| IED ID | IndEnz0005000003 |
| Enzyme Type ID | lipase000003 |
| Protein Name |
Triacylglycerol lipase 5 TAG lipase 5 TG lipase 5 EC 3.1.1.3 Lipase 5 |
| Gene Name | TGL5 STC2 YOR081C YOR29-32 YOR2964C |
| 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 | MSNTLPVTEFLLSKYYELSNTPATDSSSLFKWLYHKTLSRKQLLISDLSSQKKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMVGQFHEVLKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAITFLKEKIIISSSIKNPLQFYQPRFSEQIKSLSIMDADLPGVDLEESSSNSLSIIKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKANSLSFAIGASSLRLKKSPLKVPSRPQFKKRSSYYNQNMSAEMRKNRKKSGTISSYDVQTNSEDFPIPAIENGSFDNTLFNPSRFPMDAMSAATNDNFMNNSDIFQN |
| Enzyme Length | 749 |
| Uniprot Accession Number | Q12043 |
| Absorption | |
| Active Site | ACT_SITE 216; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 375; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Loses its lipolytic activity in cells lacking nonpolar lipids, but retains its side activity as lysophospholipid acyltransferase. {ECO:0000269|PubMed:27170177}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:16135509}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:20016004};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; Evidence={ECO:0000305|PubMed:20016004}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:42592, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:64839, ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:20016004};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593; Evidence={ECO:0000305|PubMed:20016004}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways (PubMed:16135509). Also catalyzes the acylation of lysophosphatidic acid (LPA) (PubMed:20016004). {ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:20016004}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Glycosylation (10); Modified residue (1); Motif (2); Region (1) |
| Keywords | Glycoprotein;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Phosphoprotein;Reference proteome;Sporulation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:27170177}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000269|PubMed:27170177}. |
| Modified Residue | MOD_RES 645; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11743162; 14574415; 14690591; 16267052; 16554755; 16916618; 16919863; 18258205; 18269180; 18367008; 18467557; 19536198; 19684113; 19696439; 20056167; 20231294; 20489023; 20727985; 21447998; 22345606; 22989772; 23139841; 23275493; 23383298; 24007978; 24418527; 24520995; 24597968; 24678285; 25016085; 25461829; 25894691; 26162625; 26636650; 27693354; |
| Motif | MOTIF 54..59; /note="HXXXXD acyltransferase motif"; /evidence="ECO:0000305|PubMed:20016004, ECO:0000305|Ref.12"; MOTIF 214..218; /note="GXSXG"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" |
| Gene Encoded By | |
| Mass | 84,716 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.7 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:20016004}; KM=29.3 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004}; Vmax=28.8 nmol/min/mg enzyme towards 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate {ECO:0000269|PubMed:20016004}; Vmax=38.1 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20016004}; |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:37131; RHEA:37132; RHEA:42592; RHEA:42593 |
| Cross Reference Brenda |