Bacterial enzymes serve as biocatalysts in an ecofriendly and economical way to regulate different metabolic and cellular activities for growth and pathogenesis of microbes . Of the 22 EHPs, 10 proteins were annotated as enzymes, and four proteins were characterized as transferases (Q5NFX5, Q5NFD6, Q5NEX1, and Q5NEB7). Transferases facilitate or catalyze the transfer of a functional group, except hydrogen, from a donor to an acceptor molecule. Q5NFX5 is predicted to contain a glycine cleavage system (GCS) T which is triggered when glycine concentrations are high. Their subsequent unstable complexes are loosely attached to the inner membrane of the mitochondria, and mutations in this system are connected with glycine encephalopathy . Q5NFD6 and Q5NEX1 proteins represent S-adenosyl-Lmethionine-dependent methyltransferase (SAM Mtase) superfamily. All SAM Mtase possess a structurally conserved SAM-binding domain consisting of a central seven-stranded beta sheet that is flanked by three alpha helices per side of the sheet . Q5NEB7 is predicted to have a 4'-phosphopantetheinyl transferase superfamily that transfers the 4'phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to the invariant serine of pp-binding. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP .