A species of extremely thermophilic, sulfur-reducing archaea. It grows at a maximum temperature of 95 degrees C. in marine or deep-sea geothermal areas.
A genus of extremely thermophilic, sulfate-reducing archaea, in the family Archaeoglobaceae.
Proteins found in any species of archaeon.
An order of extremely thermophilic, sulfate-reducing archaea, in the kingdom EURYARCHAEOTA. The single family Archaeoglobaceae contains one genus ARCHAEOGLOBUS.
Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in archaea.
Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)
A genus of anaerobic coccoid METHANOCOCCACEAE whose organisms are motile by means of polar tufts of flagella. These methanogens are found in salt marshes, marine and estuarine sediments, and the intestinal tract of animals.
Deoxyribonucleic acid that makes up the genetic material of archaea.
An enzyme found primarily in SULFUR-REDUCING BACTERIA where it plays an important role in the anaerobic carbon oxidation pathway.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The functional genetic units of ARCHAEA.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.

Identification of the Archaeoglobus fulgidus endonuclease III DNA interaction surface using heteronuclear NMR methods. (1/193)

BACKGROUND: Endonuclease III is the prototype for a family of DNA-repair enzymes that recognize and remove damaged and mismatched bases from DNA via cleavage of the N-glycosidic bond. Crystal structures for endonuclease III, which removes damaged pyrimidines, and MutY, which removes mismatched adenines, show a highly conserved structure. Although there are several models for DNA binding by this family of enzymes, no experimental structures with bound DNA exist for any member of the family. RESULTS: Nuclear magnetic resonance (NMR) spectroscopy chemical-shift perturbation of backbone nuclei (1H, 15N, 13CO) has been used to map the DNA-binding site on Archaeoglobus fulgidus endonuclease III. The experimentally determined interaction surface includes five structural elements: the helix-hairpin-helix (HhH) motif, the iron-sulfur cluster loop (FCL) motif, the pseudo helix-hairpin-helix motif, the helix B-helix C loop, and helix H. The elements form a continuous surface that spans the active site of the enzyme. CONCLUSIONS: The enzyme-DNA interaction surface for endonuclease III contains five elements of the protein structure and suggests that DNA damage recognition may require several specific interactions between the enzyme and the DNA substrate. Because the target DNA used in this study contained a generic apurinic/apyrimidinic (AP) site, the binding interactions we observed for A. fulgidus endonuclease III should apply to all members of the endonuclease III family and several interactions could apply to the endonuclease III/AlkA (3-methyladenine DNA glycosylase) superfamily.  (+info)

Identification and characterization of a novel ferric reductase from the hyperthermophilic Archaeon Archaeoglobus fulgidus. (2/193)

Archaeoglobus fulgidus, a hyperthermophilic sulfate-reducing Archaeon, contains high Fe(3+)-EDTA reductase activity in its soluble protein fraction. The corresponding enzyme, which constitutes about 0.75% of the soluble protein, was purified 175-fold to homogeneity. Based on SDS-polyacrylamide gel electrophoresis, the ferric reductase consists of a single subunit with a M(r) of 18,000. The M(r) of the native enzyme was determined by size exclusion chromatography to be 40,000 suggesting that the native ferric reductase is a homodimer. The enzyme uses both NADH and NADPH as electron donors to reduce Fe(3+)-EDTA. Other Fe(3+) complexes and dichlorophenolindophenol serve as alternative electron acceptors, but uncomplexed Fe(3+) is not utilized. The purified enzyme strictly requires FMN or FAD as a catalytic intermediate for Fe(3+) reduction. Ferric reductase also reduces FMN and FAD, but not riboflavin, with NAD(P)H which classifies the enzyme as a NAD(P)H:flavin oxidoreductase. The enzyme exhibits a temperature optimum of 88 degrees C. When incubated at 85 degrees C, the enzyme activity half-life was 2 h. N-terminal sequence analysis of the purified ferric reductase resulted in the identification of the hypothetical gene, AF0830, of the A. fulgidus genomic sequence. The A. fulgidus ferric reductase shares amino acid sequence similarity with a family of NAD(P)H:FMN oxidoreductases but not with any ferric reductases suggesting that the A. fulgidus ferric reductase is a novel enzyme.  (+info)

The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn(2+) flavoprotein. (3/193)

Archaeoglobus fulgidus, a hyperthermophilic, archaeal sulfate reducer, is one of the few organisms that can utilize D-lactate as a sole source for both carbon and electrons. The A. fulgidus open reading frame, AF0394, which is predicted to encode a D-(-)-lactate dehydrogenase (Dld), was cloned, and its product was expressed in Escherichia coli as a fusion with the maltose binding protein (MBP). The 90-kDa MBP-Dld fusion protein was more efficiently expressed in E. coli when coexpressed with the E. coli dnaY gene, encoding the arginyl tRNA for the codons AGA and AGG. When cleaved from the fusion protein by treatment with factor Xa, the recombinant Dld (rDld) has an apparent molecular mass of 50 kDa, similar to that of the native A. fulgidus Dld enzyme. Both the purified MBP-Dld fusion protein and its rDld cleavage fragment have lactate dehydrogenase activities specific for D-lactate, are stable at 80 degrees C, and retain activity after exposure to oxygen. The flavin cofactor FAD, which binds rDld apoprotein with a 1:1 stoichiometry, is essential for activity.  (+info)

Cellulosome-like sequences in Archaeoglobus fulgidus: an enigmatic vestige of cohesin and dockerin domains. (4/193)

The distribution of cellulosomal cohesin domains among the sequences currently compiled in various sequence databases was investigated. Two cohesin domains were detected in two consecutive open reading frames (ORFs) of the recently sequenced genome of the archaeon Archaeoglobus fulgidus. Otherwise, no cohesin-like sequence could be detected in organisms other than those of the Eubacteria. One of the A. fulgidus cohesin-containing ORFs also harbored a dockerin domain, but the additional modular portions of both genes are undefined, both with respect to sequence homology and function. It is currently unclear what function(s) the putative cohesin and dockerin-containing proteins play in the life cycle of this organism. In particular, since A. fulgidus contains no known glycosyl hydrolase gene, the presence of a cellulosome can be excluded. The results suggest that cohesin and dockerin signature sequences cannot be used alone for the definitive identification of cellulosomes in genomes.  (+info)

Assembly of archaeal signal recognition particle from recombinant components. (5/193)

Signal recognition particle (SRP) takes part in protein targeting and secretion in all organisms. Searches for components of archaeal SRP in primary databases and completed genomes indicated that archaea possess only homologs of SRP RNA, and proteins SRP19 and SRP54. A recombinant SRP was assembled from cloned, expressed and purified components of the hyperthermophilic archaeon Archaeoglobus fulgidus. Recombinant Af-SRP54 associated with the signal peptide of bovine pre-prolactin translated in vitro. As in mammalian SRP, Af-SRP54 binding to Af-SRP RNA required protein Af-SRP19, although notable amounts bound in absence of Af-SRP19. Archaeoglobus fulgidus SRP proteins also bound to full-length SRP RNA of the archaeon Methanococcus jannaschii, to eukaryotic human SRP RNA, and to truncated versions which corresponded to the large domain of SRP. Dependence on SRP19 was most pronounced with components from the same species. Reconstitutions with heterologous components revealed a significant potential of human SRP proteins to bind to archaeal SRP RNAs. Surprisingly, M.jannaschii SRP RNA bound to human SRP54M quantitatively in the absence of SRP19. This is the first report of reconstitution of an archaeal SRP from recombinantly expressed purified components. The results highlight structural and functional conservation of SRP assembly between archaea and eucarya.  (+info)

Homology modeling and identification of serine 160 as nucleophile of the active site in a thermostable carboxylesterase from the archaeon Archaeoglobus fulgidus. (6/193)

The hyperthermophilic Archaeon Archaeoglobus fulgidus has a gene (AF1763) which encodes a thermostable carboxylesterase belonging to the hormone-sensitive lipase (HSL)-like group of the esterase/lipase family. Based on secondary structure predictions and a secondary structure-driven multiple sequence alignment with remote homologous proteins of known three-dimensional structure, we previously hypothesized for this enzyme the alpha/beta-hydrolase fold typical of several lipases and esterases and identified Ser160, Asp 255 and His285 as the putative members of the catalytic triad. In this paper we report the building of a 3D model for this enzyme based on the structure of the homologous brefeldin A esterase from Bacillus subtilis whose structure has been recently elucidated. The model reveals the topological organization of the fold corroborating our predictions. As regarding the active-site residues, Ser160, Asp255 and His285 are located close each other at hydrogen bond distances. The catalytic role of Ser160 as the nucleophilic member of the triad is demonstrated by the [(3)H]diisopropylphosphofluoridate (DFP) active-site labeling and sequencing of a radioactive peptide containing the signature sequence GDSAGG.  (+info)

Uracil-DNA glycosylase in the extreme thermophile Archaeoglobus fulgidus. (7/193)

Uracil-DNA glycosylase (UDG) is an essential enzyme for maintaining genomic integrity. Here we describe a UDG from the extreme thermophile Archaeoglobus fulgidus. The enzyme is a member of a new class of enzymes found in prokaryotes that is distinct from the UDG enzyme found in Escherichia coli, eukaryotes, and DNA-containing viruses. The A. fulgidus UDG is extremely thermostable, maintaining full activity after heating for 1.5 h at 95 degrees C. The protein is capable of removing uracil from double-stranded DNA containing either a U/A or U/G base pair as well as from single-stranded DNA. This enzyme is product-inhibited by both uracil and apurinic/apyrimidinic sites. The A. fulgidus UDG has a high degree of similarity at the primary amino acid sequence level to the enzyme found in Thermotoga maritima, a thermophilic eubacteria, and suggests a conserved mechanism of UDG-initiated base excision repair in archaea and thermophilic eubacteria.  (+info)

The Archean sulfur cycle and the early history of atmospheric oxygen. (8/193)

The isotope record of sedimentary sulfides can help resolve the history of oxygen accumulation into the atmosphere. We measured sulfur isotopic fractionation during microbial sulfate reduction up to 88 degrees C and show how sulfate reduction rate influences the preservation of biological fractionations in sediments. The sedimentary sulfur isotope record suggests low concentrations of seawater sulfate and atmospheric oxygen in the early Archean (3.4 to 2.8 billion years ago). The accumulation of oxygen and sulfate began later, in the early Proterozoic (2.5 to 0.54 billion years ago).  (+info)

'Archaeoglobus fulgidus' is a species of archaea, which are single-celled microorganisms that share some characteristics with bacteria but are genetically and biochemically distinct. This particular species is extremophilic, meaning it thrives in extreme environments that are hostile to most other life forms.

'Archaeoglobus fulgidus' is found in deep-sea hydrothermal vents and oil reservoirs, where it exists under high temperatures (up to 92°C) and high pressures. It is a sulfate-reducing organism, which means it obtains energy by reducing sulfates to hydrogen sulfide, using organic compounds as electron donors. This process plays a significant role in the global sulfur cycle and the anaerobic degradation of organic matter in extreme environments.

The study of 'Archaeoglobus fulgidus' and other archaea has provided valuable insights into the evolution and diversity of life on Earth, as well as the biochemical adaptations that allow organisms to survive under extreme conditions.

'Archaeoglobus' is a genus of archaea, which are single-celled microorganisms that lack cell nuclei and are distinct from bacteria and eukaryotes. Archaeoglobus species are extremophiles, meaning they thrive in extreme environments that are hostile to most other forms of life.

Archaeoglobus species are found in deep-sea hydrothermal vents, where they obtain energy by oxidizing sulfur compounds and reducing sulfate to produce hydrogen sulfide. They are also found in hot oil reservoirs, where they can degrade crude oil and contribute to the souring of oil wells.

Archaeoglobus species have a unique metabolism that is distinct from other archaea and bacteria. They possess a variety of enzymes that allow them to thrive in extreme environments, including high temperatures, pressures, and acidity. These adaptations make Archaeoglobus species important models for studying the evolution and ecology of extremophilic microorganisms.

Archaeal proteins are proteins that are encoded by the genes found in archaea, a domain of single-celled microorganisms. These proteins are crucial for various cellular functions and structures in archaea, which are adapted to survive in extreme environments such as high temperatures, high salt concentrations, and low pH levels.

Archaeal proteins share similarities with both bacterial and eukaryotic proteins, but they also have unique features that distinguish them from each other. For example, many archaeal proteins contain unusual amino acids or modifications that are not commonly found in other organisms. Additionally, the three-dimensional structures of some archaeal proteins are distinct from their bacterial and eukaryotic counterparts.

Studying archaeal proteins is important for understanding the biology of these unique organisms and for gaining insights into the evolution of life on Earth. Furthermore, because some archaea can survive in extreme environments, their proteins may have properties that make them useful in industrial and medical applications.

Archaeoglobales is an order of archaea, a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. Archaea are extremophiles, meaning they can survive in harsh environments that are hostile to most other life forms.

Archaeoglobales are unique because they are thermophilic, which means they thrive in high-temperature environments, typically between 65 and 95°C (149-203°F). They are also sulfate-reducing organisms, which means they obtain energy by reducing sulfate to hydrogen sulfide, using organic compounds as electron donors.

These archaea have been found in various environments, including deep-sea hydrothermal vents, hot springs, and oil reservoirs. They play an essential role in the global carbon and sulfur cycles and have potential applications in bioremediation and bioenergy production.

Archaeal RNA refers to the Ribonucleic acid (RNA) molecules that are present in archaea, which are a domain of single-celled microorganisms. RNA is a nucleic acid that plays a crucial role in various biological processes, such as protein synthesis, gene expression, and regulation of cellular activities.

Archaeal RNAs can be categorized into different types based on their functions, including:

1. Messenger RNA (mRNA): It carries genetic information from DNA to the ribosome, where it is translated into proteins.
2. Transfer RNA (tRNA): It helps in translating the genetic code present in mRNA into specific amino acids during protein synthesis.
3. Ribosomal RNA (rRNA): It is a structural and functional component of ribosomes, where protein synthesis occurs.
4. Non-coding RNA: These are RNAs that do not code for proteins but have regulatory functions in gene expression and other cellular processes.

Archaeal RNAs share similarities with both bacterial and eukaryotic RNAs, but they also possess unique features that distinguish them from the other two domains of life. For example, archaeal rRNAs contain unique sequence motifs and secondary structures that are not found in bacteria or eukaryotes. These differences suggest that archaeal RNAs have evolved to adapt to the extreme environments where many archaea live.

Overall, understanding the structure, function, and evolution of archaeal RNA is essential for gaining insights into the biology of these unique microorganisms and their roles in various cellular processes.

Gene expression regulation in archaea refers to the complex cellular processes that control the transcription and translation of genes into functional proteins. This regulation is crucial for the survival and adaptation of archaea to various environmental conditions.

Archaea, like bacteria and eukaryotes, use a variety of mechanisms to regulate gene expression, including:

1. Transcriptional regulation: This involves controlling the initiation, elongation, and termination of transcription by RNA polymerase. Archaea have a unique transcription machinery that is more similar to eukaryotic RNA polymerases than bacterial ones. Transcriptional regulators, such as activators and repressors, bind to specific DNA sequences near the promoter region to modulate transcription.
2. Post-transcriptional regulation: This includes processes like RNA processing, modification, and degradation that affect mRNA stability and translation efficiency. Archaea have a variety of RNA-binding proteins and small non-coding RNAs (sRNAs) that play crucial roles in post-transcriptional regulation.
3. Translational regulation: This involves controlling the initiation, elongation, and termination of translation by ribosomes. Archaea use a unique set of translation initiation factors and tRNA modifications to regulate protein synthesis.
4. Post-translational regulation: This includes processes like protein folding, modification, and degradation that affect protein stability and function. Archaea have various chaperones, proteases, and modifying enzymes that participate in post-translational regulation.

Overall, gene expression regulation in archaea is a highly dynamic and coordinated process involving multiple layers of control to ensure proper gene expression under changing environmental conditions.

Non-heme iron proteins are a type of iron-containing protein that do not contain heme as their prosthetic group. Heme is a complex molecule consisting of an iron atom contained in the center of a porphyrin ring, which is a large organic molecule made up of four pyrrole rings joined together. In contrast, non-heme iron proteins contain iron that is bound to the protein in other ways, such as through coordination with amino acid side chains or through association with an iron-sulfur cluster.

Examples of non-heme iron proteins include ferritin and transferrin, which are involved in the storage and transport of iron in the body, respectively. Ferritin is a protein that stores iron in a form that is safe and bioavailable for use by the body. Transferrin, on the other hand, binds to iron in the intestines and transports it to cells throughout the body.

Non-heme iron proteins are important for many biological processes, including oxygen transport, electron transfer, and enzyme catalysis. They play a crucial role in energy metabolism, DNA synthesis, and other essential functions.

"Methanococcus" is a genus of archaea, which are single-celled microorganisms that share some characteristics with bacteria but are actually more closely related to eukaryotes. "Methanococcus" species are obligate anaerobes, meaning they can only survive in environments without oxygen. They are also methanogens, which means they produce methane as a byproduct of their metabolism. These microorganisms are commonly found in aquatic environments such as marine sediments and freshwater swamps, where they play an important role in the carbon cycle by breaking down organic matter and producing methane. Some "Methanococcus" species can also be found in the digestive tracts of animals, including humans, where they help to break down food waste and produce methane as a byproduct.

Archaeal DNA refers to the genetic material present in archaea, a domain of single-celled microorganisms lacking a nucleus. Like bacteria, archaea have a single circular chromosome that contains their genetic information. However, archaeal DNA is significantly different from bacterial and eukaryotic DNA in terms of its structure and composition.

Archaeal DNA is characterized by the presence of unique modifications such as methylation patterns, which help distinguish it from other types of DNA. Additionally, archaea have a distinct set of genes involved in DNA replication, repair, and recombination, many of which are more similar to those found in eukaryotes than bacteria.

One notable feature of archaeal DNA is its resistance to environmental stressors such as extreme temperatures, pH levels, and salt concentrations. This allows archaea to thrive in some of the most inhospitable environments on Earth, including hydrothermal vents, acidic hot springs, and highly saline lakes.

