Salibacterium Nitratireducens
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Salibacterium Nitratireducens
''Salibacterium'' is a genus of Gram-positive bacteria from the family of Bacillaceae. The type species is '' Salibacterium halotolerans''. ''Salibacterium'' ''aidingense'' and ''Salibacterium salarium'' were previously species belonging to ''Bacillus'', a genus that has been recognized as displaying extensive polyphyly and has been restricted by recent phylogenetic studies to only include species closely related to ''Bacillus subtilis'' and ''Bacillus cereus.'' The name ''Salibacterium'' is derived from the prefix "-sali" (from the Latin noun ''sal/salis'', which translates to "salt"''),'' and the suffix "-bacterium" (from the Latin noun ''bacterium'', referring to a rod). Together, ''Salibacterium'' translates to a rod from salt. Biochemical Characteristics and Molecular Signatures Members of this genus are aerobic or facultatively anaerobic. Most members are non-motile, except ''S. aidingense'' which exhibits motility by means of peritrichous flagella. Some members form ...
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Bacteria
Bacteria (; : bacterium) are ubiquitous, mostly free-living organisms often consisting of one Cell (biology), biological cell. They constitute a large domain (biology), domain of Prokaryote, prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit the air, soil, water, Hot spring, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria play a vital role in many stages of the nutrient cycle by recycling nutrients and the nitrogen fixation, fixation of nitrogen from the Earth's atmosphere, atmosphere. The nutrient cycle includes the decomposition of cadaver, dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, suc ...
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Bacillus Cereus
''Bacillus cereus'' is a Gram-positive bacteria, Gram-positive Bacillus, rod-shaped bacterium commonly found in soil, food, and marine sponges. The specific name, ''cereus'', meaning "waxy" in Latin, refers to the appearance of colonies grown on blood agar. Some strains are harmful to humans and cause foodborne illness due to their spore-forming nature, while other strains can be beneficial as probiotics for animals, and even exhibit mutualism with certain plants. ''B. cereus'' bacteria may be Aerobic organism, aerobes or facultative anaerobes, and like other members of the genus ''Bacillus'', can produce protective endospores. They have a wide range of virulence factors, including phospholipase C, cereulide, Metalloproteinase, sphingomyelinase, metalloproteases, and cytotoxin K, many of which are regulated via quorum sensing. ''B. cereus'' strains exhibit Flagellum, flagellar motility. The ''Bacillus cereus'' group comprises seven closely related species: ''B. cereus' ...
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List Of Bacteria Genera
This article lists the genera of the bacteria Bacteria (; : bacterium) are ubiquitous, mostly free-living organisms often consisting of one Cell (biology), biological cell. They constitute a large domain (biology), domain of Prokaryote, prokaryotic microorganisms. Typically a few micr .... The currently accepted taxonomy is based on the List of Prokaryotic names with Standing in Nomenclature (LPSN) and National Center for Biotechnology Information (NCBI). However many taxonomic names are taken from the GTDB release 08-RS214 (28 April 2023). Phyla List Notes: List of clades needed to be added: * Actinomycetota > Actinomycetia > Actinobacteridae * Bacteroidota > Bacteroidia * Cyanobacteriota > Cyanobacteria * Pseudomonadota (Proteobacteria s.s.) > " Caulobacteria", " Pseudomonadia" See also * Branching order of bacterial phyla (Woese, 1987) * Branching order of bacterial phyla (Gupta, 2001) * Branching order of bacterial phyla (Cavalier-Smith, 2002) * B ...
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Genome Taxonomy Database
The Genome Taxonomy Database (GTDB) is an online database that maintains information on a proposed nomenclature of prokaryotes, following a phylogenomic approach based on a set of conserved single-copy proteins. In addition to resolving paraphyletic groups, this method also reassigns taxonomic ranks algorithmically, updating names in both cases. Information for archaea was added in 2020, along with a species classification based on average nucleotide identity. Each update incorporates new genomes as well as automated and manual curation of the taxonomy. An open-source tool called GTDB-Tk is available to classify draft genomes into the GTDB hierarchy. The GTDB system, via GTDB-Tk, has been used to catalogue not-yet-named bacteria in the human gut microbiome and other metagenomic sources. The GTDB is incorporated into the '' Bergey's Manual of Systematics of Archaea and Bacteria'' in 2019 as its phylogenomic resource. Methodology The genomes used to construct the phyloge ...
