Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ABSTRACT: Metagenome assembly of PRJEB36096 data set (Anaerobic oxidation of ethane by archaea in different marine environments)

PROVIDER: PRJEB87643 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	ERR5000362_cleaned.contigs.fa.gz	Other
	ERR3799536_cleaned.contigs.fa.gz	Other
	ERR3799538_cleaned.contigs.fa.gz	Other
	ERR5000365_cleaned.contigs.fa.gz	Other
	ERR5000366_cleaned.contigs.fa.gz	Other

Items per page:

1 - 5 of 13

Similar Datasets

Project description:Anaerobic oxidation of ethane by archaea in different marine environments

| PRJEB36096 | ENA

Project description:Anaerobic ethane oxidation by archaea in the Guaymas Basin

| PRJEB36446 | ENA

Anaerobic ethane and butane oxidation

Project description:Bioreactor was set up to enrich microorganisms capable of mediating anaerobic ethane and butane oxidation coupled to ntirate reduction. Metaproteomics was conducted to identify the expressed proteins in active microbes.

2024-05-24 | PXD039267 | Pride

Project description:Anaerobic ethane oxidation of DAMO culture

| PRJNA563763 | ENA

marine metagenome

Project description:marine amonia oxidation archaea metagenome Metagenome

| PRJNA379351 | ENA

Identification of the proteins composing the CO dehydrogenase and furfurylformamide dehydrogenase enzymes purified from a thermophilic ethane-oxidizing microbial consortium

Project description:Identification of the peptides composing the enriched multisubunit enzymes natively purified from the microbial enrichment, based on gel bands obtained by native electrophoresis. The anaerobic oxidation of alkanes is a microbial process occurring in deep-sea hydrocarbon seeps that plays a key ecological role in these exotic niches. The metabolic capacity of anaerobic ethane oxidation, involving uncharted biochemistry, was reported in two archaeal species depending on sulfate-reducing partner bacteria. This study deciphers the molecular basis of the CO2-generating steps of ethanotrophy by characterising the native archaeal enzymes isolated from a thermophilic enrichment. While other microorganisms couple these steps to ferredoxin reduction, we found that the CO-dehydrogenase and the formylmethanofuran-dehydrogenase are bound to F420-reductase modules. The crystal structures of these multi-metalloenzyme complexes revealed electronic bridges coupling C1-oxidation to F420-reduction. Accordingly, both systems exhibit robust F420-reductase activities, which are not detected in methanogenic or methanotrophic relative organisms. We speculate that the whole catabolism of these archaea is reoriented towards F420-reduction, which facilitates the electron transfer to the sulfate-reducing partner, therefore representing the driving force of ethanotrophy.

2024-09-23 | PXD054507 | Pride

Project description:Enrichment of anaerobic ethane and butane oxidation microorganisms

| PRJNA989758 | ENA

Characterization of a thaumarchaeal symbiont that drives incomplete nitrification in the tropical sponge Ianthella basta

Project description:Marine sponges represent one of the few eukaryotic groups that ubiquitously harbor symbiotic members of the Thaumarchaeota, which are important chemoautotrophic ammonia-oxidizers in many environments. However in most studies, direct demonstration of ammonia-oxidation by these archaea within sponges is lacking, and little is known about sponge-specific adaptations of archaeal ammonia oxidizers (AOA). In this study, we characterized the thaumarchaeal symbiont of the marine sponge Ianthella basta using metaproteogenomics, fluorescence in situ hybridization, qPCR and direct isotope-based functional assays. We demonstrate that the I. basta symbiont is not closely related to other genomically sequenced sponge AOA and is a member of a new genus. “Candidatus Nitrosospongia bastadiensis” is an abundant symbiont that is solely responsible for nitrite formation from ammonia in I. basta that surprisingly does not harbor nitrite-oxidizing microbes. Consistently, Ca N. bastadiensis encodes and expresses the genetic repertoire required for chemolithoautotrophic ammonia oxidation. Furthermore, we show that this AOA is equipped with an expanded set of extracellular subtilisin-like proteases, a metalloprotease unique among archaea, as well as a putative branched-chain amino acid ABC transporter. This repertoire is strongly indicative of a mixotrophic lifestyle and is (with slight variations) also found in other sponge-associated, but not in free-living AOA. We predict that this feature as well as an expanded and unique set of secreted serpins (protease inhibitors), a unique array of eukaryotic-like proteins, and a DNA-phosporothioation system likely involved in defense against foreign DNA, represent important adaptations of AOA to life within these ancient filter-feeding animals.

2019-11-13 | PXD012484 | Pride

Metaproteomics analyses of three chronically petroleum-polluted sites

Project description:Crude oil is the one of the most important natural assets of humankind, yet it is a major environmental pollutant, in particular, in marine environments. One of the largest crude oil polluted areas in the word is the semi-enclosed Mediterranean Sea, where the metabolic potential of indigenous populations towards the chronic pollution at a large scale is yet to be defined, particularly in anaerobic and micro-anaerobic marine sites. Here, we provided a novel insight into the active microbial metabolism in sediments from three environments along the coastline of Italy. Microbial proteomes exhibited prevalence in anaerobic metabolism, not related to the biodegradation directly, suggesting the strong limitation by oxygen induced by the carbon overload. They also point at previously unrecognized metabolic coupling between methane and methanol utilizers as well as sulfur reducers in marine petroleum polluted sediments.

2015-07-24 | PXD001490 | Pride

marine metagenome

Project description:marine Archaea metagenome

| PRJNA379345 | ENA