| IED ID | IndEnz0005000682 |
| Enzyme Type ID | lipase000682 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | lip lipA |
| Organism | Burkholderia cepacia (Pseudomonas cepacia) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Betaproteobacteria Burkholderiales Burkholderiaceae Burkholderia Burkholderia cepacia complex Burkholderia cepacia (Pseudomonas cepacia) |
| Enzyme Sequence | MARTMRSRVVAGAVACAMSIAPFAGTTAVMTLATTHAAMAATAPAAGYAATRYPIILVHGLSGTDKYAGVLEYWYGIQEDLQQNGATVYVANLSGFQSDDGPNGRGEQLLAYVKTVLAATGATKVNLVGHSQGGLSSRYVAAVAPDLVASVTTIGTPHRGSEFADFVQDVLAYDPTGLSSSVIAAFVNVFGILTSSSHNTNQDALAALQTLTTARAATYNQNYPSAGLGAPGSCQTGAPTETVGGNTHLLYSWAGTAIQPTLSVFGVTGATDTSTLPLVDPANVLDLSTLALFGTGTVMINRGSGQNDGLVSKCSALYGKVLSTSYKWNHLDEINQLLGVRGAYAEDPVAVIRTHANRLKLAGV |
| Enzyme Length | 364 |
| Uniprot Accession Number | P22088 |
| Absorption | |
| Active Site | ACT_SITE 131; /note="Nucleophile"; /evidence="ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:15850979, ECO:0000305|PubMed:18386861, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP"; ACT_SITE 308; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP"; ACT_SITE 330; /note="Charge relay system"; /evidence="ECO:0000305|PubMed:11453990, ECO:0000305|PubMed:9032073, ECO:0000305|PubMed:9032074, ECO:0000305|PubMed:9660188, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by RC-(Rp,Sp)- and SC-(Rp,Sp)-1,2-dioctylcarbamoylglycero-3-O-p-nitrophenyl octylphosphonate (PubMed:9660188). Also inhibited by diethyl-p-nitrophenylphosphate (E600) (PubMed:1856176). {ECO:0000269|PubMed:1856176, ECO:0000269|PubMed:9660188}. |
| Binding Site | BINDING 61; /note="Substrate; via amide nitrogen"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP"; BINDING 132; /note="Substrate; via amide nitrogen"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:4LIP" |
| 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:1856176, ECO:0000305|PubMed:7522571}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. It shows a preference for triacylglycerols with a chain length between 6 and 12 carbons. {ECO:0000269|PubMed:1856176, ECO:0000269|PubMed:7522571}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (15); Binding site (2); Chain (1); Disulfide bond (1); Domain (1); Helix (13); Metal binding (4); 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 | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q05489}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..44; /evidence="ECO:0000269|PubMed:1856176, ECO:0000269|PubMed:1987151, ECO:0000269|PubMed:7522571" |
| Structure 3D | X-ray crystallography (9) |
| Cross Reference PDB | 1HQD; 1OIL; 1YS1; 1YS2; 2LIP; 2NW6; 3LIP; 4LIP; 5LIP; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,494 |
| Kinetics | |
| Metal Binding | METAL 286; /note="Calcium"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP"; METAL 332; /note="Calcium"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP"; METAL 336; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP"; METAL 340; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:11453990, ECO:0000269|PubMed:15850979, ECO:0000269|PubMed:18386861, ECO:0000269|PubMed:9032073, ECO:0000269|PubMed:9032074, ECO:0000269|PubMed:9660188, ECO:0007744|PDB:1HQD, ECO:0007744|PDB:1OIL, ECO:0007744|PDB:1YS1, ECO:0007744|PDB:1YS2, ECO:0007744|PDB:2LIP, ECO:0007744|PDB:2NW6, ECO:0007744|PDB:3LIP, ECO:0007744|PDB:4LIP, ECO:0007744|PDB:5LIP" |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda | 3.1.1.3; |