Archaeoglobus

Archaeoglobus

Taxobox
color = darkgray
name = "Archaeoglobus"



image_caption=The PIWI domain of an argonaute protein from A. fulgidus, bound to a short double-stranded RNA fragment and illustrating the base-pairing and aromatic stacking stabilization of the bound conformation.
domain = Archaea
phylum = Euryarchaeota
classis = Archaeoglobi
ordo = Archaeoglobales
familia = Archaeoglobaceae
genus = "Archaeoglobus"
subdivision_ranks = Species
subdivision =
* "A. fulgidus" Stetter "et al.", 1988

* "A. lithotrophicus"

* "A. profundus" Burggraf "et al.", 1990

* "A. sp. NI85-A"

* "A. sp. NS70-A"

* "A. sp. NS-tSRB-2"

* "A. sp. PM70-1"

* "A. veneficus"

* "uncultured Archaeoglobus sp."
synonyms =
* "Archaeoglobus Stetter 1988"

In taxonomy, "Archaeoglobus" is a genus of the Archaeoglobaceae. [See the NCBI [http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&id=2233 webpage on Archaeoglobus] . Data extracted from the cite web | url=ftp://ftp.ncbi.nih.gov/pub/taxonomy/ | title=NCBI taxonomy resources | publisher=National Center for Biotechnology Information | accessdate=2007-03-19]

The genus "Archaeoglobus" is a hyperthermophilic member of the Euryarchaeota. It is composed of two species, "A. fulgidus" and "A. profundus" which were isolated from hydrothermal vents. "Archaeoglobus" can also be found in high-temperature oil fields where they may contribute to oil field souring. Optimal growth of these organisms occurs at approximately 83ºC. Metabolically, "Archaeoglobus" are sulfate-reducing Archaea, coupling to the reduction of sulfate (to sulfide) to the oxidation of many different organic carbon sources, including complex polymers. "Archaeoglobus" can also live chemolithoautotrophically by coupling the oxidation of thiosulfate to the reduction of hydrogen gas. "Archaeoglobus" are the only organisms other than the traditional sulfate-reducing bacteria capable of the reduction of sulfate. Intriguingly, the completion of the complete "A. fulgidus" genome sequence (Klenk et al., 1997) revealed the presence of a nearly complete set of genes for methanogenesis. The function of these genes in "A. fulgidus" remains unknown, although the lack of the enzyme methyl-CoM reductase does not allow for methanogenesis to occur by a mechanism similar to that found in other methanogens.

References

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Further reading

cientific journals

* [http://www.nature.com/cgi-taf/DynaPage.taf?file=/nature/journal/v390/n6658/full/390364a0_fs.html&content_filetype=pdf]

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cientific books

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cientific databases

External links


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