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http://purl.uniprot.org/citations/31420548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31420548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31420548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/31420548http://www.w3.org/2000/01/rdf-schema#comment"Phosphonates are rare and unusually bioactive natural products. However, most bacterial phosphonate biosynthetic capacity is dedicated to tailoring cell surfaces with molecules like 2-aminoethylphosphonate (AEP). Although phosphoenolpyruvate mutase (Ppm)-catalyzed installation of C-P bonds is known, subsequent phosphonyl tailoring (Pnt) pathway steps remain enigmatic. Here we identify nucleotidyltransferases in over two-thirds of phosphonate biosynthetic gene clusters, including direct fusions to ~60% of Ppm enzymes. We characterize two putative phosphonyl tailoring cytidylyltransferases (PntCs) that prefer AEP over phosphocholine (P-Cho) - a similar substrate used by the related enzyme LicC, which is a virulence factor in Streptococcus pneumoniae. PntC structural analyses reveal steric discrimination against phosphocholine. These findings highlight nucleotidyl activation as a predominant chemical logic in phosphonate biosynthesis and set the stage for probing diverse phosphonyl tailoring pathways."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-11627-6"xsd:string
http://purl.uniprot.org/citations/31420548http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-11627-6"xsd:string
http://purl.uniprot.org/citations/31420548http://purl.org/dc/terms/identifier"doi:10.1038/s41467-019-11627-6"xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Kelso J."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Kelso J."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Wang D."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Wang D."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Schmidt E."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Schmidt E."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Moreno-Hagelsieb G."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Moreno-Hagelsieb G."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Bartlett C."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Bartlett C."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Batul K."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Batul K."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Horsman G.P."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Horsman G.P."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Papinski M."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Papinski M."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Pratasouskaya A."xsd:string
http://purl.uniprot.org/citations/31420548http://purl.uniprot.org/core/author"Pratasouskaya A."xsd:string