Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Activated sludge metagenome

ABSTRACT: Identification of putative bulking bacteria

PROVIDER: PRJDB8383 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	DRR180487_1.fastq.gz	Fastqsanger.gz
	DRR180487_2.fastq.gz	Fastqsanger.gz
	DRR180488_1.fastq.gz	Fastqsanger.gz
	DRR180488_2.fastq.gz	Fastqsanger.gz
	DRR180489_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 24

Similar Datasets

activated sludge metagenome

Project description:Bulking activated sludge Raw sequence reads

| PRJNA326227 | ENA

Census of the viral metagenome within an activated sludge microbial assemblage.

Project description:The viral metagenome within an activated sludge microbial assemblage was sampled using culture-dependent and culture-independent methods and compared to the diversity of activated sludge bacterial taxa. A total of 70 unique cultured bacterial isolates, 24 cultured bacteriophages, 829 bacterial metagenomic clones of 16S rRNA genes, and 1,161 viral metagenomic clones were subjected to a phylogenetic analysis.

| S-EPMC2849206 | biostudies-literature

activated sludge metagenome

Project description:Bacteria Genome sequencing

| PRJNA274327 | ENA

Gene cloning and characterization of a novel esterase from activated sludge metagenome.

Project description:A metagenomic library was prepared using pCC2FOS vector containing about 3.0 Gbp of community DNA from the microbial assemblage of activated sludge. Screening of a part of the un-amplified library resulted in the finding of 1 unique lipolytic clone capable of hydrolyzing tributyrin, in which an esterase gene was identified. This esterase/lipase gene consists of 834 bp and encodes a polypeptide (designated EstAS) of 277 amino acid residuals with a molecular mass of 31 kDa. Sequence analysis indicated that it showed 33% and 31% amino acid identity to esterase/lipase from Gemmata obscuriglobus UQM 2246 (ZP_02733109) and Yarrowia lipolytica CLIB122 (XP_504639), respectively; and several conserved regions were identified, including the putative active site, HSMGG, a catalytic triad (Ser92, His125 and Asp216) and a LHYFRG conserved motif. The EstAS was overexpressed, purified and shown to hydrolyse p-nitrophenyl (NP) esters of fatty acids with short chain lengths (< or = C8). This EstAS had optimal temperature and pH at 35 degrees C and 9.0, respectively, by hydrolysis of p-NP hexanoate. It also exhibited the same level of stability over wide temperature and pH ranges and in the presence of metal ions or detergents. The high level of stability of esterase EstAS with its unique substrate specificities make itself highly useful for biotechnological applications.

| S-EPMC3224729 | biostudies-literature

sludge metagenome

Project description:bulking activated sludge Raw sequence reads

| PRJNA376060 | ENA

sludge metagenome

Project description:bulking activated sludge Raw sequence reads

| PRJNA376090 | ENA

activated sludge metagenome

Project description:QDW1 bacteria Raw sequence reads

| PRJNA554459 | ENA

activated sludge metagenome

Project description:Activated sludge bacteria Genome sequencing