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Objectives <p>Marine bacteria are valuable reservoirs of novel carbohydrate-active enzymes (CAZymes) with industrial relevance. A halophilic marine bacterial strain PBL-D1, was isolated from Batu Laut beach in Selangor, Malaysia. The 16S rRNA gene sequence analysis identified strain PBL-D1 as a member of the genus <i>Gaetbulibacter</i>. To date, no enzymes from <i>Gaetbulibacter</i> spp. have been biochemically characterised. The present study reports on the annotated draft genome of <i>Gaetbulibacter</i> sp. PBL-D1 and comparative genome analyses of <i>Gaetbulibacter</i> glycoside hydrolase (GH) enzymes. These findings provide the first genomic insights into the GH repertoire of <i>Gaetbulibacter</i> spp., revealing unexplored enzymes with promising potential for industrial biocatalysis.</p> Data description <p>The draft genome of <i>Gaetbulibacter</i> sp. PBL-D1 is 3,433,971 bp in size, has a G+C content of 33.0%, and encodes 3,068 protein-coding genes. The CAZymes analysis revealed that <i>Gaetbulibacter</i> genomes harboured at least nine putative GH-encoding genes, grouped into starch-degrading and β-glucan-degrading enzymes. These enzymes are of industrial importance, particularly in food processing and biofuel production. Collectively, PBL-D1 and other available <i>Gaetbulibacter</i> genomes serve as attractive sources of GH candidates that may be useful in polysaccharide degradation.</p>

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Genome sequence of Gaetbulibacter sp. PBL-D1 isolated from a Malaysian beach: insights into glycoside hydrolase repertoires

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  • 发表日期：

    2025年12月8日

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  • Ummirul Mukminin Kahar,
  • Najiha Atiqah Md Nor,
  • Wan Nur Izrena Wan Izanni

摘要

Objectives

Marine bacteria are valuable reservoirs of novel carbohydrate-active enzymes (CAZymes) with industrial relevance. A halophilic marine bacterial strain PBL-D1, was isolated from Batu Laut beach in Selangor, Malaysia. The 16S rRNA gene sequence analysis identified strain PBL-D1 as a member of the genus Gaetbulibacter. To date, no enzymes from Gaetbulibacter spp. have been biochemically characterised. The present study reports on the annotated draft genome of Gaetbulibacter sp. PBL-D1 and comparative genome analyses of Gaetbulibacter glycoside hydrolase (GH) enzymes. These findings provide the first genomic insights into the GH repertoire of Gaetbulibacter spp., revealing unexplored enzymes with promising potential for industrial biocatalysis.

Data description

The draft genome of Gaetbulibacter sp. PBL-D1 is 3,433,971 bp in size, has a G+C content of 33.0%, and encodes 3,068 protein-coding genes. The CAZymes analysis revealed that Gaetbulibacter genomes harboured at least nine putative GH-encoding genes, grouped into starch-degrading and β-glucan-degrading enzymes. These enzymes are of industrial importance, particularly in food processing and biofuel production. Collectively, PBL-D1 and other available Gaetbulibacter genomes serve as attractive sources of GH candidates that may be useful in polysaccharide degradation.