| IED ID | IndEnz0005000947 |
| Enzyme Type ID | lipase000947 |
| Protein Name |
Phospholipase A1-Igamma1, chloroplastic EC 3.1.1.- DAD1-like lipase 4 |
| Gene Name | DALL4 At1g06800 F4H5.11 F4H5_10 |
| 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 | MATIPSHNLRPHTTNQRTQYSLSFRPHFSRSTLITFPARSSPARAMSRTDEEASISTRLEQESYGLTTAEDIRRRDGEAKESKRLRDTWRKIQGEDDWAGLMDPMDPVLRSELIRYGEMAQACYDAFDFDPFSRYCGSCRFTRRHLFDSLGIIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDNEATRCRLGRRDIAIAWRGTVTRLEWIADLKDFLKPVSGNGFRCPDPAVKAESGFLDLYTDKDTSCNFSKFSAREQVLTEVKRLVERYGDEEGEELSITVTGHSLGGALAVLSAYDVAEMGVNRTRKGKVIPVTAFTYGGPRVGNIRFKERIEKLGVKVLRVVNEHDVVAKSPGLFLNERAPQALMKLAGGLPWCYSHVGEMLPLDHQKSPFLKPTVDLSTAHNLEALLHLLDGYHGKGQRFVLSSGRDPALVNKASDFLKDHFMVPPYWRQDANKGMVRNTDGRWIQPDRIRADDQHAPDIHQLLTQLHHPSQLL |
| Enzyme Length | 515 |
| Uniprot Accession Number | Q941F1 |
| Absorption | |
| Active Site | ACT_SITE 303; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 366; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 422; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488; Evidence={ECO:0000269|PubMed:19527719}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + H2O = a fatty acid + an acyl-3-O-(beta-D-galactosyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:57084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:28868, ChEBI:CHEBI:141434; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57085; 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.- |
| Enzyme Function | FUNCTION: Acylhydrolase with a broad specificity. Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG). May display dual sn-1/sn-2 substrate specificity. Could be involved in early wound response. {ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:20348210}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Chain (1); Motif (1); Transit peptide (1) |
| Keywords | Alternative splicing;Chloroplast;Hydrolase;Lipid degradation;Lipid metabolism;Plastid;Reference proteome;Transit peptide |
| Interact With | |
| Induction | INDUCTION: Not induced by wounding (PubMed:18267087). Induced by wounding (PubMed:24430866). {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:24430866}. |
| Subcellular Location | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19527719}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16299169; 20855949; 23505340; 29666162; |
| Motif | MOTIF 301..305; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:Q948R1 |
| Gene Encoded By | |
| Mass | 58,445 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:40487; RHEA:40488; RHEA:57084; RHEA:57085; RHEA:48372; RHEA:48373 |
| Cross Reference Brenda |