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    <AnnotationProperty rdf:about="http://purl.obolibrary.org/obo/IAO_0000115"/>
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    <!-- http://purl.obolibrary.org/obo/ARO_0000031 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_0000031">
        <rdfs:label>antibiotic resistance gene variant or mutant</rdfs:label>
    </Class>
    


    <!-- http://purl.obolibrary.org/obo/ARO_3009562 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3009562">
        <rdfs:label>antifungal resistant ATIC enzyme</rdfs:label>
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        <oboInOwl:hasOBONamespace>antibiotic_resistance</oboInOwl:hasOBONamespace>
        <oboInOwl:id>ARO:3009562</oboInOwl:id>
        <ns3:IAO_0000115>ATIC is a bifunctional enzyme that catalyzes the final two steps of the de novo purine biosynthesis pathway in most eukaryotes. Its gene, ADE17, produces a single polypeptide chain that folds into two distinct domains. The first domain isthe 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) Transformylase domain which takes the substrate AICAR and a folate molecule to add a carbon atom. The second is the IMP Cyclohydrolase domain which takes the result of the first reaction and transforms it into a ring to create Inosine Monophosphate (IMP), which is the precursor to all DNA/RNA bases. AICAR transformylase refers to the specific functional domain of the ADE17 enzyme that is targeted or inhibited by certain chemical compounds.</ns3:IAO_0000115>
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