| IED ID | IndEnz0005000379 |
| Enzyme Type ID | lipase000379 |
| Protein Name |
Diacylglycerol O-acyltransferase 1 DGAT EC 2.3.1.20 Acyl-CoA-dependent diacylglycerol O-acyltransferase Acyl-CoA:monoacylglycerol acyltransferase MGAT EC 2.3.1.22 Triacylglycerol synthase TAG synthase |
| Gene Name | DGA1 YOR245C |
| 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 | MSGTFNDIRRRKKEEGSPTAGITERHENKSLSSIDKREQTLKPQLESCCPLATPFERRLQTLAVAWHTSSFVLFSIFTLFAISTPALWVLAIPYMIYFFFDRSPATGEVVNRYSLRFRSLPIWKWYCDYFPISLIKTVNLKPTFTLSKNKRVNEKNYKIRLWPTKYSINLKSNSTIDYRNQECTGPTYLFGYHPHGIGALGAFGAFATEGCNYSKIFPGIPISLMTLVTQFHIPLYRDYLLALGISSVSRKNALRTLSKNQSICIVVGGARESLLSSTNGTQLILNKRKGFIKLAIQTGNINLVPVFAFGEVDCYNVLSTKKDSVLGKMQLWFKENFGFTIPIFYARGLFNYDFGLLPFRAPINVVVGRPIYVEKKITNPPDDVVNHFHDLYIAELKRLYYENREKYGVPDAELKIVG |
| Enzyme Length | 418 |
| Uniprot Accession Number | Q08650 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:20225889, ECO:0000269|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22; Evidence={ECO:0000269|PubMed:20554061}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 2-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-glycerol + CoA; Xref=Rhea:RHEA:39951, ChEBI:CHEBI:52323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:27620384};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39952; Evidence={ECO:0000305|PubMed:20554061}; |
| DNA Binding | |
| EC Number | 2.3.1.20; 2.3.1.22 |
| Enzyme Function | FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty acyl-CoA as substrates. Required for storage lipid synthesis. Major DAG esterifying enzyme in stationary phase when TAG production is particularly active. Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains, and in ergosterol biosynthesis (PubMed:11741946, PubMed:11751830, PubMed:11751875, PubMed:14640980, PubMed:15155725, PubMed:21321129, PubMed:32349126). Also has monoacylglycerol acyltransferase (MGAT) activity, catalyzing the acyl-CoA-dependent esterification of monoacylglycerol to diacylglycerol (PubMed:20554061). 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). {ECO:0000269|PubMed:11741946, ECO:0000269|PubMed:11751830, ECO:0000269|PubMed:11751875, ECO:0000269|PubMed:14640980, ECO:0000269|PubMed:15155725, ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21321129, ECO:0000269|PubMed:22738231, ECO:0000269|PubMed:32349126}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000305}. |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (3); Modified residue (1); Mutagenesis (6); Region (1); Topological domain (5); Transmembrane (4) |
| Keywords | Acyltransferase;Endoplasmic reticulum;Glycerol metabolism;Glycoprotein;Lipid biosynthesis;Lipid droplet;Lipid metabolism;Membrane;Phosphoprotein;Reference proteome;Transferase;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:20225889, ECO:0000269|PubMed:21321129, ECO:0000269|PubMed:32349126}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum. {ECO:0000269|PubMed:32349126}. |
| Modified Residue | MOD_RES 17; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:17330950 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10688190; 11283351; 12743757; 15218532; 16246075; 16429126; 16916618; 16919863; 17107617; 17688423; 18258205; 18269180; 18367008; 18430725; 18614533; 18631243; 19202381; 19536198; 19608739; 19690167; 19696439; 19708857; 19763656; 20016074; 20056167; 20231294; 20400321; 20567816; 21146236; 21693588; 21729000; 21782973; 21812932; 21875690; 21933415; 22101561; 22345606; 22446555; 22454508; 22480867; 22523576; 22752918; 23139841; 23275493; 23613035; 23631861; 23899824; 23932357; 24057105; 24373967; 24418527; 24520995; 24597968; 24628496; 24663078; 24678285; 25016085; 25116045; 25117580; 25181516; 25267159; 25461829; 25483081; 25500271; 25540432; 25894691; 25908426; 25948336; 26004510; 26055703; 26162625; 26179227; 26269581; 26432633; 26615590; 26636650; 26907989; 27230908; 27270031; 27307588; 27311564; 27459103; 27506614; 27521373; 27932491; 32058036; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,711 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:27620384}; Vmax=5.8 nmol/min/mg enzyme with (9Z)-octadecenoyl-CoA as substrate {ECO:0000269|PubMed:27620384}; |
| Metal Binding | |
| Rhea ID | RHEA:10868; RHEA:32947; RHEA:39951; RHEA:39952 |
| Cross Reference Brenda | 2.3.1.20; |