In silico characterization of acid phosphatase in the functional genome of the amazon prawn

Abstract

The acid phosphatase (ACP) enzyme is responsible for the hydrolysis of phosphate monoesters under acidic conditions, being widely found in microorganisms, animals and plants. In crustaceans, the ACP plays a key role in the defense mechanism of distinct species. Furthermore, the expression of ACP is sensitive to pollution, being particularly related to the stress response by the exposure to heavy metals and organophosphate pesticides. However, most studies in crustaceans refer to the biochemical properties of ACP but little is known about its structural characterization.  In the present work, we carried out in silico searches of ACP in the functional genome of Macrobrachium amazonicum, recognized as the most abundant freshwater prawn in Amazon. The ACP gene of M. amazonicum comprised a total of 3326 nucleotides (nt), including a complete open reading frame (ORF) of 1389 nt corresponding to the translation of 462 aminoacids. Signal peptide and intermembrane regions as well as conserved Pfam Pur_ac_phosph_N, Metallophos and Pfam Metallophos_C domains were present in the protein. In addition, we located 8 active sites, 25 homotrimeric and 15 homotetrameric interfaces, and 7 metal-binding sites. In general, we detected highly conserved sites shared among crustaceans.  These data might be useful to provide effective biomarkers to assess the environmental quality and further biotechnological applications of ACP.