Overall, the study of archaeal DNA has provided valuable insights into the evolutionary history of life on Earth and the unique adaptations that allow these organisms to survive in extreme conditions.

Hydrogensulfite reductase is an enzyme found in certain bacteria and archaea that catalyzes the reduction of hydrogen sulfite (bisulfite) to sulfide, using NADPH or NADH as an electron donor. This reaction is a part of the microbial dissimilatory sulfate reduction pathway, where sulfate is reduced to sulfide and ultimately used as an electron sink for energy conservation.

The overall reaction catalyzed by hydrogensulfite reductase can be represented as follows:

HSiO3- (hydrogen sulfite) + 2H+ + 2e- → H2S (sulfide) + H2O

There are two main types of hydrogensulfite reductases, which differ in their cofactor requirements and subunit composition:

1. NADPH-dependent membrane-bound (type I) hydrogensulfite reductase: This enzyme is composed of multiple subunits and contains FAD, iron-sulfur clusters, and siroheme as cofactors. It catalyzes the reduction of hydrogen sulfite to sulfide using NADPH as an electron donor, and it is typically found in bacteria that grow under chemolithotrophic conditions (e.g., utilizing sulfur compounds or hydrogen as energy sources).
2. NADH-dependent cytoplasmic (type II) hydrogensulfite reductase: This enzyme consists of a single subunit and contains siroheme and iron-sulfur clusters as cofactors. It catalyzes the reduction of hydrogen sulfite to sulfide using NADH as an electron donor, and it is commonly found in bacteria that grow under heterotrophic conditions (e.g., utilizing organic compounds as energy sources).

In both cases, hydrogensulfite reductase plays a crucial role in the microbial sulfur cycle, contributing to the transformation of various sulfur species and their incorporation into or release from biomolecules.

Archaea are a domain of single-celled microorganisms that lack membrane-bound nuclei and other organelles. They are characterized by the unique structure of their cell walls, membranes, and ribosomes. Archaea were originally classified as bacteria, but they differ from bacteria in several key ways, including their genetic material and metabolic processes.

Archaea can be found in a wide range of environments, including some of the most extreme habitats on Earth, such as hot springs, deep-sea vents, and highly saline lakes. Some species of Archaea are able to survive in the absence of oxygen, while others require oxygen to live.

Archaea play important roles in global nutrient cycles, including the nitrogen cycle and the carbon cycle. They are also being studied for their potential role in industrial processes, such as the production of biofuels and the treatment of wastewater.

Oxidoreductases acting on sulfur group donors are a class of enzymes that catalyze redox reactions involving sulfur group donors. These enzymes play a crucial role in various biological processes, such as the metabolism of sulfur-containing compounds and the detoxification of xenobiotics.

The term "oxidoreductase" refers to any enzyme that catalyzes an oxidation-reduction reaction, where one molecule is oxidized (loses electrons) and another is reduced (gains electrons). In the case of oxidoreductases acting on sulfur group donors, the sulfur atom in the substrate serves as the electron donor.

The systematic name for this class of enzymes follows a specific format: "donor:acceptor oxidoreductase." The donor is the sulfur-containing compound that donates electrons, and the acceptor is the molecule that accepts the electrons. For example, the enzyme that catalyzes the reaction between glutathione (GSH) and a variety of electrophiles is called glutathione transferase, or GST (donor:acceptor oxidoreductase).

These enzymes are further classified into subclasses based on the type of acceptor involved in the reaction. Examples include:

* EC 1.8.1: Oxidoreductases acting on CH-NH2 group donors
* EC 1.8.3: Oxidoreductases acting on CH or CH2 groups
* EC 1.8.4: Oxidoreductases acting on the CH-CH group of donors
* EC 1.8.5: Oxidoreductases acting on a sulfur group of donors
* EC 1.8.6: Oxidoreductases acting on NADH or NADPH

The subclass EC 1.8.5, oxidoreductases acting on a sulfur group of donors, includes enzymes that catalyze redox reactions involving sulfur-containing compounds such as thiols (compounds containing -SH groups), disulfides (-S-S- bonds), and other sulfur-containing functional groups. These enzymes play crucial roles in various biological processes, including detoxification, antioxidant defense, and redox regulation.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

I'm happy to help! However, I believe there might be a slight mistake in your question. "Archaeal" is not a term used to describe genes but rather a group of single-celled organisms that are classified as archaea.

Archaea are one of the three domains of life, along with bacteria and eukaryotes (which include plants, animals, and fungi). Archaea are unique because they share characteristics with both bacteria and eukaryotes, but they also have many features that are distinctly their own. For example, archaea have a different cell membrane structure than bacteria and eukaryotes, which allows them to thrive in extreme environments such as hot springs, salt mines, and deep-sea vents.

Genes, on the other hand, are segments of DNA that contain the instructions for making proteins or performing other important functions in an organism's cells. All living organisms, including archaea, have genes that are passed down from generation to generation. Archaeal genes are made up of the same four nucleotides (A, T, C, and G) as bacterial and eukaryotic genes, and they code for proteins and RNA molecules that are essential for the survival and reproduction of archaea.

So, to summarize, there is no specific definition for "Archaeal genes" because "archaeal" is not a term used to describe genes. However, we can say that archaeal genes are segments of DNA that contain the instructions for making proteins and performing other important functions in archaea.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Enzyme stability refers to the ability of an enzyme to maintain its structure and function under various environmental conditions, such as temperature, pH, and the presence of denaturants or inhibitors. A stable enzyme retains its activity and conformation over time and across a range of conditions, making it more suitable for industrial and therapeutic applications.

Enzymes can be stabilized through various methods, including chemical modification, immobilization, and protein engineering. Understanding the factors that affect enzyme stability is crucial for optimizing their use in biotechnology, medicine, and research.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Crystallization is a process in which a substance transitions from a liquid or dissolved state to a solid state, forming a crystal lattice. In the medical context, crystallization can refer to the formation of crystals within the body, which can occur under certain conditions such as changes in pH, temperature, or concentration of solutes. These crystals can deposit in various tissues and organs, leading to the formation of crystal-induced diseases or disorders.

