Methylacidiphilum infernorum

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Methylacidiphilum infernorum
Scientific classification
Domain:
Phylum:
Class:
Unclassified
Order:
Family:
Genus:
Species:
M. infernorum
Binomial name
Methylacidiphilum infernorum
Hou et al. 2008
Type strain
Isolate V4
Synonyms

Methylokorus infernorum Dunfield et al. 2007
Strain V4 Dunfield et al. 2007
Candidatus Methylacidiphilum infernorum Hou et al.

Methylacidiphilum infernorum is an extremely acidophilic methanotrophic aerobic bacteria first isolated and described in 2007 growing on soil and sediment on Hell's Gate, New Zealand.[1][2][3] Similar organisms have also been isolated from geothermal sites on Italy and Russia.

A

polyextremophile, these non-motile rods grows optimally at pH between 2.0 and 2.5 and temperature of 60 °C. It is a methanotrophic obligated bacteria that grows at 25% (v/v) of methane in air. It is also very dependent on carbon dioxide concentrations to grow, optimally at 8% (v/v) CO2 in air.[1]

Due to its classification in the phylum

Biology

Genome

It has a single circular chromosome of 2,287,145

base pairs. Under genome analysis it was found that M. infernorum may use a novel methylotrophic pathway because it encodes methane monooxygenase enzymes but lacks known genetic modules for methanol and formaldehyde oxidation.[1][4]

All the enzymes required for the

Calvin Benson Bassham cycle were identify by genetic analysis.[5]

Metabolism

It has been predicted that M. infernorum possess most of the key metabolic pathways for the biosynthesis of all amino acids, nucleotides and cofactors, with the sole exception of the

cobalamin cofactor.[5]

Genetic studies have shown that the enzymes it uses in several metabolic pathways differs to the ones used by other methylotrophs like for example in the biosynthesis of aromatic amino acids, lipoic acid biosynthesis, urea cycle and in the number and diversity of transporters encoded.[5]

The bacteria is able to counteract extreme acidic environments thanks to the presence of various enzymes like glutamate decarboxylase, glutamate/γ-aminobutyrate antiporter, arginine decarboxylase and an arginine/agmatine antiporter.[5]

References

External links