{"database":"ENA","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Fastqsanger.gz":["ftp://ftp.sra.ebi.ac.uk/vol1/fastq/DRR053/DRR053154/DRR053154_2.fastq.gz","ftp://ftp.sra.ebi.ac.uk/vol1/fastq/DRR053/DRR053154/DRR053154_1.fastq.gz"],"Other":[""]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"omics_type":["Genomics"],"center_name":["Department of Bioscience, Faculty of Applied Bioscience, Tokyo University of Agriculture"],"full_dataset_link":["https://www.ebi.ac.uk/ena/browser/view/PRJDB4493"],"scientific_name":["Microbacterium sp. HM58-2"],"long_description":["Microbacterium sp. strain HM58-2 was isolated from soil to grow with acylhydrazide as sole carbon source. The key enzyme to degrade the compound was identified as hydrazidase, a member of amidase family, by which 1-phenylethylidene hydrazide was converted to 4-hydroxybenzamide and acetophenone hydrazone. The expression of this enzyme is under a catabolite repression, where it is induced by the addition of substrates. Since no genome information was available for this bacterium, the shotgun genome sequence by a Illumina sequencer was performed to obtain information on the catabolite mechanism of hydrazide compounds by this bacterium. Further, the elucidation of natural substrates for hydrazidase would be desirable."],"repository":["ENA"],"additional_accession":[]},"is_claimable":false,"name":"Microbacterium sp. HM58-2","description":"Study of a hydrazide degrading mechanism by Miacrobacterium sp.","dates":{"last_updated":"2025-09-24","first_public":"2016-04-25"},"accession":"PRJDB4493","cross_references":{"taxon":["1778770"]}}