For example, in patients with gout, uric acid crystals can accumulate in joints, causing inflammation, pain, and swelling. Similarly, in nephrolithiasis (kidney stones), minerals in the urine can crystallize and form stones that can obstruct the urinary tract. Crystallization can also occur in other medical contexts, such as in the formation of dental calculus or plaque, and in the development of cataracts in the eye.

Sulfur is not typically referred to in the context of a medical definition, as it is an element found in nature and not a specific medical condition or concept. However, sulfur does have some relevance to certain medical topics:

* Sulfur is an essential element that is a component of several amino acids (the building blocks of proteins) and is necessary for the proper functioning of enzymes and other biological processes in the body.
* Sulfur-containing compounds, such as glutathione, play important roles in antioxidant defense and detoxification in the body.
* Some medications and supplements contain sulfur or sulfur-containing compounds, such as dimethyl sulfoxide (DMSO), which is used topically for pain relief and inflammation.
* Sulfur baths and other forms of sulfur-based therapies have been used historically in alternative medicine to treat various conditions, although their effectiveness is not well-established by scientific research.

It's important to note that while sulfur itself is not a medical term, it can be relevant to certain medical topics and should be discussed with a healthcare professional if you have any questions or concerns about its use in medications, supplements, or therapies.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Cation transport proteins are a type of membrane protein that facilitate the movement of cations (positively charged ions) across biological membranes. These proteins play a crucial role in maintaining ion balance and electrical excitability within cells, as well as in various physiological processes such as nutrient uptake, waste elimination, and signal transduction.

There are several types of cation transport proteins, including:

1. Ion channels: These are specialized protein structures that form a pore or channel through the membrane, allowing ions to pass through rapidly and selectively. They can be either voltage-gated or ligand-gated, meaning they open in response to changes in electrical potential or binding of specific molecules, respectively.

2. Ion pumps: These are active transport proteins that use energy from ATP hydrolysis to move ions against their electrochemical gradient, effectively pumping them from one side of the membrane to the other. Examples include the sodium-potassium pump (Na+/K+-ATPase) and calcium pumps (Ca2+ ATPase).

3. Ion exchangers: These are antiporter proteins that facilitate the exchange of one ion for another across the membrane, maintaining electroneutrality. For example, the sodium-proton exchanger (NHE) moves a proton into the cell in exchange for a sodium ion being moved out.

4. Symporters: These are cotransporter proteins that move two or more ions together in the same direction, often coupled with the transport of a solute molecule. An example is the sodium-glucose cotransporter (SGLT), which facilitates glucose uptake into cells by coupling its movement with that of sodium ions.

Collectively, cation transport proteins help maintain ion homeostasis and contribute to various cellular functions, including electrical signaling, enzyme regulation, and metabolic processes. Dysfunction in these proteins can lead to a range of diseases, such as neurological disorders, cardiovascular disease, and kidney dysfunction.

