In silico characterization and structural modelling of HMBS enzyme in duck population

Nowadays, consumers are increasingly knowledgeable and favouring native livestock breeds as sources of protein, including meat and eggs, due to their high nutritional profiles. Genetic studies have become a common method to unravel the genetic mechanisms behind beneficial growth traits in both humans and livestock. Hydroxymethylbilane synthase (HMBS), an enzyme encoded by HMBS gene is an intermediate enzyme involved in the biosynthesis of heme, crucial for maintaining oxygen transport capacity, cellular respiration and detoxification processes. This study was conducted to perform a detailed computational analysis of the HMBS (Hydroxymethylbilane synthase) protein, focusing on its physicochemical properties, predictions of secondary and tertiary structures, and interacting partners. The sequence of HMBS protein in Anas platyrhynchos was retrieved in FASTA format from the National Center for Biotechnology Information (NCBI), and standard bioinformatic tools and software were used to characterize and model its structure. Computational analysis revealed HMBS to be an acidic, non-polar, and thermostable protein predominantly localized in the cytoplasm. Conserved domain analysis indicated the presence of a single highly conserved pattern in the amino acid sequences. The majority of the protein consists of random coil and alpha helix structures, facilitating interactions with other proteins. Subcellular localization suggested a cytoplasmic role, crucial for maintaining cellular metabolism. Understanding the structural characteristics of this protein will enhance insights into its molecular mechanisms. Additionally, the predicted 3-D model serves as a valuable resource for future research, providing a foundation for exploring the protein's broader functional potential.