<HashMap><database>ENA</database><file_versions><headers><Content-Type>application/xml</Content-Type></headers><body><files><Fastqsanger.gz>ftp://ftp.sra.ebi.ac.uk/vol1/fastq/DRR053/DRR053154/DRR053154_2.fastq.gz</Fastqsanger.gz><Fastqsanger.gz>ftp://ftp.sra.ebi.ac.uk/vol1/fastq/DRR053/DRR053154/DRR053154_1.fastq.gz</Fastqsanger.gz><Other></Other></files><type>primary</type></body><statusCode>OK</statusCode><statusCodeValue>200</statusCodeValue></file_versions><scores/><additional><omics_type>Genomics</omics_type><center_name>Department of Bioscience, Faculty of Applied Bioscience, Tokyo University of Agriculture</center_name><full_dataset_link>https://www.ebi.ac.uk/ena/browser/view/PRJDB4493</full_dataset_link><scientific_name>Microbacterium sp. HM58-2</scientific_name><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.</long_description><repository>ENA</repository></additional><is_claimable>false</is_claimable><name>Microbacterium sp. HM58-2</name><description>Study of a hydrazide degrading mechanism by Miacrobacterium sp.</description><dates><last_updated>2025-09-24</last_updated><first_public>2016-04-25</first_public></dates><accession>PRJDB4493</accession><cross_references><taxon>1778770</taxon></cross_references></HashMap>