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http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.13.-
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.14.-.-
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2000/01/rdf-schema#comment"The enzyme, characterized from the bacterium Gordonia sp. TY-5, is a Baeyer-Villiger type monooxygenase and participates in a propane utilization pathway."xsd:string
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2004/02/skos/core#prefLabel"acetone monooxygenase (methyl acetate-forming)"xsd:string
http://purl.uniprot.org/enzyme/1.14.13.226http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17071761
http://purl.uniprot.org/enzyme/1.14.13.226http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.14.13.226#SIP514035464910AC5B
http://purl.uniprot.org/enzyme/1.14.13.226http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.14.13.-
http://purl.uniprot.org/uniprot/A1IHE6http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.14.13.226
http://purl.uniprot.org/uniprot/A1IHE6#SIPC0F5759D8999F431http://purl.uniprot.org/core/enzymeClasshttp://purl.uniprot.org/enzyme/1.14.13.226
http://purl.uniprot.org/uniprot/#_kb.A1IHE6_up.enzyme_2409AD8B99982443http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/enzyme/1.14.13.226
http://purl.uniprot.org/enzyme/1.14.13.-http://www.w3.org/2004/02/skos/core#narrowerTransitivehttp://purl.uniprot.org/enzyme/1.14.13.226