</head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re12"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:15130468" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> <rdf:Description rdf:about="#re9"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa83"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa81" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_0" /><qual:input qual:qualitativeSpecies="sa82" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_1" /><qual:input qual:qualitativeSpecies="csa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa83" qual:transitionEffect="assignmentLevel" qual:id="tr_sa83_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa81</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa82</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa1</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re39"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:29622565" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa140"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa162" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa140_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa140" qual:transitionEffect="assignmentLevel" qual:id="tr_sa140_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa162</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re87"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:32531208" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa18"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa3" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_0" /><qual:input qual:qualitativeSpecies="sa17" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa18" qual:transitionEffect="assignmentLevel" qual:id="tr_sa18_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa3</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa17</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re4"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa46"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa36" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa46_in_0" /><qual:input qual:qualitativeSpecies="csa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa46_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa46" qual:transitionEffect="assignmentLevel" qual:id="tr_sa46_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math 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The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re4"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa13"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa13" qual:transitionEffect="assignmentLevel" qual:id="tr_sa13_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). 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The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re7"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa10"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa10" qual:transitionEffect="assignmentLevel" qual:id="tr_sa10_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re2"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_73577" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa30"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa31" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa30_in_0" /><qual:input qual:qualitativeSpecies="sa32" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa30_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa30" qual:transitionEffect="assignmentLevel" qual:id="tr_sa30_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa31</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa32</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re11"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:7923172" /> </rdf:Bag> </bqbiol:isDescribedBy> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:15689149" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa91"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa89" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa91_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa91" qual:transitionEffect="assignmentLevel" qual:id="tr_sa91_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa89</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms></qual:transition><qual:transition qual:id="tr_sa86"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa90" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa86_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa86" qual:transitionEffect="assignmentLevel" qual:id="tr_sa86_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa90</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms></qual:transition><qual:transition qual:id="tr_sa2"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa2" qual:transitionEffect="assignmentLevel" qual:id="tr_sa2_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. 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/></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re5"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> <bqmodel:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:doi:10.1101%2F2020.03.11.983056" /> </rdf:Bag> </bqmodel:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa23"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa6" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_0" /><qual:input qual:qualitativeSpecies="sa29" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_1" /><qual:input qual:qualitativeSpecies="sa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa23" qual:transitionEffect="assignmentLevel" qual:id="tr_sa23_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa6</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa29</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re7"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa47"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa45" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa47_in_0" /><qual:input qual:qualitativeSpecies="sa51" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa47_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa47" qual:transitionEffect="assignmentLevel" qual:id="tr_sa47_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa45</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa51</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re25"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:17827303" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa6"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa4" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_0" /><qual:input qual:qualitativeSpecies="sa21" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_1" /><qual:input qual:qualitativeSpecies="sa22" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_2" /><qual:input qual:qualitativeSpecies="sa64" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa6_in_3" /><qual:input qual:qualitativeSpecies="sa76" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa6_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa6" qual:transitionEffect="assignmentLevel" qual:id="tr_sa6_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa4</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa21</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa22</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa64</ci><cn type="integer">0</cn></apply><apply><eq /><ci>sa76</ci><cn type="integer">0</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re5"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> <bqmodel:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:doi:10.1101%2F2020.03.11.983056" /> </rdf:Bag> </bqmodel:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa26"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa23" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa26_in_0" /><qual:input qual:qualitativeSpecies="sa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa26_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa26" qual:transitionEffect="assignmentLevel" qual:id="tr_sa26_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa23</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re9"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa41"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa40" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_0" /><qual:input qual:qualitativeSpecies="sa43" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_1" /><qual:input qual:qualitativeSpecies="sa36" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_2" /><qual:input