2.3.1.158	evolution	PDAT belongs to the LCAT-like family	720694	
2.3.1.158	evolution	phylogenetic analysis showed that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1	757544	
2.3.1.158	evolution	phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1	757544	
2.3.1.158	evolution	two PDAT orthologues, AtPDAT1 and AtPDAT2, with 57% amino acid sequence similarity, are identified in Arabidopsis thaliana. Phylogenetic analysis shows that plant PDAT can be grouped into four clades, two of which have one putative transmembrane domain (TMD) while the other two are predicted to be entirely soluble. The majority of PDAT in the database have the single-predicted TMD consisting of a small cytosolic N-terminus and a large C-terminal domain in the endoplasmic reticulum lumen. The N-terminal region is hydrophilic with arginine clusters similar to those observed in DGAT1	757544	
2.3.1.158	malfunction	artificial microRNA silencing of PDAT alters the membrane lipid composition, reducing the maximum specific growth rate	720694	
2.3.1.158	malfunction	LRO1 single knockout has a markedly reduced level of the coreinduced LD formation	758135	
2.3.1.158	malfunction	seedlings deficient in the enzyme PDAT1 are unable to accumulate triacylglycerols after heat stress	758046	
2.3.1.158	malfunction	the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity	-, 757544	
2.3.1.158	metabolism	different members of Camelina sativa phospholipid diacylglycerol acyltransferase family are involved in different types of stress responses in camelina seedlings, providing evidence of their roles in oil biosynthesis and regulation in camelina vegetative tissue	756132	
2.3.1.158	metabolism	specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis	758030	
2.3.1.158	metabolism	specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG	757544	
2.3.1.158	metabolism	specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG	757544	
2.3.1.158	metabolism	specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of 1,2-diacyl-sn-glycerol (sn-1,2-DAG) to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1,2-DAG to yield TAG. PDAT and DGAT2 are the major contributors to TAG biosynthesis and their relative contributions were dependent on the yeast growth stage	-, 757544	
2.3.1.158	metabolism	the enzyme catalyses the final acylation step in triacylglycerol biosynthesis by transferring a fatty acyl moiety from a phospholipid to diacylglycerol	756132	
2.3.1.158	metabolism	the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors	-, 757544	
2.3.1.158	metabolism	the enzyme contributes to the conversion of membrane lipids into triacylglycerol in Myrmecia incisa during the nitrogen starvation stress	-, 758363	
2.3.1.158	metabolism	the enzyme is a major determinant of triacylglycerol biosynthesis at the exponential growth stage. Overexpression of AtPDAT1 results in no effects on the fatty-acid and lipid composition, despite the fact that increased PDAT activity is observed in microsomes prepared from AtPDAT1 Arabidopsis overexpressor lines. PDAT1 is a dominant determinant in Arabidopsis seed triacylglycerol biosynthesis in the absence of DGAT1 activity	757544	
2.3.1.158	metabolism	the enzyme is responsible for Hepatitis C Virus core-induced lipid droplet formation in yeast	758135	
2.3.1.158	metabolism	the enzyme is responsible for the last step of triacylglycerol synthesis in the acyl-CoA-independent pathway, catalyzing membrane lipid transformation	-, 755830	
2.3.1.158	metabolism	the enzyme plays an important role in triacylglycerol synthesis	758053	
2.3.1.158	metabolism	triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). Scheme for triacylglycerol (TAG) biosynthesis in developing seeds of oleaginous higher plants. Specific role of DGAT (EC 2.3.1.20) and PDAT (EC 2.3.1.158) genes in fatty acid biosynthesis, regulation, overview. DGAT catalyzes the final acylation of the sn-3 position of sn-1, 2-DAG to form TAG, which is the committed step in acyl-CoA-dependent TAG biosynthesis. TAG can also be synthesized through acyl-CoA-independent pathways via the catalytic action of PDAT, which catalyzes the transfer of an acyl moiety from the sn-2 position of phosphatidylcholine (PtdCho) to the sn-3 position of sn-1, 2-DAG to yield TAG. The gradually increased transcription levels of MiPDAT in Myrmecia incisa during the cultivation under nitrogen starvation conditions is proposed to be responsible for the decrease and increase of the phosphatidylcholine and TAG levels, respectively	-, 758363	
2.3.1.158	additional information	comparison to human enzyme LCAT (EC 2.3.1.43)	-, 757544	