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The All-Species Living Tree Project
The All-Species Living Tree' Project is a collaboration between various academic groups/institutes, such as ARB, SILVA rRNA database project, and LPSN, with the aim of assembling a database of 16S rRNA sequences of all validly published species of ''Bacteria'' and ''Archaea''. At one stage, 23S sequences were also collected, but this has since stopped. Currently there are over 10,950 species in the aligned dataset and several more are being added either as new species are discovered or species that are not represented in the database are sequenced. Initially the latter group consisted of 7% of species. Similar (and more recent) projects include the Genomic Encyclopedia of Bacteria and Archaea (GEBA), which focused on whole genome sequencing of bacteria and archaea. Tree The tree was created by maximum likelihood analysis without bootstrap: consequently accuracy is traded off for size and many phylum level clades are not correctly resolved (such as the Firmicutes). (Eukaryote ...
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National Center For Biotechnology Information
The National Center for Biotechnology Information (NCBI) is part of the National Library of Medicine (NLM), a branch of the National Institutes of Health (NIH). It is approved and funded by the government of the United States. The NCBI is located in Bethesda, Maryland, and was founded in 1988 through legislation sponsored by US Congressman Claude Pepper. The NCBI houses a series of databases relevant to biotechnology and biomedicine and is an important resource for bioinformatics tools and services. Major databases include GenBank for DNA sequences and PubMed, a bibliographic database for biomedical literature. Other databases include the NCBI Epigenomics database. All these databases are available online through the Entrez search engine. NCBI was directed by David Lipman, one of the original authors of the BLAST sequence alignment program and a widely respected figure in bioinformatics. GenBank NCBI had responsibility for making available the GenBank DNA seque ...
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List Of Prokaryotic Names With Standing In Nomenclature
List of Prokaryotic names with Standing in Nomenclature (LPSN) is an online database that maintains information on the naming and taxonomy of prokaryotes, following the taxonomy requirements and rulings of the International Code of Nomenclature of Prokaryotes. The database was curated from 1997 to June 2013 by Jean P. Euzéby. From July 2013 to January 2020, LPSN was curated by Aidan C. Parte. In February 2020, a new version of LPSN was published as a service of the Leibniz Institute DSMZ, thereby also integrating the Prokaryotic Nomenclature Up-to-date service and since 2022 LPSN is interconnected with the Type (Strain) Genome Server (TYGS), DSMZ's high-throughput platform for accurate genome-based taxonomy. See also * Code of Nomenclature of Prokaryotes Described from Sequence Data References External links List of Prokaryotic names with Standing in Nomenclature
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L-arabinose Isomerase
In enzymology, a L-arabinose isomerase () is an enzyme that catalyzes the chemical reaction :L-arabinose \rightleftharpoons L-ribulose Hence, this enzyme has one substrate, L-arabinose, and one product, L-ribulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The systematic name of this enzyme class is L-arabinose aldose-ketose-isomerase. This enzyme participates in pentose and glucuronate interconversions. This enzyme catalyses the conversion of L-arabinose to L-ribulose as the first step in the pathway of L-arabinose utilization as a carbon source. Industrial applications In 1993, scientists discovered that L-arabinose isomerase from the bacterium ''Lactobacillus gayonii'' can convert D-Galactose to D-Tagatose. Tagatose is a biologically rare sugar that has been explored as an alternative sweetening agent in foods due to its low glycemic index. L-arabinose isomerase has been expl ...
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Exonuclease
Exonucleases are enzymes that work by cleaving nucleotides one at a time from the end (exo) of a polynucleotide chain. A hydrolyzing reaction that breaks phosphodiester bonds at either the 3′ or the 5′ end occurs. Its close relative is the endonuclease, which cleaves phosphodiester bonds in the middle (endo) of a polynucleotide chain. Eukaryotes and prokaryotes have three types of exonucleases involved in the normal turnover of mRNA: 5′ to 3′ exonuclease (Xrn1), which is a dependent decapping protein; 3′ to 5′ exonuclease, an independent protein; and poly(A)-specific 3′ to 5′ exonuclease. In both archaea and eukaryotes, one of the main routes of RNA degradation is performed by the multi-protein exosome complex, which consists largely of 3′ to 5′ exoribonucleases. Significance to polymerase RNA polymerase II is known to be in effect during transcriptional termination; it works with a 5' exonuclease (human gene Xrn2) to degrade the newly formed transcr ...
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Dihydrolipoamide Dehydrogenase
Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the ''DLD'' gene. DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide. Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial enzyme that plays a vital role in energy metabolism in eukaryotes. This enzyme is required for the complete reaction of at least five different multi-enzyme complexes. Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are directly involved in catalysis. The enzyme associates into tightly bound homodimers required for its enzymatic activity. File:Lipoamide-2D-skeletal.png, Lipoamide File:Dihydrolipoamide.svg, Dihydrolipoamide Structure The protein encoded by the DLD gene comes together with another protein to form a dimer in the central metabolic pathway. Several amino acids within the catalytic pocket have been identified ...
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