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http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.5.-.-
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.-.-.-
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/enzyme/1.5.1.-
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#subClassOfhttp://purl.uniprot.org/core/Enzyme
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#comment"Unlike EC 1.5.1.39, this enzyme does not use NADH as acceptor."xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#comment"While FMN is the preferred substrate, the enzyme can also use FAD and riboflavin with lower activity."xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#comment"The enzymes from bioluminescent bacteria contain FMN, while the enzyme from Escherichia coli does not."xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2000/01/rdf-schema#comment"The enzyme often forms a two-component system with monooxygenases such as luciferase."xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2004/02/skos/core#prefLabel"FMN reductase (NADPH)"xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8206832
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8885832
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10480865
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/1175652
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/23827
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/880288
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8990272
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9772191
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2004/02/skos/core#altLabel"flavin reductase P"xsd:string
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.5.1.29
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/replaceshttp://purl.uniprot.org/enzyme/1.6.8.1
http://purl.uniprot.org/enzyme/1.5.1.38http://purl.uniprot.org/core/activityhttp://purl.uniprot.org/enzyme/1.5.1.38#SIPAD05C3AE5B78A5AC
http://purl.uniprot.org/enzyme/1.5.1.38http://www.w3.org/2004/02/skos/core#broaderTransitivehttp://purl.uniprot.org/enzyme/1.5.1.-
http://purl.uniprot.org/uniprot/A0A2Z5C3T5http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.5.1.38
http://purl.uniprot.org/uniprot/A0AA95JZA9http://purl.uniprot.org/core/enzymehttp://purl.uniprot.org/enzyme/1.5.1.38