| IED ID | IndEnz0005000702 |
| Enzyme Type ID | lipase000702 |
| Protein Name |
Triacylglycerol lipase SDP1 EC 3.1.1.3 Protein SUGAR-DEPENDENT 1 |
| Gene Name | SDP1 At5g04040 F8F6.10 F8F6_250 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MDISNEASVDPFSIGPSSIMGRTIAFRVLFCRSMSQLRRDLFRFLLHWFLRFKLTVSPFVSWFHPRNPQGILAVVTIIAFVLKRYTNVKIKAEMAYRRKFWRNMMRTALTYEEWAHAAKMLEKETPKMNESDLYDEELVKNKLQELRHRRQEGSLRDIMFCMRADLVRNLGNMCNSELHKGRLQVPRHIKEYIDEVSTQLRMVCNSDSEELSLEEKLSFMHETRHAFGRTALLLSGGASLGAFHVGVVRTLVEHKLLPRIIAGSSVGSIICAVVASRSWPELQSFFENSLHSLQFFDQLGGVFSIVKRVMTQGALHDIRQLQCMLRNLTSNLTFQEAYDMTGRILGITVCSPRKHEPPRCLNYLTSPHVVIWSAVTASCAFPGLFEAQELMAKDRSGEIVPYHPPFNLDPEVGTKSSSGRRWRDGSLEVDLPMMQLKELFNVNHFIVSQANPHIAPLLRLKDLVRAYGGRFAAKLAHLVEMEVKHRCNQVLELGFPLGGLAKLFAQEWEGDVTVVMPATLAQYSKIIQNPTHVELQKAANQGRRCTWEKLSAIKSNCGIELALDDSVAILNHMRRLKKSAERAATATSSSHHGLASTTRFNASRRIPSWNVLARENSTGSLDDLVTDNNLHASSGRNLSDSETESVELSSWTRTGGPLMRTASANKFIDFVQSLDIDIALVRGFSSSPNSPAVPPGGSFTPSPRSIAAHSDIESNSNSNNLGTSTSSITVTEGDLLQPERTSNGFVLNVVKRENLGMPSIGNQNTELPESVQLDIPEKEMDCSSVSEHEEDDNDNEEEHNGSSLVTVSSEDSGLQEPVSGSVIDA |
| Enzyme Length | 825 |
| Uniprot Accession Number | Q9LZA6 |
| Absorption | |
| Active Site | ACT_SITE 265; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161; ACT_SITE 424; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diethyl-p-nitrophenyl phosphate, diisopropyl fluorophosphate and [E]-6-[bromoethylene]-3-[1-naphthalenyl]-2H-tetrahydropyran-2-one. {ECO:0000269|PubMed:16473965}. |
| 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:16473965};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000269|PubMed:16473965}; CATALYTIC ACTIVITY: Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + di-(9Z)-octadecenoylglycerol + H(+); Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; Evidence={ECO:0000269|PubMed:16473965};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; Evidence={ECO:0000269|PubMed:16473965}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Involved in the release of fatty acids from the oil body in germinating seedlings (PubMed:16473965, PubMed:19136267, PubMed:27466365). Can hydrolyze triacylglycerols and diacylglycerols but not monoacylglycerols, phospholipids, galactolipids or cholesterol esters (PubMed:16473965, PubMed:19136267). SDP1 lipase activity is required to limit triacylglycerol accumulation in roots, leaves and stems, which are vegetative tissues (PubMed:23686420). Functions synergistically with PDAT1 in regulating fatty acid flow from membrane lipid synthesis toward peroxisomal beta-oxidation through a transient triacylglycerol pool (PubMed:25293755). {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:19136267, ECO:0000269|PubMed:23686420, ECO:0000269|PubMed:25293755, ECO:0000269|PubMed:27466365}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Broad optimum pH around 8.0. {ECO:0000269|PubMed:16473965}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (1); Erroneous initiation (1); Glycosylation (7); Motif (1); Mutagenesis (3); Region (3) |
| Keywords | Glycerol metabolism;Glycoprotein;Hydrolase;Lipid degradation;Lipid droplet;Lipid metabolism;Membrane;Peroxisome;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:25775518}. Membrane {ECO:0000269|PubMed:16473965}; Peripheral membrane protein {ECO:0000305}. Peroxisome {ECO:0000269|PubMed:25775518}. Note=Associates with the oil body membrane (PubMed:16473965). Migrates from peroxisomes to the oil body surface through peroxisomal tubulation (PubMed:25775518). {ECO:0000269|PubMed:16473965, ECO:0000269|PubMed:25775518}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 17449810; 18650403; 18775970; 21515696; 21825108; 22760209; 23171303; 23505340; 24606605; 24696520; 26410300; 26898465; 28572457; 28842550; 29666162; 30796452; |
| Motif | MOTIF 263..267; /note=GXSXG; /evidence=ECO:0000255|PROSITE-ProRule:PRU01161 |
| Gene Encoded By | |
| Mass | 92,092 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12044; RHEA:12045; RHEA:38575; RHEA:38576 |
| Cross Reference Brenda |