http://purl.uniprot.org/citations/31420548 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/31420548 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/31420548 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/31420548 | http://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/31420548 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-11627-6"xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-11627-6"xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-019-11627-6"xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Kelso J."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Kelso J."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Schmidt E."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Schmidt E."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Moreno-Hagelsieb G."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Moreno-Hagelsieb G."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Bartlett C."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Bartlett C."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Batul K."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Batul K."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Horsman G.P."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Horsman G.P."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Papinski M."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Papinski M."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Pratasouskaya A."xsd:string |
http://purl.uniprot.org/citations/31420548 | http://purl.uniprot.org/core/author | "Pratasouskaya A."xsd:string |