2.3.1.222	evolution	PduL homologues are distributed among at least 49 bacterial species but are absent from the Archaea and Eukarya. Sequence analyses show that PduL is unrelated in amino acid sequence to known phosphotransacylase, PTAC, enzymes	719708	
2.3.1.222	evolution	the phosphotransacylase (PTAC) predominantly associated with metabolosomes (PduL) has no sequence homology to the PTAC ubiquitous among fermentative bacteria (Pta). PduL and Pta exemplify functional, but not structural, convergent evolution	-, 758101	
2.3.1.222	malfunction	both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate	755849	
2.3.1.222	malfunction	pduL mutants are unable to ferment 1,2-propanediol and are also impaired for aerobic growth on this compound, overview. Ectopic expression of pduL corrects the growth defects of a pta mutant, the pta gene encodes another PTAC enzyme	719708	
2.3.1.222	metabolism	both pduL genes (pduL1 and pduL2) are associated with acetate formation via acetyl-coenzyme A (acetyl-CoA). Their disruption enables a shift in the homoacetic pathway to the genetically synthesized homolactic pathway via pyruvate	755849	
2.3.1.222	metabolism	PduL is required in the 1,2-propandiol degradation pathway, overview	719708	
2.3.1.222	metabolism	the fact that PduL is confined almost exclusively to metabolosomes can be used to develop an inhibitor that blocks only PduL and not Pta as a way to selectively disrupt bacterial microcompartments(BMC)-based metabolism, while not affecting most commensal organisms that require phosphotransacylase (PTAC) activity	-, 758101	
2.3.1.222	physiological function	PduL is a phosphotransacylase, PTAC, required for 1,2-propanediol degradation	719708