| IED ID | IndEnz0005000984 |
| Enzyme Type ID | lipase000984 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | lip lipA |
| Organism | Pseudarthrobacter phenanthrenivorans (Arthrobacter phenanthrenivorans) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Micrococcales Micrococcaceae Pseudarthrobacter Pseudarthrobacter phenanthrenivorans (Arthrobacter phenanthrenivorans) |
| Enzyme Sequence | ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV |
| Enzyme Length | 319 |
| Uniprot Accession Number | P0DUB9 |
| Absorption | |
| Active Site | ACT_SITE 87; /note=Nucleophile; /evidence=ECO:0000305|PubMed:8683577; ACT_SITE 263; /note=Charge relay system; /evidence=ECO:0000305|PubMed:8683577; ACT_SITE 285; /note=Charge relay system; /evidence=ECO:0000305|PubMed:8683577 |
| Activity Regulation | |
| Binding Site | BINDING 17; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088; BINDING 88; /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:7786905}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {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); Sequence conflict (1); Sequence uncertainty (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DUB8}. Note=Correct periplasmic folding, necessary for secretion, requires the lipase-specific foldase LifO. Secretion probably occurs via a type II secretion system. {ECO:0000250|UniProtKB:P0DUB8}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1CVL; 1QGE; |
| Mapped Pubmed ID | 8405390; |
| Motif | |
| Gene Encoded By | |
| Mass | 33,092 |
| Kinetics | |
| Metal Binding | METAL 241; /note="Calcium"; /evidence="ECO:0000269|PubMed:8683577, ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"; METAL 287; /note="Calcium"; /evidence="ECO:0000269|PubMed:8683577, ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"; METAL 291; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8683577, ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE"; METAL 295; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:8683577, ECO:0007744|PDB:1CVL, ECO:0007744|PDB:1QGE" |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |