| IED ID | IndEnz0005000061 |
| Enzyme Type ID | lipase000061 |
| Protein Name |
Phospholipase A1 PLIP2, chloroplastic EC 3.1.1.32 Galactolipase PLIP2 EC 3.1.1.26 Protein PLASTID LIPASE 2 |
| Gene Name | PLIP2 At1g02660 T14P4.6 |
| 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 | MDSLCLNSGLHGVIPAITAVGNGGCGGVVEVRATASAPSQKRGPFGFSFKYPLTPFWSRGGGGGIASRRRSGLCLDDAVLVDSGDSRKPIAEETAVEMDTERRNGSWVLKILDVQSTWKHEEEEDDDEVEDEDGDEDEEVELDDAVVSEDDGGCDVCSVLEDDGNEANKFQLDRESFSKLLRRVTLPESKLYAQLSYLGNLAYSISKIKPANLSKYYGLRFVTSSAEKTESALKAENGEVSGETKPIVEAEEEVEEEEKNKSRKISASAAYEIVASAASYLHSRTNNILPFNSSSKAENSDKHDVNLTNAESSSDVAYSVTSVVAAEEDVKQAVADDLKSTISSPCDWFICDDDQSHTRFVVIQGSESLASWQANLLFEPIEFEGLGAIVHRGIYEAAKGMYEQMLPEVKAHIKTHGTSAKFRFTGHSLGGSLSLLLNLMLLVRGEVPASSLLPVITYGAPFVLCGGDRLLKKLGLPKSHVQAIVMHRDIVPRAFSCNYPYHVAELLKAVNGNFRSHPCLNKQSMLYSPMGELLILQPDETFSPGHELLPSGNGLYLLTSDFESPDIEDSDEERLRAAQTVFLNTPHPLDILSDRSAYGSSGTIQRDHDMNSYLKAVRSVIRKEVNQIRRAKREHRRSLWWPILVARESGSSGIAVSNGQINGQDFSGMMQTGRKSLQRFSRLVASQHMPLIVVMLFPVKLLFLGAFNVFSFR |
| Enzyme Length | 713 |
| Uniprot Accession Number | F4HXL0 |
| Absorption | |
| Active Site | ACT_SITE 428; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 489; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 608; /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=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56449; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+) + octadecanoate; Xref=Rhea:RHEA:56636, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:76084, ChEBI:CHEBI:84822; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56637; Evidence={ECO:0000269|PubMed:29666162}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:56640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:42027, ChEBI:CHEBI:76084; Evidence={ECO:0000269|PubMed:29666162};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56641; 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 monogalactosyldiacylglycerol (MGDG). 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); Compositional bias (1); Erroneous gene model prediction (1); Motif (1); Mutagenesis (1); Region (2); Sequence conflict (3); 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}. Plastid, chloroplast stroma {ECO:0000269|PubMed:29666162}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12810710; 15720654; 15890746; 17217462; 17408486; 18070919; 18684332; 18775970; 23505340; 23517122; |
| Motif | MOTIF 426..430; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:Q948R1 |
| Gene Encoded By | |
| Mass | 78,346 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13189; RHEA:13190; RHEA:18689; RHEA:18690; RHEA:38783; RHEA:38784; RHEA:56448; RHEA:56449; RHEA:40823; RHEA:40824; RHEA:56636; RHEA:56637; RHEA:56640; RHEA:56641; RHEA:38787; RHEA:38788 |
| Cross Reference Brenda |