| IED ID | IndEnz0005000405 |
| Enzyme Type ID | lipase000405 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | lip lipA |
| Organism | Burkholderia plantarii |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia plantarii |
| Enzyme Sequence | MVRSMRSRVAARAVAWALAVMPLAGAAGLTMAASPAAVAADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV |
| Enzyme Length | 358 |
| Uniprot Accession Number | P0DUB8 |
| Absorption | |
| Active Site | ACT_SITE 126; /note="Nucleophile"; /evidence="ECO:0000269|PubMed:1476423, ECO:0000305|PubMed:8405390"; ACT_SITE 302; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:1476423, ECO:0000305|PubMed:8405390"; ACT_SITE 324; /note="Charge relay system"; /evidence="ECO:0000269|PubMed:1476423, ECO:0000305|PubMed:8405390" |
| Activity Regulation | |
| Binding Site | BINDING 56; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088; BINDING 127; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088 |
| Calcium Binding | |
| catalytic Activity | 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; EC=3.1.1.3; Evidence={ECO:0000305|PubMed:1476423}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {ECO:0000269|PubMed:1476423, ECO:0000269|PubMed:7786905}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (13); Binding site (2); Chain (1); Disulfide bond (1); Domain (1); Helix (14); Metal binding (4); Mutagenesis (8); Signal peptide (1); Turn (5) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal |
| Interact With | Q05490 |
| Induction | INDUCTION: By growth on olive oil or oleic acid; part of the lip-lifO (also called lipA-lipB) operon. {ECO:0000269|PubMed:8412704}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:1476423, ECO:0000305|PubMed:8412704}. Note=Correct periplasmic folding, necessary for secretion, requires the lipase-specific foldase LifO (also called lipB). Secretion probably occurs via a type II secretion system. {ECO:0000269|PubMed:8412705, ECO:0000305|PubMed:8412704}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000269|PubMed:1476423 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1TAH; 2ES4; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 36,929 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for oil emulsion {ECO:0000269|PubMed:1476423}; Vmax=4 umol/min/mg enzyme {ECO:0000269|PubMed:1476423}; |
| Metal Binding | METAL 280; /note="Calcium"; /evidence="ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH, ECO:0007744|PDB:2ES4"; METAL 326; /note="Calcium"; /evidence="ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH, ECO:0007744|PDB:2ES4"; METAL 330; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH, ECO:0007744|PDB:2ES4"; METAL 334; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:16518399, ECO:0000269|PubMed:8405390, ECO:0007744|PDB:1TAH, ECO:0007744|PDB:2ES4" |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |