Detail Information for IndEnz0005000646
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