Detail Information for IndEnz0005000092
IED ID IndEnz0005000092
Enzyme Type ID lipase000092
Protein Name Phospholipase A1-Igamma2, chloroplastic
EC 3.1.1.-
DAD1-like lipase 3
Gene Name DALL3 At2g30550 T6B20.10
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 MAAIPSHNNLLTINHKNSITGSSSLNTNFSEINFPAKFRVATRALSRTDESSLSAVISRLERERRERQGLLIEEAEGAGELWMTAEDIRRRDKKTEEERRLRDTWRKIQGEDDWAGLMDPMDPILRSELIRYGEMAQACYDAFDFDPASKYCGTSRFTRLEFFDSLGMIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDETSRNRLGRRDIAIAWRGTVTKLEWIADLKDYLKPVTENKIRCPDPAVKVESGFLDLYTDKDTTCKFARFSAREQILTEVKRLVEEHGDDDDSDLSITVTGHSLGGALAILSAYDIAEMRLNRSKKGKVIPVTVLTYGGPRVGNVRFRERMEELGVKVMRVVNVHDVVPKSPGLFLNESRPHALMKIAEGLPWCYSHVGEELALDHQNSPFLKPSVDVSTAHNLEAMLHLLDGYHGKGERFVLSSGRDHALVNKASDFLKEHLQIPPFWRQDANKGMVRNSEGRWIQAERLRFEDHHSPDIHHHLSQLRLDHPC
Enzyme Length 529
Uniprot Accession Number Q3EBR6
Absorption
Active Site ACT_SITE 318; /note=Acyl-ester intermediate; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 381; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q948R1; ACT_SITE 437; /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}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:19527719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; Evidence={ECO:0000269|PubMed:19527719};
DNA Binding
EC Number 3.1.1.-
Enzyme Function FUNCTION: Acylhydrolase with broad specificity (PubMed:19527719). Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position (PubMed:19527719). Possesses moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG) (PubMed:19527719). {ECO:0000269|PubMed:19527719}.
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: Slightly induced by wounding (PubMed:18267087). Induced by wounding (PubMed:24430866, PubMed:31928671). Induced by cadmium and selenium in roots (PubMed:31928671). {ECO:0000269|PubMed:18267087, ECO:0000269|PubMed:24430866, ECO:0000269|PubMed:31928671}.
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:19527719, ECO:0000269|PubMed:31928671}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11595796; 14682612; 15047898; 15235117; 15489280; 15728340; 16284313; 16299169; 17181774; 18650403; 18775970; 18805951; 23505340; 29666162;
Motif MOTIF 316..320; /note=GXSXG; /evidence=ECO:0000250|UniProtKB:Q948R1
Gene Encoded By
Mass 60,402
Kinetics
Metal Binding
Rhea ID RHEA:40487; RHEA:40488; RHEA:57084; RHEA:57085; RHEA:48372; RHEA:48373; RHEA:12044; RHEA:12045
Cross Reference Brenda