Poxvirus TMP kinase is able to phosphorylate dTMP, dUMP and also dGMP from any purine and pyrimidine nucleoside triphosphate. The large substrate specificity is explained by the presence of a canal connecting the edge of the dimer interface to the TMP base binding pocket, canal not found in the human homolog. ATP + dTMP = ADP + dTDP Pyrimidine metabolism; dTTP biosynthesis. Homodimer; the dimer arrangement is orthogonal and not antiparallel as in human enzyme. Belongs to the thymidylate kinase family.