| IED ID | IndEnz0010001185 |
| Enzyme Type ID | esterase001185 |
| Protein Name |
Phospholipase Culp4 EC 3.1.1.- Cutinase-like protein 4 Culp4 |
| Gene Name | cut4 Rv3452 |
| 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 | MIPRPQPHSGRWRAGAARRLTSLVAAAFAAATLLLTPALAPPASAGCPDAEVVFARGTGEPPGLGRVGQAFVSSLRQQTNKSIGTYGVNYPANGDFLAAADGANDASDHIQQMASACRATRLVLGGYSQGAAVIDIVTAAPLPGLGFTQPLPPAADDHIAAIALFGNPSGRAGGLMSALTPQFGSKTINLCNNGDPICSDGNRWRAHLGYVPGMTNQAARFVASRI |
| Enzyme Length | 226 |
| Uniprot Accession Number | O06319 |
| Absorption | |
| Active Site | ACT_SITE 128; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:O53581; ACT_SITE 195; /evidence=ECO:0000250|UniProtKB:O53581; ACT_SITE 207; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:O53581 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by high concentrations of paraoxon (PubMed:19225166). Inhibited by tetrahydrolipstatin (THL), a specific lipase inhibitor (PubMed:20103719). {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000269|PubMed:20103719}; 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:19225166, ECO:0000269|PubMed:20103719};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}; |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: A2-type phospholipase, which is probably involved in the degradation of macrophage membrane (PubMed:20103719). Hydrolyzes dipalmitoylphosphatidylcholine (PubMed:20103719). Also shows moderate esterase activity and hydrolyzes the p-nitrophenol-linked aliphatic ester pNP-butyrate (C4) (PubMed:19225166, PubMed:20103719). Does not exhibit cutinase activity (PubMed:19225166). {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (2); Signal peptide (1); Site (1) |
| Keywords | Cell membrane;Cell wall;Disulfide bond;Hydrolase;Membrane;Reference proteome;Secreted;Serine esterase;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17416658}. Secreted, cell wall {ECO:0000269|PubMed:17416658}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..45; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 23,113 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:41223; RHEA:41224; RHEA:47348; RHEA:47349 |
| Cross Reference Brenda |