Pre_GI: SWBIT SVG BLASTP

Query: NC_020134:2295092 Clostridium stercorarium subsp. stercorarium DSM 8532, complete

Lineage: Clostridium stercorarium; Clostridium; unclassified Ruminococcaceae; Clostridiales; Firmicutes; Bacteria

General Information: Lignocellulosic biomass has great potential as an abundant and renewable source of fermentable sugars through enzymic saccharification. Clostridium stercorarium is a catabolically versatile bacterium producing a wide range of hydrolases for degradation of biomass. Together with Clostridium thermocellum, Clostridium aldrichii and other cellulose degraders, it forms group I of the clostridia. It is moderately thermophilic, with an optimum growth temperature of 65 degrees C, and has repeatedly been isolated from self-heated compost. The two-component cellulase system of C. stercorarium has been investigated thoroughly. Due to its ability to utilize the various polysaccharides present in biomass it is especially suited for the fermentation of hemicellulose to organic solvents. Some isolates have been used in Japan in a single-step ethanol-fermenting pilot-process with lignocellulosic biomass as substrate.

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BLASTP Alignment.txt

Subject: NC_006624:2016000 Thermococcus kodakarensis KOD1, complete genome

Lineage: Thermococcus kodakarensis; Thermococcus; Thermococcaceae; Thermococcales; Euryarchaeota; Archaea

General Information: This organism was originally identified as Pyrococcus sp. strain KOD1. It was isolated from a solfatara on Kodakara Island, Japan. Hyperthermophilic archeon. This genus is a member of the order Thermococcales in the Euryarchaeota. Thermococcus sp. are the most commonly isolated hyperthermophilic organisms and are often isolated from marine hydrothermal vents and terrestrial hot sulfur springs. Elemental sulfur is either required for, or stimulates, growth. These obligate heterotrophs can ferment a variety of organic compounds, including peptides, amino acids, and sugars in the absence of sulfur. Thermococcus kodakaraensis is a hyperthermophilic archeon. Proteins from this organism have been extensively studied to find thermostable enzymes for industrial and biotechnological applications.