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http://purl.uniprot.org/citations/18218779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18218779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18218779http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18218779http://www.w3.org/2000/01/rdf-schema#comment"Clostridium kluyveri is unique among the clostridia; it grows anaerobically on ethanol and acetate as sole energy sources. Fermentation products are butyrate, caproate, and H2. We report here the genome sequence of C. kluyveri, which revealed new insights into the metabolic capabilities of this well studied organism. A membrane-bound energy-converting NADH:ferredoxin oxidoreductase (RnfCDGEAB) and a cytoplasmic butyryl-CoA dehydrogenase complex (Bcd/EtfAB) coupling the reduction of crotonyl-CoA to butyryl-CoA with the reduction of ferredoxin represent a new energy-conserving module in anaerobes. The genes for NAD-dependent ethanol dehydrogenase and NAD(P)-dependent acetaldehyde dehydrogenase are located next to genes for microcompartment proteins, suggesting that the two enzymes, which are isolated together in a macromolecular complex, form a carboxysome-like structure. Unique for a strict anaerobe, C. kluyveri harbors three sets of genes predicted to encode for polyketide/nonribosomal peptide synthetase hybrides and one set for a nonribosomal peptide synthetase. The latter is predicted to catalyze the synthesis of a new siderophore, which is formed under iron-deficient growth conditions."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0711093105"xsd:string
http://purl.uniprot.org/citations/18218779http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0711093105"xsd:string
http://purl.uniprot.org/citations/18218779http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0711093105"xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Buckel W."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Buckel W."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Buckel W."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Brueggemann H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Brueggemann H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Brueggemann H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Gottschalk G."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Gottschalk G."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Gottschalk G."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Fricke W.F."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Fricke W.F."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Fricke W.F."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Liesegang H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Liesegang H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Liesegang H."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Li F."xsd:string
http://purl.uniprot.org/citations/18218779http://purl.uniprot.org/core/author"Li F."xsd:string