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http://purl.uniprot.org/citations/31469543http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31469543http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31469543http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/31469543http://www.w3.org/2000/01/rdf-schema#comment"Coenzyme F420 is a specialized redox cofactor with a negative redox potential. It supports biochemical processes like methanogenesis, degradation of xenobiotics, and the biosynthesis of antibiotics. Although well-studied in methanogenic archaea and actinobacteria, not much is known about F420 in Gram-negative bacteria. Genome sequencing revealed F420 biosynthetic genes in the Gram-negative, endofungal bacterium Paraburkholderia rhizoxinica, a symbiont of phytopathogenic fungi. Fluorescence microscopy, high-resolution LC-MS, and structure elucidation by NMR demonstrated that the encoded pathway is active and yields unexpected derivatives of F420 (3PG-F420). Further analyses of a biogas-producing microbial community showed that these derivatives are more widespread in nature. Genetic and biochemical studies of their biosynthesis established that a specificity switch in the guanylyltransferase CofC reprogrammed the pathway to start from 3-phospho-d-glycerate, suggesting a rerouting event during the evolution of F420 biosynthesis. Furthermore, the cofactor activity of 3PG-F420 was validated, thus opening up perspectives for its use in biocatalysis. The 3PG-F420 biosynthetic gene cluster is fully functional in Escherichia coli, enabling convenient production of the cofactor by fermentation."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.org/dc/terms/identifier"doi:10.1021/acschembio.9b00605"xsd:string
http://purl.uniprot.org/citations/31469543http://purl.org/dc/terms/identifier"doi:10.1021/acschembio.9b00605"xsd:string
http://purl.uniprot.org/citations/31469543http://purl.org/dc/terms/identifier"doi:10.1021/acschembio.9b00605"xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Guo H."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Guo H."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Hertweck C."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Hertweck C."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Beemelmanns C."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Beemelmanns C."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Braga D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Braga D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Hasan M."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Hasan M."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Lackner G."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Lackner G."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Last D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Last D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Leichnitz D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Leichnitz D."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Richter I."xsd:string
http://purl.uniprot.org/citations/31469543http://purl.uniprot.org/core/author"Richter I."xsd:string