Bioinformatics Analysis of Pyruvate Kinase of Rhodococcus Opacus

In order to deeply explore the key regulation mechanism of carbon metabolism of Rhodococcus, the pyruvate kinase (PyK) of Rhodococcus opacus was systematically analyzed by bioinformatics. The results show that the enzyme has a typical PK-like superfamily domain, which can form a homotetramer spatial conformation, and its ADP binding site with metal ions is highly conserved in evolution. Multi-sequence alignment and phylogenetic analysis further revealed that it was conserved in many species, and suggested that it belonged to Cluster II PyK, and its activity did not depend entirely on potassium ions. In addition, the prediction of phosphorylation sites showed that the enzyme had 44 potential modification sites, indicating that its activity might be regulated by complex post-translational modifications. This study provides an important theoretical basis and a new transformation strategy for optimizing the lipid synthesis and environmental remediation ability of Rhodococcus through metabolic engineering.