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WS/DGAT domain-containing protein
This domain is found at the C-terminus of wax ester synthases (WS)/diacylglycerol O-acyltransferases (DGAT). These enzymes are utilised for the in vivo production of biodiesel and other wax esters [1]. [1]. 31559109. Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters. Petronikolou N, Nair SK;. ACS Catal. 2018;8:6334-6344. (from Pfam)
wax ester/triacylglycerol synthase domain-containing protein
This domain is found in wax ester synthases/diacylglycerol O-acyltransferases (WS/DAGs), largely found in bacteria, plants and animals. They catalyse the condensation of a fatty alcohol and a fatty acyl-Coenzyme A (acyl-CoA) and they can also catalyse the transesterification of acyl-CoAs with diacylglycerols. These are bifunctional enzymes (WS/DAGs) that share low overall sequence similarity but all WS/DGATs share a conserved HHXXXDG motif, which is also found in other acyltransferases [1,2]. This entry represents the N-terminal catalytic domain of WS/DAGs which contains the conserved HHXXXDG motif. It consists of a mixed beta-sheet flanked by four alpha-helices and a small antiparallel beta-sheet [2]. [1]. 12502715. A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol acyltransferase mediates wax ester and triacylglycerol biosynthesis in Acinetobacter calcoaceticus ADP1. Kalscheuer R, Steinbuchel A;. J Biol Chem. 2003;278:8075-8082. [2]. 31559109. Structural and Biochemical Studies of a Biocatalyst for the Enzymatic Production of Wax Esters. Petronikolou N, Nair SK;. ACS Catal. 2018;8:6334-6344. (from Pfam)
WS/DGAT/MGAT family O-acyltransferase
WS/DGAT/MGAT family O-acyltransferase catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates; such as Acinetobacter baylyi O-acyltransferase WSD, a bifunctional wax ester synthase/diacylglycerol acyltransferase
wax ester/triacylglycerol synthase family O-acyltransferase
This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase.
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