| IED ID | IndEnz0010000111 |
| Enzyme Type ID | esterase000111 |
| Protein Name |
Esterase Rv1288 EC 3.1.1.- |
| Gene Name | Rv1288 MTCY373.07 |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| 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 ATCC 25618 / H37Rv) |
| Enzyme Sequence | MVSTHAVVAGETLSALALRFYGDAELYRLIAAASGIADPDVVNVGQRLIMPDFTRYTVVAGDTLSALALRFYGDAELNWLIAAASGIADPDVVNVGQRLIMPDFTRYTVVAGDTLSALAARFYGDASLYPLIAAVNGIADPGVIDVGQVLVIFIGRSDGFGLRIVDRNENDPRLWYYRFQTSAIGWNPGVNVLLPDDYRTSGRTYPVLYLFHGGGTDQDFRTFDFLGIRDLTAGKPIIIVMPDGGHAGWYSNPVSSFVGPRNWETFHIAQLLPWIEANFRTYAEYDGRAVAGFSMGGFGALKYAAKYYGHFASASSHSGPASLRRDFGLVVHWANLSSAVLDLGGGTVYGAPLWDQARVSADNPVERIDSYRNKRIFLVAGTSPDPANWFDSVNETQVLAGQREFRERLSNAGIPHESHEVPGGHVFRPDMFRLDLDGIVARLRPASIGAAAERAD |
| Enzyme Length | 456 |
| Uniprot Accession Number | P9WM39 |
| Absorption | |
| Active Site | ACT_SITE 294; /evidence=ECO:0000305|PubMed:30560095; ACT_SITE 391; /evidence=ECO:0000305|PubMed:30560095; ACT_SITE 425; /evidence=ECO:0000305|PubMed:30560095 |
| 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:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; Evidence={ECO:0000269|PubMed:30560095}; CATALYTIC ACTIVITY: Reaction=a tetradecanoate ester + H2O = an aliphatic alcohol + H(+) + tetradecanoate; Xref=Rhea:RHEA:47388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:87691; Evidence={ECO:0000269|PubMed:30560095}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Exhibits lipolytic activity with medium chain length esters as optimum substrates (PubMed:30560095). In vitro, pNP-caprylate (C8) is the optimum substrate followed by pNP-capricate (C10) (PubMed:30560095). May modulate the cell wall lipids to favor the survival of bacteria under stress conditions (PubMed:30560095). {ECO:0000269|PubMed:30560095}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. {ECO:0000269|PubMed:30560095}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:30560095}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (3); Mutagenesis (3) |
| Keywords | Cell wall;Hydrolase;Lipid metabolism;Reference proteome;Repeat;Secreted;Serine esterase |
| Interact With | |
| Induction | INDUCTION: Expression is up-regulated under nutrient depletion condition. {ECO:0000269|PubMed:30560095}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:30560095}. Note=Cell wall anchored. Binds peptidoglycans via the LytM domains. {ECO:0000269|PubMed:30560095}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,619 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for pNP-caprylate {ECO:0000269|PubMed:30560095}; Note=kcat is 2 min(-1) with pNP-caprylate as substrate. {ECO:0000269|PubMed:30560095}; |
| Metal Binding | |
| Rhea ID | RHEA:59388; RHEA:47356; RHEA:47360; RHEA:47364; RHEA:47348; RHEA:12957; RHEA:47388 |
| Cross Reference Brenda |