Detail Information for IndEnz0005000062
IED ID IndEnz0005000062
Enzyme Type ID lipase000062
Protein Name Phospholipase A1 PLIP3, chloroplastic
EC 3.1.1.32
Galactolipase PLIP3
EC 3.1.1.26
Protein PLASTID LIPASE 3
Gene Name PLIP3 At3g62590 F26K9_20
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 MEGVFLKMSVVGVSPMIPVGPSSFICAIGGSVEEKSTAASLPRWVSLRRLRPLEFLRIGGKREEKGTVRDDDAVLLERRDRNRNENDNGNWVLKILEVGSIWKGKRQRSGGGGGGEEDEEEEVAEPKKKEDLCEECDFCRIDDDDEDEEKEKTVFEFSEMLSKIPVEDAQMFAKLSFLGNLAYSIPKIKPENLLKYQKLRFVTSSIEKRMSLKVEENNNGEEDEEKKKLINPAVAYRIAASAASRLFSHSKSVLPFGSSKRQDNEEASLLATADSVTAVVAAKEEVKQAVADDLKSNRSPPCEWFVCDDDKSGTRFFFIQGSDSLASWQANLLFEPVPFEDLDVLVHRGIYEAAKGIYEQMLPEVHAHLNSRGKNRAFLRFSGHSLGGSLSLLVNLMLLIRGQVPASSLLPVITFGSPCIMCGGDRLLQKLGLPKSHLLGISMHRDIVPRAFSCNYPNRAAKLLKALNGNFRNHPCLNNQNVLYSPMGKLLILQPSERFSPPHPLLPPGSGLYLLASKNTDETEKSLRAAKILFFNSPHPLEILSDRRSYGSEGKIKRNHDMSSYLKALRHVIRKELKQMKAERDQWLRKFFIINILFSGRDSLKLITRFVASRSSQLVIIFFLPIRLLIMSVYSVVFHHSQAHFSFFK
Enzyme Length 649
Uniprot Accession Number Q940L4
Absorption
Active Site ACT_SITE 385; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 446; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 560; /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:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13190; Evidence={ECO:0000269|PubMed:29666162}; 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:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:38787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74667, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38788; Evidence={ECO:0000269|PubMed:29666162};
DNA Binding
EC Number 3.1.1.32; 3.1.1.26
Enzyme Function FUNCTION: Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic phosphatidylglycerol (PG). May function downstream of abscisic acid (ABA), and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG). {ECO:0000269|PubMed:29666162}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Erroneous gene model prediction (1); Motif (1); Mutagenesis (1); Region (1); Transit peptide (1)
Keywords Chloroplast;Hydrolase;Lipid degradation;Lipid metabolism;Membrane;Plastid;Reference proteome;Transit peptide
Interact With
Induction INDUCTION: Induced by abscisic acid (ABA) and cold stress. {ECO:0000269|PubMed:29666162}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000269|PubMed:29666162}; Peripheral membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17419845; 18441212; 18650403; 18775970; 23505340;
Motif MOTIF 383..387; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:Q948R1
Gene Encoded By
Mass 73,044
Kinetics
Metal Binding
Rhea ID RHEA:13189; RHEA:13190; RHEA:18689; RHEA:18690; RHEA:38783; RHEA:38784; RHEA:38787; RHEA:38788
Cross Reference Brenda