The Archaeoglobus fulgidus genome is a circular chromosome roughly half the size of E. coli at 2,178,000 base pairs. Although ... PubMed references for Archaeoglobus PubMed Central references for Archaeoglobus Google Scholar references for Archaeoglobus ( ... for Archaeoglobus Search Species2000 page for Archaeoglobus MicrobeWiki page for Archaeoglobus LPSN page for Archaeoglobus ... Archaeoglobus is a genus of the phylum Euryarchaeota. Archaeoglobus can be found in high-temperature oil fields where they may ...
Archaeoglobus fulgidus (370 aas; gbAE001071), Methanobacterium thermoautotrophicum (365 aas; gbAE000865) and Synechocystis (383 ...
... and the archaeon Archaeoglobus fulgidus. With the exception of A. fulgidus, all known microbes that grow via perchlorate ...
"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry. 49 (41): 8912-21. doi:10.1021 ...
"Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry. 49 (41): 8912-21. doi:10.1021 ...
November 1997). "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus". ... June 2010). "Complete genome sequence of Archaeoglobus profundus type strain (AV18)". Standards in Genomic Sciences. 2 (3): 327 ...
November 1997). "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus". ... Archaeoglobus fulgidus in 1997, and Pyrococcus horikoshii in 1998. Although genes of archaellins were identified all these ...
... from Archaeoglobus Fulgidus". Journal of Structural and Functional Genomics. 7 (1): 37-50. doi:10.1007/s10969-006-9008-x. PMID ...
hgcG is significantly similar to a region of the Archaeoglobus fulgidus genome. The genes were named hgcA through hgcG ("high ...
... sulphate-reducing archaeon Archaeoglobus fulgidus". Nature. 390 (6658): 364-370. Bibcode:1997Natur.390..364K. doi:10.1038/37052 ... Archaeoglobus are chemoorganotrophic sulfate-reducing archaea, the only known member of the Archaea that possesses this type of ... Archaeoglobus species are found in a variety of extreme environments, including deep-sea hydrothermal vents, oil reservoirs, ... Archaeoglobaceae have three genera and here are some brief differences between them: Archaeoglobus: This genus contains the ...
The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined. In humans, the genes NADK and MNADK ... "Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP". Journal of Molecular ...
The α′2 structure is only found in Archaeoglobus fulgidus and Thermoplasma acidophilum. The heterotetramer (αβ)2 structure is ...
The sulfate-reducing Archaeoglobus fulgidus (and several other archaea) also have this enzyme. Reduction of 2-hydroxyphenazine ...
"Oxygen detoxification in the strict anaerobic archaeon Archaeoglobus fulgidus: superoxide scavenging by neelaredoxin". Mol. ...
February 2002). "Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution ...
Formyl-MFR dehydrogenase was also isolated from Methanosarcina barkeri and Archaeoglobus fulgidus cell extracts. Molybdenum- ...
showed evidence that CRISPR repeat regions from the genome of Archaeoglobus fulgidus were transcribed into the long RNA ... May 2002). "Identification of 86 candidates for small non-messenger RNAs from the archaeon Archaeoglobus fulgidus". Proceedings ...
Hyperthermophilic sulfate-reducing archaen Archaeoglobus fulgidus has been recently reported to enable anaerobic oxidation of ... Archaeoglobus fulgidus". The ISME Journal. 8 (11): 2153-66. doi:10.1038/ismej.2014.58. PMC 4992073. PMID 24763368. Benjdia A, ... PflD is reported to be responsible for the capacity of A. fulgidus to grow on a wide range of unsaturated carbons and fatty ...
Archaeoglobus fulgidus MDR1 (troR), a metal-dependent transcriptional repressor, which negatively regulates its own ...
Ftr from the mesophilic methanogen Methanosarcina barkeri and the sulphate-reducing archaeon Archaeoglobus fulgidus have a ...
"The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A". ...
"The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A". J. ...
... from Archaeoglobus fulgidus. Atomic-resolution structures of three other bacterial importers, E. coli BtuCD, E. coli maltose ...
Archaeoglobus fulgidus Methanococcus jannaschii Aeropyrum pernix Sulfolobus Methanopyrus kandleri strain 116, an archaeon in 80 ...
... with two members in Archaeoglobus fulgidus. They are related to UbiD, a 3-octaprenyl-4-hydroxybenzoate carboxy-lyase from ...
Cys-tRNA synthase from Archaeoglobus fulgidus". Journal of Molecular Biology. 370 (1): 128-41. doi:10.1016/j.jmb.2007.04.050. ...
... gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non-ribosomal peptide synthases". Journal of ...
... gamma-glutamyl ligase from Archaeoglobus fulgidus -- a member of a new family of non-ribosomal peptide synthases". Journal of ...
In the Archaeoglobus fulgidus CopA (TC# 3.A.3.5.7), invariant residues in helixes 6, 7 and 8 form two transmembrane metal ... The delivery of Cu+ by Archaeoglobus fulgidus Cu+-chaperone, CopZ (see TC# 3.A.3.5.7), to the corresponding Cu+-ATPase, CopA ( ... 2008) have determined structures of two constructs of the Cu (CopA) pump from Archaeoglobus fulgidus by cryoelectron microscopy ...
... archaeoglobus MeSH B07.200.080.080.100 - archaeoglobus fulgidus MeSH B07.200.400.400 - halobacteriaceae MeSH B07.200.400.400. ...
Find proteins for O28984 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)) ... Archaeoglobus fulgidus thioredoxin 3 M60H. *PDB DOI: https://doi.org/10.2210/pdb4XHM/pdb ...
Timeline for Species Archaeon Archaeoglobus fulgidus [TaxId:2234] from c.31.1.5 AF0112, Sir2 homolog (Sir2-AF2): *Species ... PDB entries in Species: Archaeon Archaeoglobus fulgidus:. *Domain(s) for 1ma3: *. Domain d1ma3a_: 1ma3 A: [78883]. complexed ... Species Archaeon Archaeoglobus fulgidus [TaxId:2234] from c.31.1.5 AF0112, Sir2 homolog (Sir2-AF2) appears in SCOP 1.67. * ... Species Archaeon Archaeoglobus fulgidus [TaxId:2234] from c.31.1.5 AF0112, Sir2 homolog (Sir2-AF2) appears in SCOP 1.71. * ...
Timeline for Species Archaeoglobus fulgidus [TaxId:2234] from c.124.1.5 Putative eIF-2B delta-subunit: *Species Archaeoglobus ... PDB entry in Species: Archaeoglobus fulgidus [TaxId: 2234]:. *Domain(s) for 1t5o: *. Domain d1t5oa1: 1t5o A:4-341 [106459]. ... Lineage for Species: Archaeoglobus fulgidus [TaxId: 2234]. *Root: SCOPe 2.08 *. Class c: Alpha and beta proteins (a/b) [51349 ... Species Archaeoglobus fulgidus [TaxId:2234] from c.124.1.5 Putative eIF-2B delta-subunit appears in SCOPe 2.07. ...
Archaeoglobus fulgidus DSM 8774). Find diseases associated with this biological target and compounds tested against it in ...
This provided a basis for a model of the CO metabolism of ,i,A. fulgidus,/i,. The model suggests proton translocation by &# ... Overall, carboxidotrophic growth seems as an intrinsic capacity of ,i,A. fulgidus,/i, with little need for novel resistance or ... Herein, transcription profiles were obtained from ,i,A. fulgidus,/i, during growth with CO and sulfate or thiosulfate, or ... Archaeoglobus fulgidus,/i,, utilizes CO as an energy source and it is resistant to the toxic effects of high CO concentrations ...
Find proteins for O29664 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)) ... Crystal structure of a PIN (PilT N-terminus) domain (AF0591) from Archaeoglobus fulgidus at 1.90 A resolution. Levin, I., ... CRYSTAL STRUCTURE OF a PIN (PILT N-TERMINUS) DOMAIN CONTAINING PROTEIN (AF0591) FROM ARCHAEOGLOBUS FULGIDUS AT 1.90 A ... FROM ARCHAEOGLOBUS FULGIDUS AT 1.90 A RESOLUTION ... Archaeoglobus fulgidus. Mutation(s): 3 Gene Names: AF0591. EC: ...
The Archaeoglobus fulgidus genome is a circular chromosome roughly half the size of E. coli at 2,178,000 base pairs. Although ... PubMed references for Archaeoglobus PubMed Central references for Archaeoglobus Google Scholar references for Archaeoglobus ( ... for Archaeoglobus Search Species2000 page for Archaeoglobus MicrobeWiki page for Archaeoglobus LPSN page for Archaeoglobus ... Archaeoglobus is a genus of the phylum Euryarchaeota. Archaeoglobus can be found in high-temperature oil fields where they may ...
Archaeoglobus fulgidus 2fwr_a O29889 99.40 4.70E-18 5.10E-22 197.90 0 0 0 0 0 0 0 0 ...
Archaeoglobus fulgidus 1txg_b O29390 99.50 8.10E-19 4.80E-23 148.90 0 0 0 0 0 0 0 0 ...
Archaeoglobus fulgidus reverse gyrase complexed with ADPNP; X-RAY DIFFRACTION 3.20 Å SMTL ID. 1gl9.1. Ligands. ... Archaeoglobus fulgidus reverse gyrase complexed with ADPNP ...
... robot was employed to set up 2D crystallization trials with the membrane proteins CopA from Archaeoglobus fulgidus and light- ...
Archaeoglobus fulgidus 1ob8 (chain B). Holliday-junction resolving enzyme Hje. Q97YX6 (HJE_SACS2). 135. 3.0-3.1. Saccharolobus ... The other two Hj-resolving enzymes originate from Archaeoglobus fulgidus and P. furiosus (see Table 3. for an overview of the ... except for HJC_ARCFU (A. fulgidus) and HJC_SACS2 (S. solfataricus), which are quite similar in their dimeric organizations ( ...
Vis forfatter(e) (2006). Excision of 1-methyladenine and 3-methylcytosine from DNA by AfAlkA of Archaeoglobus fulgidus. ... Vis forfatter(e) (2005). Excision of dUMP from DNA by the hyperthermophilic archaeon Archaeoglobus fulgidus. ... Vis forfatter(e) (2005). Excision of dUMP from DNA by the hyperthermophilic archaeon Archaeoglobus fulgidus. ... Vis forfatter(e) (2004). Excision of dUMP from DNA by the hyperthermophilic archaeon Archaeoglobus fulgidus. ...
Archaeoglobus fulgidus (2). *. Caenorhabditis elegans (1). *. Homo sapiens (19). *. Mus musculus (3). ...
Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB. 2g9n. Structure of the DEAD domain of Human eukaryotic ... Reverse gyrase from Archaeoglobus fulgidus. 1gl9. Archaeoglobus fulgidus reverse gyrase complexed with ADPNP. ...
Archaeoglobus fulgidus takes the perchlorate in, gains energy by transforming it into highly reactive chlorite and moves on. ... Its possible, then, that A. fulgidus is one of the most primeval forms of life on the Earth, evolving potentially even before ... The rise of that modern atmosphere-creating process may have driven A. fulgiduss ancestors to the dark, deep, hot places of ... The byproduct of that breakdown, however, is oxygen, which A. fulgidus cannot tolerate. It survives the potential onslaught by ...
2013) Crystal structure of Cas1 from Archaeoglobus fulgidus and characterization of its nucleolytic activity Biochemical and ... that from Archaeoglobus fulgidus (Kim et al., 2013) with which it shares 32% sequence identity, the N-terminal domains have an ... that from Archaeoglobus fulgidus (Kim et al., 2013) with which it shares 32% sequence identity, the N-terminal domains have an ... fulgidus, as well as those of the aligned N-termini and catalytic domains. The following sentence has now been included in the ...
Crystal Structure of the Archaeal Homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus. ... Crystal Structure of the Archaeal homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus. ...
EpnrDVLVIVGGIVPEEDVPKLKEMGVAKVFGPGTPLNEIIDFIRAEVPKLKR 144 Archaeoglobus fulgidus WP_010884372 88 GIkvnE---DVLVVAGGIIPPDDAEELKKM ... 010879708 10 RKIRVIVAKPGLDGHDRGAKVVARALRDAGFEVIYTGIRRTPEEIAETALQEDADVVGLSILSGAHLELTPMVIEELRKR 89 Archaeoglobus f... WP_ ... The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond ...
Archaeoglobus fulgidus complete genome. 2178400 bp. 12/17/97. Arctic ground squirrel hepatitis B virus. 3302 bp. 8/9/95. ...
Here we report crystal structures of XPB in complex with Bax1 from Archaeoglobus fulgidus (Af) and Sulfolobus tokodaii (St). ...
Methanocaldococcus janaschii1-3 and Archaeoglobus fulgidus, both TyrRS systems), the addition of a third OTS to this group is ... Diese stammen von Methanocaldococcus janaschii1-3 und Archaeoglobus fulgidus (beides TyrRS Systeme). Ein drittes OTS in dieser ... Methanocaldococcus janaschii1-3 and Archaeoglobus fulgidus, both TyrRS systems), the addition of a third OTS to this group is ...
Archaeoglobus fulgidus NADH oxidase (NoxA-3). We developed two patterns for the rhodanese family. They are based on highly ...
Crystal structure of adenosine 5ʹ-phosphosulfate kinase isolated from Archaeoglobus fulgidus. Kawakami, T., Teramoto, T. & ...
Archaeoglobus fulgidus DSM 4304 ) [TaxId: 224325 ], SCOPe (2.08). A. d2phna_. Alpha and beta proteins (a+b). CofE-like. CofE- ... Crystal structure of an amide bond forming F420-gamma glutamyl ligase from Archaeoglobus fulgidus. ...
... 另一種嗜高溫古生菌Archaeoglobus fulgidus脂肪酶(AFL)具有嗜熱與嗜鹼的特性,最適作用條件分別為,pH值為10.0、溫度為90℃。BSL與AFL的X-ray結晶立體結構已經被解出,AFL的 C- ... Lipase from Archaeoglobus fulgidus (AFL) has been proved to be a hyperthermophilic and alkalophilic enzyme with a optimal pH ... Archaeoglobus fulgidus 脂肪酶. zh_TW. dc.description.abstract. B. subtilis lipase (BSL) has been used in the fields
  • Archaeoglobi Archaeoglobales Archaeoglobaceae Archaeoglobus Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC. (expasy.org)
  • RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination. (unil.ch)
  • The crystal structure of AF1521 (a Macro domain-only protein from Archaeoglobus fulgidus) has also been reported and compared with other Macro domain containing proteins. (sdsc.edu)
