Query: NC_004757:427483 Nitrosomonas europaea ATCC 19718, complete genome
Lineage: Nitrosomonas europaea; Nitrosomonas; Nitrosomonadaceae; Nitrosomonadales; Proteobacteria; Bacteria
General Information: Ammonia-oxidizing bacterium. This organism is an obligate chemo-lithoautotroph as it only uses ammonia and carbon dioxide and mineral salts for growth, and is an important part of the global biogeochemical nitrogen cycle. It can derive all energy requirements from the oxidation of ammonia to nitrate, driving global nitrogen from the reduced insoluble form to the oxidized and potentially gaseous form (including NO and NO2 which are greenhouse gases). The energy derived from ammonia oxidation is in turn used to drive carbon fixation. This bacterium also provides plants with a readily available form of nitrogen, is important in wastewater treatment, and may be involved in bioremediation of sites contaminated with toxic compounds.
Subject: NC_011898:2907017 Clostridium cellulolyticum H10, complete genome
Lineage: Clostridium cellulolyticum; Clostridium; Clostridiaceae; Clostridiales; Firmicutes; Bacteria
General Information: A non-ruminal mesophilic cellulolytic bacterium originally isolated from decayed grass compost. This genus comprises about 150 metabolically diverse species of anaerobes that are ubiquitous in virtually all anoxic habitats where organic compounds are present, including soils, aquatic sediments and the intestinal tracts of animals and humans. This shape is attributed to the presence of endospores that develop under conditions unfavorable for vegetative growth and distend single cells terminally or sub-terminally. Spores germinate under conditions favorable for vegetative growth, such as anaerobiosis and presence of organic substrates. It is believed that present day Mollicutes (Eubacteria) have evolved regressively (i.e., by genome reduction) from gram-positive clostridia-like ancestors with a low GC content in DNA. Clostridium cellulolyticum is a mesophilic cellulolytic bacterium. Cellulose-degradation by C. cellulolyticum has been extensively studied. The cellulolytic enzymes of this organism are bound to a protein scaffold in an extracellular multienzyme complex called a cellulosome.