Detail Information for IndEnz0005000682
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;