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    <!-- http://purl.obolibrary.org/obo/ARO_3009561 -->

    <Class rdf:about="http://purl.obolibrary.org/obo/ARO_3009561">
        <rdfs:label>echinocandin resistant fungal ATIC enzyme</rdfs:label>
        <rdfs:subClassOf rdf:resource="http://purl.obolibrary.org/obo/ARO_3009562"/>
        <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. The ATIC enzyme is not typically associated with echinocandin resistance in a mutational context. When a fungi experiences stress of its cell wall (like echinocandin induced stress) it responds by up regulating gene transcription to repair the wall. ADE17 is one of these genes.</ns3:IAO_0000115>
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        <rdfs:label>antifungal resistant ATIC enzyme</rdfs:label>
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