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    <!-- http://purl.obolibrary.org/obo/CHEBI_15377 -->

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    <!-- http://purl.obolibrary.org/obo/HINO_0003810 -->

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        <rdfs:label rdf:datatype="http://www.w3.org/2001/XMLSchema#string">FGAR + L-Glutamine + ATP + H2O =&gt; FGAM + L-Glutamate + ADP + Pi</rdfs:label>
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        <ns3:name rdf:datatype="http://www.w3.org/2001/XMLSchema#string">5&#39;-phosphoribosylformylglycinamide (FGAR) + L-glutamine + ATP + H2O  =&gt; 5&#39;-phosphoribosylformylglycinamidine (FGAM) + L-glutamate + adenosine 5&#39;-diphosphate + orthophosphate</ns3:name>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Authored: D&#39;Eustachio, P, 2004-02-13 10:19:00</rdfs:comment>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">EC Number: 6.3.5.3</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Edited: D&#39;Eustachio, P, Jassal, B, 0000-00-00 00:00:00</rdfs:comment>
        <obo:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed18388293</obo:IAO_0000119>
        <obo:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pubmed8110788</obo:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome Database ID Release 4373812</rdfs:seeAlso>
        <obo:IAO_0000119 rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reactome, http://www.reactome.org</obo:IAO_0000119>
        <rdfs:seeAlso rdf:datatype="http://www.w3.org/2001/XMLSchema#string">ReactomeREACT_1427</rdfs:seeAlso>
        <rdfs:comment rdf:datatype="http://www.w3.org/2001/XMLSchema#string">The irreversible transfer of an amino group from L-glutamine to 5&#39;-phosphoribosylformylglycinamide (FGAR), forming 5&#39;-phosphoribosylformylglycinamidine (FGAM) and glutamate, accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by phosphoribosylformylglycinamidine synthetase.  The human enzyme has been purified and characterized biochemically (Barnes et al. 1994). Fluoresence microscopy studies of cultured human cells have shown that the enzyme is cytosolic and suggest that it may co-localize with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).</rdfs:comment>
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