Query: NC_016894:77853 Acetobacterium woodii DSM 1030 chromosome, complete genome Lineage: Acetobacterium woodii; Acetobacterium; Eubacteriaceae; Clostridiales; Firmicutes; Bacteria General Information: Acetobacterium woodii is a Gram positive, motile, strict anaerobic, acetogenic bacterium, that relies on Na+ as coupling ion in bioenergetic reactions. The organism can use a wide range of substrates, such as sugars, alcohols, methoxylated aromatic acids or C1 compounds. Electrons derived from these electron donors are used in the Wood-Ljungdahl-pathway where the organism fixes CO2 and produces acetate. The pathway of CO2-fixation is coupled to energy conservation via a chemiosmotic mechanism, one enzyme that seems to be involved is the Rnf complex. The produced Na+ gradient can be used to drive ATP-synthesis or flagella rotation. The ATP synthase is a member of the F1FO class of enzymes and has an unusual hybrid rotor. Can use alternative electron acceptors like the lignin degradation product caffeate.
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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.