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    <AnnotationProperty rdf:about="http://purl.obolibrary.org/obo/IAO_0000115"/>
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    <!-- http://purl.obolibrary.org/obo/ARO_2000001 -->

    <ObjectProperty rdf:about="http://purl.obolibrary.org/obo/ARO_2000001">
        <rdfs:label>confers_resistance_to_drug_class</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_2000001 -->

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        <rdfs:label>confers_resistance_to_drug_class</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_3007499 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3007499">
        <rdfs:label>triazole antifungal</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_3007500 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3007500">
        <rdfs:label>imidazole antibiotic</rdfs:label>
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    <!-- http://purl.obolibrary.org/obo/ARO_3009621 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3009621">
        <rdfs:label>azole resistant fungal 14 alpha demethylase</rdfs:label>
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        <oboInOwl:hasOBONamespace>antibiotic_resistance</oboInOwl:hasOBONamespace>
        <ns4:IAO_0000115>Lanosterol 14 alpha demethylase is involved in a critical step in the ergosterol biosynthesis pathway. It&#39;s encoded by ERG11 (Cyp51) which is a cytochrome P450 enzyme that catalyzes the oxidative removal of the 14 alpha methyl group from lanosterol. It is the primary target of azole antifungals, which bind to the heme iron in the enzyme&#39;s active site to block substrate access. This also causes the accumulation of toxic 14 alpha methylated sterol intermediates. Resistance mediated through ERG11 typically arises via point mutations in the active site that reduce azole binding affinity without abolishing catalytic activity. Additionally, upregulation of ERG11 can overwhelm the presence of azoles.</ns4:IAO_0000115>
        <oboInOwl:id>ARO:3009621</oboInOwl:id>
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    <!-- http://purl.obolibrary.org/obo/ARO_3009622 -->

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        <rdfs:label>antifungal resistant fungal 14 alpha demethylase</rdfs:label>
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