qual:qualitativeSpecies="sa42" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa41" qual:transitionEffect="assignmentLevel" qual:id="tr_sa41_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa40</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa43</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa36</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa42</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re21"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:5411547" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> <rdf:Description rdf:about="#re20"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:28458037" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa45"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa35" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa45_in_0" /><qual:input qual:qualitativeSpecies="csa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa45_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa45" qual:transitionEffect="assignmentLevel" qual:id="tr_sa45_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa35</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re24"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:24809024" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa15"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa2" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_0" /><qual:input qual:qualitativeSpecies="sa16" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa15" qual:transitionEffect="assignmentLevel" qual:id="tr_sa15_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa2</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa16</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. 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sa30 1 sa33 1 sa23 1 sa25 1

</head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re12"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:15130468" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> <rdf:Description rdf:about="#re9"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa83"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa81" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_0" /><qual:input qual:qualitativeSpecies="sa82" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_1" /><qual:input qual:qualitativeSpecies="csa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa83_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa83" qual:transitionEffect="assignmentLevel" qual:id="tr_sa83_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa81</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa82</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa1</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re39"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:29622565" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa140"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa162" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa140_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa140" qual:transitionEffect="assignmentLevel" qual:id="tr_sa140_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa162</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re87"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:32531208" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa18"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa3" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_0" /><qual:input qual:qualitativeSpecies="sa17" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa18_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa18" qual:transitionEffect="assignmentLevel" qual:id="tr_sa18_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa3</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa17</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re4"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa46"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa36" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa46_in_0" /><qual:input qual:qualitativeSpecies="csa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa46_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa46" qual:transitionEffect="assignmentLevel" qual:id="tr_sa46_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math 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carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re2"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_73577" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa4"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa3" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa4_in_0" /><qual:input qual:qualitativeSpecies="sa17" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa4_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa4_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa4" qual:transitionEffect="assignmentLevel" qual:id="tr_sa4_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa3</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa17</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re4"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa13"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa13_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa13" qual:transitionEffect="assignmentLevel" qual:id="tr_sa13_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re2"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_73577" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa52"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa47" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa52_in_0" /><qual:input qual:qualitativeSpecies="sa54" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa52_in_1" /><qual:input qual:qualitativeSpecies="sa53" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa52_in_2" /><qual:input qual:qualitativeSpecies="sa57" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa52_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa52" qual:transitionEffect="assignmentLevel" qual:id="tr_sa52_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa47</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa54</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa53</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa57</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re28"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:18837522" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> <rdf:Description rdf:about="#re77"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:doi:10.1074%2Fjbc.M114.617720" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa3"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa2" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa3_in_0" /><qual:input qual:qualitativeSpecies="sa16" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa3_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa3_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa3" qual:transitionEffect="assignmentLevel" qual:id="tr_sa3_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa2</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa16</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re3"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa34"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa31" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa34_in_0" /><qual:input qual:qualitativeSpecies="sa33" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa34_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa34" qual:transitionEffect="assignmentLevel" qual:id="tr_sa34_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math 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The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re7"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa10"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa10_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa10" qual:transitionEffect="assignmentLevel" qual:id="tr_sa10_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re2"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_73577" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa30"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa31" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa30_in_0" /><qual:input qual:qualitativeSpecies="sa32" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa30_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa30" qual:transitionEffect="assignmentLevel" qual:id="tr_sa30_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa31</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa32</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re11"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:7923172" /> </rdf:Bag> </bqbiol:isDescribedBy> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:15689149" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa91"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa89" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa91_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa91" qual:transitionEffect="assignmentLevel" qual:id="tr_sa91_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa89</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms></qual:transition><qual:transition