| IED ID | IndEnz0005000521 |
| Enzyme Type ID | lipase000521 |
| Protein Name |
Triacylglycerol lipase EC 3.1.1.3 Extracellular lipase Triacylglycerol ester hydrolase |
| Gene Name | hlyC lipA VC_A0221 |
| Organism | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio cholerae Vibrio cholerae O1 Vibrio cholerae O1 biovar El Tor Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
| Enzyme Sequence | MNKIIILIALSLFSSSIWAGTSAHALSQQGYTQTRYPIVLVHGLFGFDTLAGMDYFHGIPQSLTRDGAQVYVAQVSATNSSERRGEQLLAQVESLLAVTGAKKVNLIGHSHGGPTIRYVASVRPDLVASVTSIGGVHKGSAVADLVRGVIPSGSVSEQVAVGLTQGLVALIDLLSGGKAHPQDPLASLAALTTEGSLKFNQYYPEGVPTSACGEGAYQVNGVRYYSWSGAATVTNILDPSDVAMGLIGLVFNEPNDGLVATCSTHLGKVIRDDYRMNHLDEINGLLGIHSLFETDPVTLYRQHANRLKQAGL |
| Enzyme Length | 312 |
| Uniprot Accession Number | P15493 |
| Absorption | |
| Active Site | ACT_SITE 110; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 256; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876; ACT_SITE 278; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P26876 |
| Activity Regulation | |
| Binding Site | BINDING 44; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P22088; BINDING 111; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P26876 |
| 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:0000250|UniProtKB:P26876}; |
| DNA Binding | |
| EC Number | 3.1.1.3 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {ECO:0000269|PubMed:9371455, ECO:0000305|PubMed:8817490}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (2); Chain (1); Disulfide bond (1); Domain (1); Erroneous initiation (1); Metal binding (4); Signal peptide (1) |
| Keywords | Calcium;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: During infection. {ECO:0000269|PubMed:8817490}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26876}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 32,995 |
| Kinetics | |
| Metal Binding | METAL 238; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 280; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P26876; METAL 284; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P26876; METAL 288; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P26876 |
| Rhea ID | RHEA:12044 |
| Cross Reference Brenda |