IED ID | IndEnz0005000646 |
Enzyme Type ID | lipase000646 |
Protein Name |
Galactolipase DONGLE, chloroplastic EC 3.1.1.26 EC 3.1.1.32 Phospholipase A1 DONGLE Phospholipase A1-Ialpha1 |
Gene Name | DGL At1g05800 T20M3.6 |
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 | MAAKVFTQNPIYSQSLVRDKTPQQKHNLDHFSISQHTSKRLVVSSSTMSPPISSSPLSLPSSSSSQAIPPSRAPAVTLPLSRVWREIQGSNNWENLIEPLSPILQQEITRYGNLLSASYKGFDLNPNSKRYLSCKYGKKNLLKESGIHDPDGYQVTKYIYATPDINLNPIKNEPNRARWIGYVAVSSDESVKRLGRRDILVTFRGTVTNHEWLANLKSSLTPARLDPHNPRPDVKVESGFLGLYTSGESESKFGLESCREQLLSEISRLMNKHKGEEISITLAGHSMGSSLAQLLAYDIAELGMNQRRDEKPVPVTVFSFAGPRVGNLGFKKRCEELGVKVLRITNVNDPITKLPGFLFNENFRSLGGVYELPWSCSCYTHVGVELTLDFFDVQNISCVHDLETYITLVNRPRCSKLAVNEDNFGGEFLNRTSELMFSKGRRQALHFTNAATNAAYLLCSISNHMLYYNIF |
Enzyme Length | 471 |
Uniprot Accession Number | Q9MA46 |
Absorption | |
Active Site | ACT_SITE 286; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 349; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 400; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + 2 H2O = 3-beta-D-galactosyl-sn-glycerol + 2 a fatty acid + 2 H(+); Xref=Rhea:RHEA:13189, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15754, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868; EC=3.1.1.26; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000269|PubMed:19527719}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000269|PubMed:19527719}; CATALYTIC ACTIVITY: Reaction=1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H2O = a fatty acid + acyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-galactosyl]-sn-glycerol + H(+); Xref=Rhea:RHEA:48372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28396, ChEBI:CHEBI:28868, ChEBI:CHEBI:90310; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48373; Evidence={ECO:0000269|PubMed:19527719}; |
DNA Binding | |
EC Number | 3.1.1.26; 3.1.1.32 |
Enzyme Function | FUNCTION: Sn-1-specific phospholipase that releases free fatty acids from phosphatidylcholine. Has a higher galactolipase activity than phospholipase A1 activity when digalactosyldiacylglycerol (DGDG) is used as substrate. Catalyzes the initial step of jasmonic acid biosynthesis. Required for the biosynthesis of basal-level endogenous jasmonate in vegetative tissues. Regulates leaves growth. Not essential for jasmonate biosynthesis after wounding or upon pathogen infection. {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:20348210}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:18267087}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Motif (1); Region (1); Transit peptide (1) |
Keywords | Chloroplast;Hydrolase;Lipid degradation;Lipid metabolism;Plastid;Reference proteome;Transit peptide |
Interact With | |
Induction | INDUCTION: Induced by wounding (PubMed:18267087, PubMed:20348210, PubMed:24430866). Induced by methyl jasmonate (PubMed:24430866). {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:20348210, ECO:0000269|PubMed:24430866}. |
Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:20348210}. Note=PubMed:20348210 shows a localization in lipid droplets. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 14576160; 18375658; 18667720; 19704561; 20855949; 23505340; 29666162; |
Motif | MOTIF 284..288; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:Q948R1 |
Gene Encoded By | |
Mass | 52,800 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:13189; RHEA:13190; RHEA:18689; RHEA:18690; RHEA:48372; RHEA:48373 |
Cross Reference Brenda |