qual:id="tr_sa86"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa90" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa86_in_0" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa86" qual:transitionEffect="assignmentLevel" qual:id="tr_sa86_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><eq /><ci>sa90</ci><cn type="integer">1</cn></apply></math></qual:functionTerm></qual:listOfFunctionTerms></qual:transition><qual:transition qual:id="tr_sa2"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa1" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_0" /><qual:input qual:qualitativeSpecies="sa7" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_1" /><qual:input qual:qualitativeSpecies="sa8" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_2" /><qual:input qual:qualitativeSpecies="sa9" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_3" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa2_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa2" qual:transitionEffect="assignmentLevel" qual:id="tr_sa2_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa1</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa7</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa8</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa9</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. 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/></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re5"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> <bqmodel:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:doi:10.1101%2F2020.03.11.983056" /> </rdf:Bag> </bqmodel:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa23"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa6" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_0" /><qual:input qual:qualitativeSpecies="sa29" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_1" /><qual:input qual:qualitativeSpecies="sa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa23_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa23" qual:transitionEffect="assignmentLevel" qual:id="tr_sa23_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa6</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa29</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). 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The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re7"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa47"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa45" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa47_in_0" /><qual:input qual:qualitativeSpecies="sa51" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa47_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa47" qual:transitionEffect="assignmentLevel" qual:id="tr_sa47_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa45</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa51</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re25"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:17827303" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa6"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa4" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_0" /><qual:input qual:qualitativeSpecies="sa21" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_1" /><qual:input qual:qualitativeSpecies="sa22" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa6_in_2" /><qual:input qual:qualitativeSpecies="sa64" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa6_in_3" /><qual:input qual:qualitativeSpecies="sa76" qual:transitionEffect="none" qual:sign="negative" qual:id="tr_sa6_in_4" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa6" qual:transitionEffect="assignmentLevel" qual:id="tr_sa6_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa4</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa21</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa22</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa64</ci><cn type="integer">0</cn></apply><apply><eq /><ci>sa76</ci><cn type="integer">0</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re5"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> <bqmodel:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:doi:10.1101%2F2020.03.11.983056" /> </rdf:Bag> </bqmodel:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa26"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa23" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa26_in_0" /><qual:input qual:qualitativeSpecies="sa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa26_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa26" qual:transitionEffect="assignmentLevel" qual:id="tr_sa26_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa23</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states, as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985). </notes> </body></html></notes><annotation><rdf:RDF><rdf:Description rdf:about="#re9"> <bqbiol:is> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:reactome:REACT_1698" /> </rdf:Bag> </bqbiol:is> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa41"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa40" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_0" /><qual:input qual:qualitativeSpecies="sa43" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_1" /><qual:input qual:qualitativeSpecies="sa36" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_2" /><qual:input qual:qualitativeSpecies="sa42" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa41_in_3" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa41" qual:transitionEffect="assignmentLevel" qual:id="tr_sa41_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><or /><apply><and /><apply><eq /><ci>sa40</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa43</ci><cn type="integer">1</cn></apply></apply><apply><and /><apply><eq /><ci>sa36</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa42</ci><cn type="integer">1</cn></apply></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re21"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:5411547" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> <rdf:Description rdf:about="#re20"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:28458037" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa45"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa35" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa45_in_0" /><qual:input qual:qualitativeSpecies="csa25" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa45_in_1" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa45" qual:transitionEffect="assignmentLevel" qual:id="tr_sa45_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa35</ci><cn type="integer">1</cn></apply><apply><eq /><ci>csa25</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><annotation><rdf:RDF><rdf:Description rdf:about="#re24"> <bqbiol:isDescribedBy> <rdf:Bag> <rdf:li rdf:resource="urn:miriam:pubmed:24809024" /> </rdf:Bag> </bqbiol:isDescribedBy> </rdf:Description> </rdf:RDF></annotation></qual:transition><qual:transition qual:id="tr_sa15"><qual:listOfInputs><qual:input qual:qualitativeSpecies="sa2" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_0" /><qual:input qual:qualitativeSpecies="sa16" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_1" /><qual:input qual:qualitativeSpecies="sa19" qual:transitionEffect="none" qual:sign="positive" qual:id="tr_sa15_in_2" /></qual:listOfInputs><qual:listOfOutputs><qual:output qual:qualitativeSpecies="sa15" qual:transitionEffect="assignmentLevel" qual:id="tr_sa15_out" /></qual:listOfOutputs><qual:listOfFunctionTerms><qual:defaultTerm qual:resultLevel="0" /><qual:functionTerm qual:resultLevel="1"><math xmlns="http://www.w3.org/1998/Math/MathML"><apply><and /><apply><eq /><ci>sa2</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa16</ci><cn type="integer">1</cn></apply><apply><eq /><ci>sa19</ci><cn type="integer">1</cn></apply></apply></math></qual:functionTerm></qual:listOfFunctionTerms><notes><html xmlns="http://www.w3.org/1999/xhtml"><head><title /></head><body>Reaction (id=reaction_glyph_7__reaction_73577, name=L-glutamine + 2 ATP + HCO3- + H2O => carbamoyl phosphate + L-glutamate + 2 ADP + orthophosphate; R-HSA-8956320_pyrimidine_biosynth-fixed.xml) <notes> The synthesis of carbamoyl phosphate from glutamine, bicarbonate, and ATP is catalyzed by the carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). 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