| IED ID | IndEnz0005001429 |
| Enzyme Type ID | lipase001429 |
| Protein Name |
Probable N-octanoylanthranilate hydrolase AqdA2 EC 3.5.1.- |
| Gene Name | aqdA2 XU06_29730 |
| Organism | Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Nocardiaceae Rhodococcus Rhodococcus erythropolis group Rhodococcus erythropolis (Arthrobacter picolinophilus) |
| Enzyme Sequence | MFQTVTAPTGVWRGRVTGDVTVFHGIQYARADRFAPPQRCEPQLQHLVEVPEPGPIAPQSPSRLEGVMGAPSSLKQSEACLTVTVTTPHLAQPGSLPVLVWLHGGAFLSGSGAWEQYGAEQLVRETGIVVVSVNYRLGVLGYLCAPGISSGNLGLLDQITALEWVRDNIEAFGGDNGRVTLDGQSAGAHSIVAMLGIDRARSLFSRAIIQSAPLGLGFHSVEQARRAAEIFEEELGSDPRRAVVTDILAAQARTAHRLAGRGAMNSAPPFLPVHGMAPLPFVGEWNGKVAANAARRKILIGNTRDEMAAFFGPHPVFSAMRRVPLAGPQLAGAIQRRVQKVVFDNPVQEFADRFASAGASVWRYGIGPLHPDNPFGACHCIDIPLLFGDGDTWRDAPMLRPLSPKEIGESGTRTRRYWGEFVHTGRISDPAWPMHRPKSRYAHLLTDETIGGSA |
| Enzyme Length | 454 |
| Uniprot Accession Number | A0A0E4AET8 |
| Absorption | |
| Active Site | ACT_SITE 185; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 306; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141; ACT_SITE 379; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P23141 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=H2O + N-octanoylanthranilate = anthranilate + H(+) + octanoate; Xref=Rhea:RHEA:60356, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:25646, ChEBI:CHEBI:143722; Evidence={ECO:0000305|PubMed:26319870};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60357; Evidence={ECO:0000305|PubMed:26319870}; |
| DNA Binding | |
| EC Number | 3.5.1.- |
| Enzyme Function | FUNCTION: Involved in the degradation of the Pseudomonas aeruginosa quorum sensing signal molecules HHQ (2-heptyl-4-quinolone) and PQS (2-heptyl-3-hydroxy-4-quinolone) to anthranilic acid. Probably catalyzes the hydrolysis of N-octanoylanthranilic acid to anthranilic acid. {ECO:0000269|PubMed:26319870}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Hydrolase;Plasmid |
| Interact With | |
| Induction | INDUCTION: Up-regulated by PQS. {ECO:0000269|PubMed:26319870}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | Plasmid pRLCBG43 |
| Mass | 48,937 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:60356; RHEA:60357 |
| Cross Reference Brenda |