2.3.1.158: phospholipid:diacylglycerol acyltransferase
This is an abbreviated version!
For detailed information about phospholipid:diacylglycerol acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.158
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2.3.1.158
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diacylglycerols
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acyl-coa:diacylglycerol
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biodiesel
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acyl-coa-dependent
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acyltransferase1
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presenile
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biotechnology
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camelina
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lpcat
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accase
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oleosins
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energy production
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industry
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synthesis
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molecular biology
- 2.3.1.158
- diacylglycerols
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acyl-coa:diacylglycerol
-
biodiesel
-
acyl-coa-dependent
-
acyltransferase1
-
presenile
- biotechnology
- camelina
- lpcat
- accase
-
oleosins
- energy production
- industry
- synthesis
- molecular biology
Reaction
Synonyms
acyl-CoA-independent phospholipid:diacylglycerol acyltransferase, At3g44830, At5g13640, AtPDAT1, AtPDAT2, CHLREDRAFT_184281, CHLREDRAFT_188937, CsPDAT1-A, CsPDAT1-B, CsPDAT1-C, CsPDAT2-A, CsPDAT2-B, DGTT1, DGTT2, DGTT3, diacylglycerol acyltransferase type 2, LRO1, MiPDAT, PDAT, PDAT1, PDAT1A, PDAT2, phospholipid: diacylglycerol acyltransferase, phospholipid:diacylglycerol acyltransferase, ScPDAT, SiPDAT, SiPDAT2, YNR008w
ECTree
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Localization
Localization on EC 2.3.1.158 - phospholipid:diacylglycerol acyltransferase
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XP_011088820, XP_020553631
SiPDAT2 does not have any transmembrane domains
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additional information
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soluble form is produced for comparison with the native membrane bound enzyme
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
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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
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additional information
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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
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additional information
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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
-
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
-
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
-
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
-
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
-
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
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