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The annotation and conditions in this rule are derived from the following entries: Q0VCA8 (3HAO_BOVIN), Q78JT3 (3HAO_MOUSE), Q54S02 (3HAO_DICDI), P46952 (3HAO_HUMAN), P47096 (3HAO_YEAST)

If a protein meets these conditions... i

Common conditions

    • Matches HAMAP signature MF_00825
    • taxon = Eukaryota
    • fragment ≠ the sequence is fragmented

Special conditions

    • taxon = Metazoa Subsequence at position 47 - 47 aligns to "H" in entry Q0VCA8 Subsequence at position 53 - 53 aligns to "E" in entry Q0VCA8 Subsequence at position 91 - 91 aligns to "H" in entry Q0VCA8
    • taxon = Fungi Subsequence at position 49 - 49 aligns to "H" in entry P47096 Subsequence at position 55 - 55 aligns to "E" in entry P47096 Subsequence at position 97 - 97 aligns to "H" in entry P47096
    • taxon = Metazoa Subsequence at position 47 - 47 aligns to "H" in entry Q0VCA8 Subsequence at position 53 - 53 aligns to "E" in entry Q0VCA8 Subsequence at position 91 - 91 aligns to "H" in entry Q0VCA8
    • taxon = Fungi Subsequence at position 49 - 49 aligns to "H" in entry P47096 Subsequence at position 55 - 55 aligns to "E" in entry P47096 Subsequence at position 97 - 97 aligns to "H" in entry P47096
    • taxon = Fungi Subsequence at position 126 - 126 aligns to "C" in entry P47096 Subsequence at position 129 - 129 aligns to "C" in entry P47096 Subsequence at position 163 - 163 aligns to "C" in entry P47096 Subsequence at position 166 - 166 aligns to "C" in entry P47096
  • taxon = Fungi Subsequence at position 126 - 126 aligns to "C" in entry P47096 (applies "Divalent metal cation") Subsequence at position 129 - 129 aligns to "C" in entry P47096 (applies "Divalent metal cation") Subsequence at position 163 - 163 aligns to "C" in entry P47096 (applies "Divalent metal cation") Subsequence at position 166 - 166 aligns to "C" in entry P47096 (applies "Divalent metal cation")
  • taxon = Metazoa Subsequence at position 47 - 47 aligns to "H" in entry Q0VCA8 (applies "Iron; catalytic") Subsequence at position 53 - 53 aligns to "E" in entry Q0VCA8 (applies "Iron; catalytic") Subsequence at position 91 - 91 aligns to "H" in entry Q0VCA8 (applies "Iron; catalytic")
    • taxon = Fungi
    • Subsequence at position 45 - 45 aligns to "R" in entry P47096 (individually applies "Dioxygen")
    • Subsequence at position 55 - 55 aligns to "E" in entry P47096 (individually applies "Substrate")
    • Subsequence at position 101 - 101 aligns to "R" in entry P47096 (individually applies "Substrate")
    • Subsequence at position 111 - 111 aligns to "E" in entry P47096 (individually applies "Substrate")
  • taxon = Fungi Subsequence at position 49 - 49 aligns to "H" in entry P47096 (applies "Iron; catalytic") Subsequence at position 55 - 55 aligns to "E" in entry P47096 (applies "Iron; catalytic") Subsequence at position 97 - 97 aligns to "H" in entry P47096 (applies "Iron; catalytic")
    • taxon = Metazoa
    • Subsequence at position 43 - 43 aligns to "R" in entry Q0VCA8 (individually applies "Dioxygen")
    • Subsequence at position 53 - 53 aligns to "E" in entry Q0VCA8 (individually applies "Substrate")
    • Subsequence at position 95 - 95 aligns to "R" in entry Q0VCA8 (individually applies "Substrate")
    • Subsequence at position 105 - 105 aligns to "E" in entry Q0VCA8 (individually applies "Substrate")
    • Subsequence at position 161 - 177 aligns to entry Q0VCA8 (individually applies "Linker")
    • Subsequence at position 178 - @CTER@ aligns to entry Q0VCA8 (individually applies "Domain B")
    • Subsequence at position @NTER@ - 160 aligns to entry Q0VCA8 (individually applies "Domain A (catalytic)")

... 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 namesi

  • Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenase (EC:1.13.11.6)
    Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
    Short name:
    HAD
    Biosynthesis of nicotinic acid protein 1
    3-hydroxyanthranilate oxygenase
    Short name:
    3-HAO
  • Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenase (EC:1.13.11.6)
    Alternative name(s):
    3-hydroxyanthranilic acid dioxygenase
    Short name:
    HAD
    3-hydroxyanthranilate oxygenase
    Short name:
    3-HAO

<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 namesi

  • Name:BNA1
  • Name:HAAO

<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_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: NAD(+) biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes quinolinate from L-kynurenine. This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

<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/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

  • Monomer.

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

  • Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.

<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 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 ‘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

  • Dioxygen (to residues corresponding to position 45)
  • Substrate (to residues corresponding to position 55)
  • Substrate (to residues corresponding to position 101)
  • Substrate (to residues corresponding to position 111)
  • Dioxygen (to residues corresponding to position 43)
  • Substrate (to residues corresponding to position 53)
  • Substrate (to residues corresponding to position 95)
  • Substrate (to residues corresponding to position 105)

<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

  • Divalent metal cation (to residues corresponding to position 126)
  • Divalent metal cation (to residues corresponding to position 129)
  • Divalent metal cation (to residues corresponding to position 163)
  • Divalent metal cation (to residues corresponding to position 166)
  • Iron; catalytic (to residues corresponding to position 47)
  • Iron; catalytic (to residues corresponding to position 53)
  • Iron; catalytic (to residues corresponding to position 91)
  • Iron; catalytic (to residues corresponding to position 49)
  • Iron; catalytic (to residues corresponding to position 55)
  • Iron; catalytic (to residues corresponding to position 97)

<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

  • Linker (to residues corresponding to positions 161 - 177)
  • Domain B (to residues corresponding to positions 178 - @CTER@i)
  • Domain A (catalytic) (to residues corresponding to positions @NTER@i - 160)

<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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