, Volume 18, Issue 2, pp 295–309 | Cite as

Analysis of the complete genome of Fervidococcus fontis confirms the distinct phylogenetic position of the order Fervidicoccales and suggests its environmental function

  • Alexander V. Lebedinsky
  • Andrey V. Mardanov
  • Ilya V. Kublanov
  • Vadim M. Gumerov
  • Alexey V. Beletsky
  • Anna A. Perevalova
  • Salima Kh. Bidzhieva
  • Elizaveta A. Bonch-Osmolovskaya
  • Konstantin G. Skryabin
  • Nikolai V. Ravin
Original Paper


The complete genome of the obligately anaerobic crenarchaeote Fervidicoccus fontis Kam940T, a terrestrial hot spring inhabitant with a growth optimum of 65–70 °C, has been sequenced and analyzed. The small 1.3-Mb genome encodes several extracellular proteases and no other extracellular hydrolases. No complete pathways of carbohydrate catabolism were found. Genes coding for enzymes necessary for amino acid transamination and further oxidative decarboxylation are present. The genome encodes no mechanisms of acyl-CoA and acetyl-CoA oxidation. Two [NiFe]-hydrogenases are encoded: a membrane-bound energy-converting hydrogenase and a cytoplasmic one. The ATP-synthase is H+-dependent as inferred from the amino acid sequence of the membrane rotor subunit. On the whole, genome analysis shows F. fontis to be a peptidolytic heterotroph with a restricted biosynthetic potential, which is in accordance with its phenotypic properties. The analysis of phylogenetic markers and of the distribution of best blastp hits of F. fontis proteins in the available genomes of Crenarchaeota supports distinct phylogenetic position of the order Fervidicoccales as a separate lineage adjoining the heterogeneous order Desulfurococcales. In addition, certain F. fontis genomic features correlate with its adaptation to temperatures of 60–80 °C, which are lower than temperatures preferred by Desulfurococcales.


Fervidicoccus fontis Fervidicoccales Crenarchaeota Extreme thermophile Obligate anaerobe Complete genome 



We are grateful to Bettina Siebers and Biswarup Mukhopadhyay for helpful discussions. This work was supported by Ministry of Education and Sciences of Russia (contract 02.512.11.2201), the Russian Foundation for Basic Research (projects 11-04-01723-a and 11-04-00671-a), and by the program “Molecular and Cellular Biology” of the Russian Academy of Science within the projects of E.A.B.-O. and N.V.R. The work of I.V.K. on the analysis of hydrolases and glycosyltransferases was supported by grant #MК-7948.2010.4 from the advisory board for the research grants of the President of the Russian Federation.


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Copyright information

© Springer Japan 2013

Authors and Affiliations

  • Alexander V. Lebedinsky
    • 1
  • Andrey V. Mardanov
    • 2
  • Ilya V. Kublanov
    • 1
  • Vadim M. Gumerov
    • 2
  • Alexey V. Beletsky
    • 2
  • Anna A. Perevalova
    • 1
  • Salima Kh. Bidzhieva
    • 1
  • Elizaveta A. Bonch-Osmolovskaya
    • 1
  • Konstantin G. Skryabin
    • 2
  • Nikolai V. Ravin
    • 2
  1. 1.Winogradsky Institute of MicrobiologyRussian Academy of SciencesMoscowRussia
  2. 2.Centre “Bioengineering”Russian Academy of SciencesMoscowRussia

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