ArticlePLoS computational biology2023
Knowledge-guided data mining on the standardized architecture of NRPS: Subtypes, novel motifs, and sequence entanglements.
Article in PLoS computational biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Genome-Guided Discovery of an Antimicrobial Peptide Scaffold from an Undescribed AntarcticInternational journal of molecular sciences · 2026Article
- Bacterial Siderophore Production in Metal-Rich Environments: Underexplored Sources of Siderophores and Insights into Bioremediation.Journal of natural products · 2026Review
- Revealing Microbial Siderophores: From Genes to Applications.Microorganisms · 2026Review
- Multiple active-sites editing of adenylation domains of srfA operon for constructing diverse surfactin lipopeptide.Communications biology · 2026Article
- Discovery of Fusadapamides, Accessory Chromosome-Associated Metabolites Incorporating l-2,3-Diaminopropionic Acid inJournal of natural products · 2025Article
- Thiotemplated Polyketide Chain Fusion and Reductive Cyclization Build the Reactive Butenolide Core of Malleicyprol.Angewandte Chemie (International ed. in English) · 2025Article
- Forging the iron-net: Towards a quantitative understanding of microbial communities via siderophore-mediated interactions.Quantitative biology (Beijing, China) · 2025Article
- Siderophore synthetase-receptor gene coevolution reveals habitat- and pathogen-specific bacterial iron interaction networks.Science advances · 2025Article
- Feature sequence-based genome mining uncovers the hidden diversity of bacterial siderophore pathways.eLife · 2024Article
- Natural diversifying evolution of nonribosomal peptide synthetases in a defensive symbiont reveals nonmodular functional constraints.PNAS nexus · 2024Article
- SIDERITE: Unveiling hidden siderophore diversity in the chemical space through digital exploration.iMeta · 2024Article
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Authors and funding
8 authors.
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Abstract
Non-ribosomal peptide synthetase (NRPS) is a diverse family of biosynthetic enzymes for the assembly of bioactive peptides. Despite advances in microbial sequencing, the lack of a consistent standard for annotating NRPS domains and modules has made data-driven discoveries challenging. To address this, we introduced a standardized architecture for NRPS, by using known conserved motifs to partition typical domains. This motif-and-intermotif standardization allowed for systematic evaluations of sequence properties from a large number of NRPS pathways, resulting in the most comprehensive cross-kingdom C domain subtype classifications to date, as well as the discovery and experimental validation of novel conserved motifs with functional significance. Furthermore, our coevolution analysis revealed important barriers associated with re-engineering NRPSs and uncovered the entanglement between phylogeny and substrate specificity in NRPS sequences. Our findings provide a comprehensive and statistically insightful analysis of NRPS sequences, opening avenues for future data-driven discoveries.
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