In discovering novel laccase enzymes with interesting catalytic and stability properties, there is still scope for improvement in exploring new sites in Algeria. The bio-prospecting approach allowed the isolation of a novel strain, Streptomyces sp. HBD30 from the Agrioun River, northern Algeria. Following a functional approach, two laccases (LacI and LacII) were purified and characterised, showing appealing properties as thermostable enzymes, and oxidised typical phenolic and non-phenolic substrates with a higher affinity towards syringaldazine, followed by 2,6-dimethoxyphenol and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid). Further analyses revealed that the Streptomyces sp. HDB30 genome contained an array of genes coding for carbohydrate active enzymes (CAZome) and lignin-degrading enzymes to degrade lignocellulose. In addition to enlarging the repertoire of thermostable laccases, this study uncovered the metabolic potential of a new Streptomyces strain, which is useful for a wide range of applications.