IED ID | IndEnz0010000402 |
Enzyme Type ID | esterase000402 |
Protein Name |
Carboxylesterase Culp1 EC 3.1.1.- Cutinase-like protein 1 Culp1 |
Gene Name | MT2037 |
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 | MTPRSLVRIVGVVVATTLALVSAPAGGRAAHADPCSDIAVVFARGTHQASGLGDVGEAFVDSLTSQVGGRSIGVYAVNYPASDDYRASASNGSDDASAHIQRTVASCPNTRIVLGGYSQGATVIDLSTSAMPPAVADHVAAVALFGEPSSGFSSMLWGGGSLPTIGPLYSSKTINLCAPDDPICTGGGNIMAHVSYVQSGMTSQAATFAANRLDHAG |
Enzyme Length | 217 |
Uniprot Accession Number | P9WP42 |
Absorption | |
Active Site | ACT_SITE 118; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P9WP43; ACT_SITE 181; /evidence=ECO:0000250|UniProtKB:P9WP43; ACT_SITE 193; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:P9WP43 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000250|UniProtKB:P9WP43};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59389; Evidence={ECO:0000250|UniProtKB:P9WP43}; |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | FUNCTION: Shows esterase activity, with a preference for short- and medium-chain fatty acids. {ECO:0000250|UniProtKB:P9WP43}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1); Site (1) |
Keywords | Disulfide bond;Hydrolase;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WP43}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..32; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 21,782 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:59388; RHEA:59389 |
Cross Reference Brenda |