Pre_GI: SWBIT SVG BLASTN

Query: NC_018145:147759 Zymomonas mobilis subsp. mobilis ATCC 29191 chromosome, complete

Lineage: Zymomonas mobilis; Zymomonas; Sphingomonadaceae; Sphingomonadales; Proteobacteria; Bacteria

General Information: Isolation: Fermenting Elaeis palm sap; Temp: Mesophile. The natural habitat of this organism includes sugar-rich plant saps where the bacterium ferments sugar to ethanol. The high conversion of sugars to ethanol makes this organism useful in industrial production systems, particularly in production of bioethanol for fuel. A recombinant strain of this bacterium is utilized for the conversion of sugars, particularly xylose, which is not utilized by another common sugar-fermenting organism such as yeast, to ethanol. Since xylose is a common breakdown product of cellulose or a waste component of the agricultural industry, it is an attractive source for ethanol production. Zymomonas mobilis was chosen for this process as it is ethanol-tolerant (up to 120 grams of ethanol per litre) and productive (5-10% more ethanol than Saccharomyces). This bacterium ferments using the Enter-Doudoroff pathway, with the result that less carbon is used in cellular biomass production and more ends up as ethanol, another factor that favors this organism for ethanol production.

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BLASTN Alignment.txt

Subject: NC_008782:2062962 Acidovorax sp. JS42, complete genome

Lineage: Acidovorax; Acidovorax; Comamonadaceae; Burkholderiales; Proteobacteria; Bacteria

General Information: Acidovorax sp. JS42, formerly Pseudomonas sp. JS42, was isolated from nitrobenzene-contaminated sediment and is capable of using 2-nitrotolulene as a sole carbon and energy source. 2-nitrotolulene, a nitroaromatic compound, is used in the manufacture of dyes, pigments and explosives. Nitroaromatic compounds, which contain an aromatic ring with one or more nitro groups attached, are a significant contaminant in industrial soils. Acidovorax sp. JS42 degrades 2-nitrotolulene by first removing the nitro moiety producing 3-methylcatechol. The enzyme involved in this process, 2-nitrotolulene dioxygenase, has been purified and characterized.