| IED ID | IndEnz0005000046 |
| Enzyme Type ID | lipase000046 |
| Protein Name |
Phospholipid:diacylglycerol acyltransferase PDAT EC 2.3.1.158 LCAT-related open reading frame 1 Lecithin cholesterol acyl transferase-related open reading frame 1 Triacylglycerol synthase TAG synthase |
| Gene Name | LRO1 YNR008W N2042 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MGTLFRRNVQNQKSDSDENNKGGSVHNKRESRNHIHHQQGLGHKRRRGISGSAKRNERGKDFDRKRDGNGRKRWRDSRRLIFILGAFLGVLLPFSFGAYHVHNSDSDLFDNFVNFDSLKVYLDDWKDVLPQGISSFIDDIQAGNYSTSSLDDLSENFAVGKQLLRDYNIEAKHPVVMVPGVISTGIESWGVIGDDECDSSAHFRKRLWGSFYMLRTMVMDKVCWLKHVMLDPETGLDPPNFTLRAAQGFESTDYFIAGYWIWNKVFQNLGVIGYEPNKMTSAAYDWRLAYLDLERRDRYFTKLKEQIELFHQLSGEKVCLIGHSMGSQIIFYFMKWVEAEGPLYGNGGRGWVNEHIDSFINAAGTLLGAPKAVPALISGEMKDTIQLNTLAMYGLEKFFSRIERVKMLQTWGGIPSMLPKGEEVIWGDMKSSSEDALNNNTDTYGNFIRFERNTSDAFNKNLTMKDAINMTLSISPEWLQRRVHEQYSFGYSKNEEELRKNELHHKHWSNPMEVPLPEAPHMKIYCIYGVNNPTERAYVYKEEDDSSALNLTIDYESKQPVFLTEGDGTVPLVAHSMCHKWAQGASPYNPAGINVTIVEMKHQPDRFDIRGGAKSAEHVDILGSAELNDYILKIASGNGDLVEPRQLSNLSQWVSQMPFPM |
| Enzyme Length | 661 |
| Uniprot Accession Number | P40345 |
| Absorption | |
| Active Site | ACT_SITE 324; /note="Acyl-ester intermediate"; /evidence="ECO:0000250|UniProtKB:Q8NCC3"; ACT_SITE 567; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q8NCC3"; ACT_SITE 618; /note="Charge relay system"; /evidence="ECO:0000250|UniProtKB:Q8NCC3, ECO:0000305|PubMed:32349126" |
| Activity Regulation | |
| Binding Site | BINDING 162; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NCC3; BINDING 325; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:Q8NCC3 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a monoacylglycerophospholipid + a triacyl-sn-glycerol; Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615, ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158; Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386, ECO:0000269|PubMed:30706417}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1-acyl-sn-glycerol = a 1,2-diacyl-sn-glycerol + a 1-acyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:32859, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:64683; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32860; Evidence={ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44232, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986; Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44233; Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1,2-di-(9Z-octadecenoyl)-sn-glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:44236, ChEBI:CHEBI:28610, ChEBI:CHEBI:52333, ChEBI:CHEBI:53753, ChEBI:CHEBI:74669; Evidence={ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44237; Evidence={ECO:0000305|PubMed:10829075, ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-(9Z-octadecenoyl)-sn-glycerol = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + di-(9Z)-octadecenoylglycerol; Xref=Rhea:RHEA:44240, ChEBI:CHEBI:28610, ChEBI:CHEBI:74669, ChEBI:CHEBI:75757, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44241; Evidence={ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:44244, ChEBI:CHEBI:28610, ChEBI:CHEBI:52323, ChEBI:CHEBI:73990, ChEBI:CHEBI:74669; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44245; Evidence={ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44248, ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:75583, ChEBI:CHEBI:78813; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44249; Evidence={ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44252, ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:77686, ChEBI:CHEBI:84234; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44253; Evidence={ECO:0000305|PubMed:18037386}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphoethanolamine = 1,2-di-(9Z)-octadecenoyl-3-(9Z,12Z)-octadecadienoyl-sn-glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:44256, ChEBI:CHEBI:52333, ChEBI:CHEBI:74971, ChEBI:CHEBI:74977, ChEBI:CHEBI:77683; Evidence={ECO:0000269|PubMed:18037386};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44257; Evidence={ECO:0000305|PubMed:18037386}; |
| DNA Binding | |
| EC Number | 2.3.1.158 |
| Enzyme Function | FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid (PubMed:10747858, PubMed:10829075, PubMed:32349126). The preferred acyl donors are phosphatidylethanolamine (PE) and phosphatidylcholine (PC). Also capable of using broad acyl donors such as phosphatidic acid (PA), phosphatidylserine (PS), phosphatidylglycerol (PG) and phosphatidylinositol (PI), as well as monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG), and acyl-CoA, and it is more likely to use unsaturated acyl donors. As acyl acceptors, it prefers 1,2- over 1,3-diacylglycerol (DAG). Additionally, has esterification activity that can utilize methanol as acyl acceptor to generate fatty acid methyl esters (FAME) (PubMed:30706417). Can also utilize ceramide instead of DAG, acylating the ceramides by attaching a fatty acid to the hydroxy group on the first carbon atom of the long-chain base to produce 1-O-acylceramides (PubMed:22738231). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane upon nutrient starvation, where it provides a site of TAG synthesis, which is coupled with nuclear membrane remodeling (PubMed:31422915). {ECO:0000269|PubMed:10747858, ECO:0000269|PubMed:10829075, ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:30706417, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Compositional bias (2); Glycosylation (4); Motif (3); Mutagenesis (2); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Acyltransferase;Endoplasmic reticulum;Glycoprotein;Membrane;Nucleus;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22446555, ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}; Single-pass type II membrane protein {ECO:0000269|PubMed:22446555}. Nucleus inner membrane {ECO:0000269|PubMed:31422915}; Single-pass type II membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum (PubMed:22454508, PubMed:32349126). Relocates from the endoplasmic reticulum to a subdomain of the inner nuclear membrane that associates with the nucleolus upon nutrient starvation (PubMed:31422915). {ECO:0000269|PubMed:22454508, ECO:0000269|PubMed:31422915, ECO:0000269|PubMed:32349126}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11111085; 11741946; 11751830; 11751875; 11786293; 11805837; 12489128; 12743757; 14654091; 14690591; 15218532; 16246075; 16916618; 16919863; 17010666; 18269180; 18367008; 18430725; 18614533; 19202381; 19536198; 19608739; 19690167; 19708857; 19763656; 19930686; 20016074; 20056167; 20231294; 20554061; 20675578; 21060891; 21729000; 21782973; 21875690; 22345606; 22480867; 22523576; 22752918; 22989772; 23139841; 23275493; 23383298; 23631861; 24057105; 24418527; 24520995; 24597968; 24628496; 24663078; 24678285; 25016085; 25181516; 25500271; 25540432; 25894691; 25908426; 25948336; 26004510; 26055703; 26162625; 26269581; 26432633; 26590613; 26636650; 26907989; 27230908; 27270031; 27307588; 27459103; 27521373; 27932491; |
| Motif | MOTIF 43..50; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 64..71; /note=Bipartite nuclear localization signal; /evidence=ECO:0000255|PROSITE-ProRule:PRU00768; MOTIF 322..326; /note=GHSXG lipase motif; /evidence=ECO:0000305|PubMed:31422915 |
| Gene Encoded By | |
| Mass | 75,393 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:14057; RHEA:32859; RHEA:32860; RHEA:44232; RHEA:44233; RHEA:44236; RHEA:44237; RHEA:44240; RHEA:44241; RHEA:44244; RHEA:44245; RHEA:44248; RHEA:44249; RHEA:44252; RHEA:44253; RHEA:44256; RHEA:44257 |
| Cross Reference Brenda | 2.3.1.158; |