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1.
FIG. 1.

FIG. 1. From: The Genome Sequence of the Crenarchaeon Acidilobus saccharovorans Supports a New Order, Acidilobales, and Suggests an Important Ecological Role in Terrestrial Acidic Hot Springs .

Comparisons of proteomes of A. saccharovorans and other archaea. (A) The numbers of A. saccharovorans protein-encoding genes present in the genomes of other archaea. Genes were considered present in a pair of genomes if the region of similarity covered >70% of the corresponding protein with an E value of <1010. Abbreviations: Asac, A. saccharovorans; Aper, Aeropyrum pernix; Dkam, Desulfurococcus kamchatkensis; Hbut, Hyperthermus butylicus; Ihos, Ignicoccus hospitalis; Smar, Staphylothermus marinus; Ssol, Sulfolobus solfataricus; Sacid, Sulfolobus acidocaldarius; Stok, Sulfolobus tokodaii; Msed, Metallosphaera sedula; Cmaq, Caldivirga maquilingensis; Tpen, Thermofilum pendens; Pisl, Pyrobaculum islandicum; Tneut, Thermoproteus neutrophilus; Ptor, Picrophilus torridus; Tacid, Thermoplasma acidophilum; Pfur, Pyrococcus furiosus; Aful, Archaeoglobus fulgidus. (B) The best BLASTP hits of A. saccharovorans proteins. Significant BLASTP hits were detected for 1,218 of 1,499 proteins found in the A. saccharovorans genome. Proteins unique to A. saccharovorans were excluded from this analysis.

Andrey V. Mardanov, et al. Appl Environ Microbiol. 2010 August;76(16):5652-5657.
2.
FIG. 2.

FIG. 2. From: The Genome Sequence of the Crenarchaeon Acidilobus saccharovorans Supports a New Order, Acidilobales, and Suggests an Important Ecological Role in Terrestrial Acidic Hot Springs .

Overview of catabolic pathways encoded by the A. saccharovorans genome. Substrates utilized are in boldface, enzymes and proteins encoded by genes identified on the genome are in blue, and energy-rich intermediate compounds are in red. Panels: A, utilization of carbohydrates; B, utilization of proteins; C, glycolysis (EM and ED pathways); D, pyruvate degradation; E, pentose phosphate synthesis; F, β-oxidation of long-chain fatty acids; G, formation of proton motive force coupled with ATP generation. TCA, oxidative tricarboxylic acid cycle. Abbreviations: POR, pyruvate:ferredoxin oxidoreductase; VOR, 2-ketoisovalerate:ferredoxin oxidoreductase; IOR, indolepyruvate:ferredoxin oxidoreductase; KGOR, 2-ketoglutarate:ferredoxin oxidoreductase; ACS, acetyl-CoA synthetase; SCS, succinyl-CoA synthetase; AOR, aldehyde:ferredoxin oxidoreductases; HK, ADP-dependent hexokinase; PGI, phosphoglucose isomerase; PFK, ADP-dependent phosphofructokinase; FBA, fructose-1,6-bisphosphate aldolase; GAPOR, glyceraldehyde-3-phosphate:ferredoxin oxidoreductase; GAPN, nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase; PGM, phosphoglycerate mutase; PYK, pyruvate kinase; PPDK, pyruvate phosphate dikinase; PEP, phosphoenolpyruvate; GDH, glucose dehydrogenase; GAD, gluconate dehydratase; KDGK, 2-keto-3-deoxy-gluconate kinase; KD(P)GA, 2-keto-3-deoxy-(6-phospho)gluconate aldolase; GK, glycerate kinase; PHI, 6-phospho-3-hexuloisomerase; HPS, 3-hexulose-6-phosphate synthase; RPI, ribose-5-phosphate isomerase; PPS, phosphoribosyl pyrophosphate synthase; FOR, formaldehyde:ferredoxin oxidoreductase; Fd(ox), oxidized ferredoxin; Fd(red), reduced ferredoxin; FNOR, ferredoxin:NAD(P)+ oxidoreductase complex; NSR, NAD(P)H:elemental sulfur oxidoreductase; PPase, H+-translocating pyrophosphatase; SQOR, succinate:quinone oxidoreductase complex; SR, sulfur reductase complex; Etf, electron transfer flavoprotein; Etf-QOR, electron transfer protein-quinone oxidoreductase; CoASH, coenzyme A; FAD, flavin adenine dinucleotide; FADH2, reduced FAD.

Andrey V. Mardanov, et al. Appl Environ Microbiol. 2010 August;76(16):5652-5657.

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