  • The hyperthermophilic, sulfate-reducing archaeon, Archaeoglobus fulgidus , utilizes CO as an energy source and it is resistant to the toxic effects of high CO concentrations. (hindawi.com)
  • The complete A. fulgidus genome sequence revealed the presence of a nearly complete set of genes for methanogenesis. (wikipedia.org)
  • The Archaeoglobus fulgidus genome is a circular chromosome roughly half the size of E. coli at 2,178,000 base pairs. (wikipedia.org)
  • Comparative genomic studies on archaeal genomes provide evidence that members of the genus Archaeoglobus are the closest relatives of methanogenic archaea. (wikipedia.org)
  • Additionally, 18 proteins which are uniquely found in members of Thermococci, Archaeoglobus and methanogens have been identified, suggesting that these three groups of Archaea may have shared a common relative exclusive of other Archaea. (wikipedia.org)
  • Archaeoglobus species utilize their environment by acting as scavengers with many potential carbon sources. (wikipedia.org)
  • High-temperature sulfate reduction by Archaeoglobus species contributes to deep subsurface oil-well 'souring' by iron sulfide, which causes corrosion of iron and steel in oil-and gas-processing systems. (up.ac.za)
  • quinone oxidoreductase complex (Fqo) is crucial in energy conservation in A. fulgidus during growth with lactate [ 13 ]. (hindawi.com)
  • Archaeoglobus is a genus of the phylum Euryarchaeota. (wikipedia.org)
  • This is supported by the presence of 10 conserved signature proteins that are uniquely found in all methanogens and Archaeoglobus. (wikipedia.org)
  • A liquid-handling robot was employed to set up 2D crystallization trials with the membrane proteins CopA from Archaeoglobus fulgidus and light-harvesting complex II (LH2) from Rhodobacter sphaeroides. (nih.gov)
  • Lipase from Archaeoglobus fulgidus (AFL) has been proved to be a hyperthermophilic and alkalophilic enzyme with a optimal pH and temperature of 10.0 and 90℃, respectively. (ntnu.edu.tw)
  • Archaeoglobus members are hyperthermophiles that can be found in hydrothermal vents, oil deposits, and hot springs. (wikipedia.org)
  • Herein, transcription profiles were obtained from A. fulgidus during growth with CO and sulfate or thiosulfate, or without an electron acceptor. (hindawi.com)
  • The hyperthermophile, Archaeoglobus fulgidus , is so far the only known carboxydotrophic sulfate-reducing archaeon and has a high tolerance for CO, growing at more than 200 kPa of CO [ 2 , 3 ]. (hindawi.com)
  • No H 2 was detected in cultures of A. fulgidus supplemented with CO and sulfate [ 2 ] ruling out H 2 cycling as a relevant energy conservation mechanism. (hindawi.com)
  • This provided a basis for a model of the CO metabolism of A. fulgidus . (hindawi.com)
  • Which of these CODHs that are essential in the CO metabolism of A. fulgidus remains unknown. (hindawi.com)
  • Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus Arch. (wikipedia.org)
  • The most similar archaeal sequences are separate chains, such as AF2215 and AF2219 of Archaeoglobus fulgidus, that correspond roughly to the first 500 and last 130 residues, respectively of known methylmalonyl-CoA mutases. (nih.gov)
  • It's possible, then, that A. fulgidus is one of the most primeval forms of life on the Earth, evolving potentially even before oxygen-producing photosynthesis . (scientificamerican.com)
  • Overall, carboxidotrophic growth seems as an intrinsic capacity of A. fulgidus with little need for novel resistance or respiratory complexes. (hindawi.com)
  • Archaeoglobus grow anaerobically at extremely high temperatures between 60 and 95 °C, with optimal growth at 83 °C (ssp. (wikipedia.org)
  • 83 °C) are ideal growth temperatures for Archaeoglobus, although a biofilm environment provides some environmental elasticity. (wikipedia.org)
  • Archaeoglobus fulgidus takes the perchlorate in, gains energy by transforming it into highly reactive chlorite and moves on. (scientificamerican.com)
  • The rise of that modern atmosphere-creating process may have driven A. fulgidus 's ancestors to the dark, deep, hot places of the globe. (scientificamerican.com)
  • The putative lipase, AF1763, from Archaeoglobus fulgidus is a carboxylesterase with a very high pH optimum. (mpg.de)
  • Archaeoglobus is a genus of the phylum Euryarchaeota. (wikipedia.org)
  • Comparative genomic studies on archaeal genomes provide evidence that members of the genus Archaeoglobus are the closest relatives of methanogenic archaea. (wikipedia.org)
  • The role of nonconserved residues of Archaeoglobus fulgidus ferritin on its unique structure and biophysical properties. (anl.gov)
  • Archaeoglobus fulgidus ferritin (AfFtn) is the only tetracosameric ferritin known to form a tetrahedral cage, a structure that remains unique in structural biology. (anl.gov)
  • The structure of AF2331, a 11-kDa orphan protein of unknown function from Archaeoglobus fulgidus, was solved by Se-Met MAD to 2.4 Å resolution. (mssm.edu)
  • The function of these genes in A. fulgidus remains unknown, while 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. (wikipedia.org)
  • The Archaeoglobus fulgidus genome is a circular chromosome roughly half the size of E. coli at 2,178,000 base pairs. (wikipedia.org)
  • It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. (unl.edu)
  • We have solved the structures of the proteolytic domain of A and B type Lon proteases, encoded by E. coli and Archaeoglobus fulgidus, as well as the N-terminal and α domains of E. coli Lon. (nih.gov)
  • 14. Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP. (nih.gov)
  • Archaeoglobus veneficus sp. (dsmz.de)
  • Using the Y2H (yeast two-hybrid) system, with candidate Archaeoglobus fulgidus replication factors as baits, a number of novel. (silverchair.com)
  • 19. Autophosphorylation of Archaeoglobus fulgidus Rio2 and crystal structures of its nucleotide-metal ion complexes. (nih.gov)
  • Here, we report the crystal structures of Archaeoglobus fulgidus RNase HII in complex with PCNA, and human PCNA bound to a C-terminal peptide of RNASEH2B. (ox.ac.uk)
  • Enzymes and coenzymes of the carbon monoxide dehydrogenase pathway for autotrophic CO2 fixation in Archaeoglobus lithotrophicus and the lack of carbon monoxide dehydrogenase in the heterotrophic A. profundus Arch. (wikipedia.org)
  • Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity]. (nih.gov)
  • Archaeoglobus can be found in high-temperature oil fields where they may contribute to oil field souring. (wikipedia.org)
  • Archaeoglobus grow anaerobically at extremely high temperatures between 60 and 95 °C, with optimal growth at 83 °C (ssp. (wikipedia.org)