2.3.1.158	physiological function	expression of isoform DGTT1 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis and leads to presence of oleic acid and lipid droplet formation	736102	
2.3.1.158	physiological function	expression of isoform DGTT2 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis. Complementation by DGTT2 increased triacylglycerol content by 9fold	736102	
2.3.1.158	physiological function	expression of isoform DGTT3 complements the defect in the yeast DELTAdga1DELTAlro1 mutant that lacks the activity of triacylglycerol synthesis	736102	
2.3.1.158	physiological function	expression of isoform PDAT1 restores triacylglycerol synthesis in Saccharomyces cerevisiae H1246 when culturing yeast in the presence of alpha-linolenic acid	736422	
2.3.1.158	physiological function	MiPDAT links triacylglycerol (TAG) accumulation with phospholipid during the course of nitrogen starvation. This enzyme transfers an acyl group from the sn-2 position of phospholipids (PLs) to the sn-3 position of diacylglycerol (DAG), yielding sn-1-lysophospholipid and TAG, respectively. The temporal and spatial evidence for MiPDAT contributing to the conversion of membrane lipids into TAG Myrmecia incisa during nitrogen starvation stress is provided, MiPDAT can use membrane phosphatidylcholine to synthesize TAG in the microalgae grown under nitrogen starvation stress	-, 758363	
2.3.1.158	physiological function	overexpression of isoform PDAT1 increases leaf triacylglycerol accumulation, leading to oil droplet overexpansion through fusion. Ectopic expression of oleosin promotes the clustering of small oil droplets. Coexpression of PDAT1 with oleosin boosts leaf triacylglycerol content by up to 6.4% of the dry weight without affecting membrane lipid composition and plant growth. PDAT1 overexpression stimulates fatty acid synthesis and increases fatty acid flux toward the prokaryotic glycerolipid pathway. In the trigalactosyldiacylglycerol1-1 mutant, defective in eukaryotic thylakoid lipid synthesis, the combined overexpression of PDAT1 with oleosin increases leaf triacylglycerol content to 8.6% of the dry weight and total leaf lipid by fourfold. In the plastidic glycerol-3-phosphate acyltransferase1 mutant, defective in the prokaryotic glycerolipid pathway, PDAT1 overexpression enhances triacylglycerol content at the expense of thylakoid membrane lipids, leading to defects in chloroplast division and thylakoid biogenesis	736985	
2.3.1.158	physiological function	PDAT1-mediated triacylglycerol accumulation increases heat resistance	758046	
2.3.1.158	physiological function	phospholipid:diacylglycerol acyltransferase (PDAT) is an acyl-CoA-independent pathway enzyme using phosphatidylcholine (PC) as the acyl donor, in which the transfer of an acyl group from the sn-2 position of phosphatidylcholine to the sn-3 position of DAG yields triacylglycerol (TAG)	758030	
2.3.1.158	physiological function	phospholipid:diacylglycerol acyltransferase in the green microalga Chlamydomonas reinhardtii catalyzes triacylglycerol synthesis via two pathways: transacylation of diacylglycerol with acyl groups from phospholipids and galactolipids and diacylglycerol:diacylglycerol transacylation. PDAT-mediated membrane lipid turnover and triacylglycerol synthesis is essential for vigorous growth under favorable culture conditions and for membrane lipid degradation with concomitant production of triacylglycerol for survival under stress. PDAT also possesses acyl hydrolase activities using triacylglycerols, phospholipids, galactolipids, and cholesteryl esters as substrates	720694	
2.3.1.158	physiological function	triacylglycerol (TAG) can be formed through acyl-CoA-independent pathways via the catalytic action of membrane-bound phospholipid:diacylglycerol acyltransferase (PDAT). PDAT catalyzes the transfer of the acyl moiety at the sn-2 position of phosphatidylcholine (PtdCho) or phosphatidylethanolamine to the sn-3 position of sn-1, 2-DAG, yielding TAG and sn-1 lyso-PtdCho or sn-1 lysophosphatidylethanolamine	-, 757544	
2.3.1.158	physiological function	upon expression of heterologous oleate 12-hydroxylase in Arabidopsis thaliana mutants deficient in phospholipid:diacylglycerol acyltransferases 1 or 2 accumulate hydroxy fatty acids and show no difference with wild-type plants. Mutants are also able to accumulate hydroxy fatty acids in seed neutral lipids. Individually, phospholipid:diacylglycerol acyltransferases 1 or 2 do not play a major role in the incorporation of hydroxy fatty acids into triacylglycerols	697014