| http://purl.uniprot.org/citations/30952857 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30952857 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30952857 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/30952857 | http://www.w3.org/2000/01/rdf-schema#comment | "Cofactor F420 plays critical roles in primary and secondary metabolism in a range of bacteria and archaea as a low-potential hydride transfer agent. It mediates a variety of important redox transformations involved in bacterial persistence, antibiotic biosynthesis, pro-drug activation and methanogenesis. However, the biosynthetic pathway for F420 has not been fully elucidated: neither the enzyme that generates the putative intermediate 2-phospho-L-lactate, nor the function of the FMN-binding C-terminal domain of the γ-glutamyl ligase (FbiB) in bacteria are known. Here we present the structure of the guanylyltransferase FbiD and show that, along with its archaeal homolog CofC, it accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the previously uncharacterized intermediate dehydro-F420-0. The C-terminal domain of FbiB then utilizes FMNH2 to reduce dehydro-F420-0, which produces mature F420 species when combined with the γ-glutamyl ligase activity of the N-terminal domain. These new insights have allowed the heterologous production of F420 from a recombinant F420 biosynthetic pathway in Escherichia coli."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-09534-x"xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-09534-x"xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-09534-x"xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Scott C."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Scott C."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Jackson C.J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Jackson C.J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Baker E.N."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Baker E.N."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Greening C."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Greening C."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Shah M.V."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Shah M.V."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Antoney J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Antoney J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Bashiri G."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Bashiri G."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Copp J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Copp J."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Jirgis E.N.M."xsd:string |
| http://purl.uniprot.org/citations/30952857 | http://purl.uniprot.org/core/author | "Jirgis E.N.M."xsd:string |