| IED ID | IndEnz0010000984 |
| Enzyme Type ID | esterase000984 |
| Protein Name |
Carboxylesterase/phospholipase LipF EC 3.1.1.1 EC 3.1.4.3 |
| Gene Name | lipF MT3591 |
| Organism | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| Enzyme Sequence | MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI |
| Enzyme Length | 373 |
| Uniprot Accession Number | Q7D5F9 |
| Absorption | |
| Active Site | ACT_SITE 186; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 285; /evidence=ECO:0000250|UniProtKB:O06350; ACT_SITE 315; /evidence=ECO:0000250|UniProtKB:O06350 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000250|UniProtKB:O06350}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; Evidence={ECO:0000250|UniProtKB:O06350};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605; Evidence={ECO:0000250|UniProtKB:O06350}; |
| DNA Binding | |
| EC Number | 3.1.1.1; 3.1.4.3 |
| Enzyme Function | FUNCTION: A short-chain esterase and phospholipase. {ECO:0000250|UniProtKB:O06350}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Erroneous initiation (1); Motif (1) |
| Keywords | Hydrolase;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Induced by acidic conditions (PubMed:12595455, PubMed:17434691). Induction levels are the same at pH 4.5 and pH 5.0 and decrease as the pH approaches 6.4. No induction is seen at higher pH, nor by oxidative, hypoxic or temperature stress (PubMed:17869077). Induction is maximal after 22 hours exposure to acid. Induction does not depend on sigF, and does not seem to occur in activated murine macrophages (PubMed:12595455). {ECO:0000269|PubMed:12595455, ECO:0000269|PubMed:17434691, ECO:0000269|PubMed:17869077}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 116..118; /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 | 39,611 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21164; RHEA:10604; RHEA:10605 |
| Cross Reference Brenda |