| IED ID | IndEnz0005001216 |
| Enzyme Type ID | lipase001216 |
| Protein Name |
Acetyl esterase EC 3.1.1.- |
| Gene Name | aes EcE24377A_0514 |
| Organism | Escherichia coli O139:H28 (strain E24377A / ETEC) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O139:H28 Escherichia coli O139:H28 (strain E24377A / ETEC) |
| Enzyme Sequence | MKPENKLPVLDLISAEMKTVVNTLQSDLPSWPATGTIAEQRQYYTLERRFWNAGAPEMATRAYMVPTKYGQVETRLFCPQPDSPATLFYLHGGGFILGNLDTHDRIMRLLASYSQCTVIGIDYPLSPEARFPQAIEEIVAACCYFHQQAEDYQINMSRIGFAGDSAGAMLTLASALWLRDKQIDCGKIAGVLLWYGLYGLRDSVTRRLLGGVWDGLTQQDLQMYEEAYLSNDADRESPYYCLFNNDLTREVPPCFIAGAEFDPLLDDSRLLYQTLAAHQQPCEFKLYPGTLHAFLHYSRMMKTADEALRDGAQFFTAQL |
| Enzyme Length | 319 |
| Uniprot Accession Number | A7ZIN6 |
| Absorption | |
| Active Site | ACT_SITE 165; /evidence=ECO:0000255|HAMAP-Rule:MF_01958; ACT_SITE 262; /evidence=ECO:0000255|HAMAP-Rule:MF_01958; ACT_SITE 292; /evidence=ECO:0000255|HAMAP-Rule:MF_01958 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Displays esterase activity towards short chain fatty esters (acyl chain length of up to 8 carbons). Able to hydrolyze triacetylglycerol (triacetin) and tributyrylglycerol (tributyrin), but not trioleylglycerol (triolein) or cholesterol oleate. Negatively regulates MalT activity by antagonizing maltotriose binding. Inhibits MelA galactosidase activity. {ECO:0000255|HAMAP-Rule:MF_01958}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Motif (1) |
| Keywords | Cytoplasm;Hydrolase;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01958}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 91..93; /note=Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole; /evidence=ECO:0000250|UniProtKB:Q5NUF3 |
| Gene Encoded By | |
| Mass | 36,054 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |