Application | Comment | Organism |
---|---|---|
biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Brassica napus |
biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Crepis palaestina |
biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Arabidopsis thaliana |
biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Helianthus annuus |
biotechnology | the enzymes catalyzing the terminal steps of triacylglycerol (TAG) formation, DGAT and PDAT play crucial roles in determining the flux of carbon into seed TAG and thus have been considered as the key targets for engineering oil production | Ricinus communis |
Cloned (Comment) | Organism |
---|---|
gene LRO1, DNA and amino acid sequence determination and analysis | Saccharomyces cerevisiae |
overexpression in Arabidopsis thaliana increases alpha-linolenic acis content in seed oil | Linum usitatissimum |
overexpression in Arabidopsis thaliana increases hydroxy fatty acid in seed oil | Ricinus communis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | - |
Helianthus annuus | - |
- |
additional information | 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 | Crepis palaestina | - |
- |
additional information | 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 | Arabidopsis thaliana | - |
- |
additional information | 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 | Saccharomyces cerevisiae | - |
- |
additional information | 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 | Brassica napus | - |
- |
additional information | 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 | Helianthus annuus | - |
- |
additional information | 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 | Ricinus communis | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1,2-diacyl-sn-glycerol | Brassica napus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Crepis palaestina | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Arabidopsis thaliana | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Saccharomyces cerevisiae | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Helianthus annuus | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Ricinus communis | - |
CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | Saccharomyces cerevisiae ATCC 204508 | - |
CoA + 1,2,3-triacylglycerol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | Q9FNA9 | - |
- |
Arabidopsis thaliana | Q9FYC7 | - |
- |
Brassica napus | - |
- |
- |
Crepis palaestina | - |
- |
- |
Helianthus annuus | A0A251VCQ4 | - |
- |
Linum usitatissimum | - |
- |
- |
Ricinus communis | - |
- |
- |
Ricinus communis | F2VR35 | - |
- |
Saccharomyces cerevisiae | P40345 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P40345 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds | Arabidopsis thaliana | - |
additional information | isozyme AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds, whereas isozyme AtPDAT2 is highly expressed in seeds | Arabidopsis thaliana | - |
seed | - |
Helianthus annuus | - |
seed | high expression | Arabidopsis thaliana | - |
seed | AtPDAT1 is expressed generally at higher levels in vegetative tissues than in seeds | Arabidopsis thaliana | - |
seed | highly expressed in seeds | Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Brassica napus | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Crepis palaestina | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Arabidopsis thaliana | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Saccharomyces cerevisiae | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Helianthus annuus | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Ricinus communis | CoA + 1,2,3-triacylglycerol | - |
? | |
acyl-CoA + 1,2-diacyl-sn-glycerol | - |
Saccharomyces cerevisiae ATCC 204508 | CoA + 1,2,3-triacylglycerol | - |
? | |
additional information | Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity | Saccharomyces cerevisiae | ? | - |
- |
|
additional information | Saccharoymces cerevisiae PDAT also displays low DAG:DAG transacylase activity | Saccharomyces cerevisiae ATCC 204508 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
At3g44830 | - |
Arabidopsis thaliana |
At5g13640 | - |
Arabidopsis thaliana |
AtPDAT1 | - |
Arabidopsis thaliana |
AtPDAT2 | - |
Arabidopsis thaliana |
LRO1 | - |
Saccharomyces cerevisiae |
PDAT | - |
Brassica napus |
PDAT | - |
Ricinus communis |
PDAT | - |
Linum usitatissimum |
PDAT | - |
Crepis palaestina |
PDAT | - |
Arabidopsis thaliana |
PDAT | - |
Saccharomyces cerevisiae |
PDAT | - |
Helianthus annuus |
PDAT1 | - |
Arabidopsis thaliana |
PDAT2 | - |
Arabidopsis thaliana |
phospholipid:diacylglycerol acyltransferase | - |
Brassica napus |
phospholipid:diacylglycerol acyltransferase | - |
Crepis palaestina |
phospholipid:diacylglycerol acyltransferase | - |
Arabidopsis thaliana |
phospholipid:diacylglycerol acyltransferase | - |
Saccharomyces cerevisiae |
phospholipid:diacylglycerol acyltransferase | - |
Helianthus annuus |
phospholipid:diacylglycerol acyltransferase | - |
Ricinus communis |
YNR008w | - |
Saccharomyces cerevisiae |
Organism | Comment | Expression |
---|---|---|
Brassica napus | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
Crepis palaestina | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
Arabidopsis thaliana | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
Helianthus annuus | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
Ricinus communis | the R2R3-type MYB96 transcription factor is shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
Saccharomyces cerevisiae | the R2R3-type MYB96 transcription factor was shown to regulate TAG biosynthesis by directly activating the expression of DGAT1 and PDAT1. DGAT1 expression is regulated by MYB96 through binding to the promoter of ABI4, whereas MYB96 regulates PDAT1 expression by directly binding to the PDAT1 promoter | up |
General Information | Comment | Organism |
---|---|---|
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 | Helianthus annuus |
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 | Ricinus communis |
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 | Brassica napus |
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 | Crepis palaestina |
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 | Arabidopsis thaliana |
malfunction | the removal of the putative N-terminal transmembrane domain (TMD) in Saccharomyces cerevisiae PDAT does not affect activity | Saccharomyces cerevisiae |
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 | Arabidopsis thaliana |
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 | Brassica napus |
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 | Crepis palaestina |
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 | Arabidopsis thaliana |
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 | Helianthus annuus |
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 | Ricinus communis |
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 | Saccharomyces cerevisiae |
metabolism | the enzyme catalyzes the acyl-CoA-independent synthesis of triacylglycerol using membrane glycerolipids as acyl donors | Saccharomyces cerevisiae |
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 | Arabidopsis thaliana |
additional information | comparison to human enzyme LCAT (EC 2.3.1.43) | Saccharomyces cerevisiae |
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 | Brassica napus |
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 | Crepis palaestina |
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 | Arabidopsis thaliana |
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 | Saccharomyces cerevisiae |
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 | Helianthus annuus |
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 | Ricinus communis |