acetyl-L-ornithine (linear). This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-ornithine from N(2)-acetyl-L-ornithine (linear), the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

  • (to residues corresponding to position 82)
  • (to residues corresponding to position 144)

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

  • Cobalt or zinc 2 (to residues corresponding to position 145)
  • Cobalt or zinc 1 (to residues corresponding to position 112)
  • Cobalt or zinc 2 (to residues corresponding to position 112)
  • Cobalt or zinc 1 (to residues corresponding to position 169)
  • Cobalt or zinc 2 (to residues corresponding to position 355)
  • Cobalt or zinc 1 (to residues corresponding to position 80)

<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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