IED ID | IndEnz0005000412 |
Enzyme Type ID | lipase000412 |
Protein Name |
Esterase TesA EC 3.1.1.1 |
Gene Name | tesA PA2856 |
Organism | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas aeruginosa group Pseudomonas aeruginosa Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Enzyme Sequence | MRALLLSGCLALVLLTQQAAAQTLLVVGDSISAALGLDTSQGWVALLQKRLADEGYDYRVVNASISGDTSAGGLARLPALLAEEKPALVVIELGGNDGLRGMAPAQLQQNLASMAQKARAEGAKVLLLGIQLPPNYGPRYIEAFSRVYGAVAAQEKTALVPFFLEGVGGVQGMMQADGIHPALAAQPRLLENVWPTLKPLL |
Enzyme Length | 201 |
Uniprot Accession Number | Q9HZY8 |
Absorption | |
Active Site | ACT_SITE 30; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 177; /evidence=ECO:0000250; ACT_SITE 180; /evidence=ECO:0000250 |
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:0000269|PubMed:20931591}; |
DNA Binding | |
EC Number | 3.1.1.1 |
Enzyme Function | FUNCTION: Esterase that exhibits the highest activity towards Tween detergents and p-nitrophenyl esters of short acyl chain length. Also displays a low thioesterase activity towards palmitoyl-coenzyme A, but is not active towards acetyl-coenzyme A. {ECO:0000269|PubMed:20931591}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (6); Chain (1); Helix (11); Signal peptide (1); Turn (3) |
Keywords | 3D-structure;Hydrolase;Reference proteome;Secreted;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 4JGG; |
Mapped Pubmed ID | 23874889; |
Motif | |
Gene Encoded By | |
Mass | 21,038 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.0 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:20931591}; Vmax=37 umol/min/mg enzyme with p-nitrophenyl butyrate as substrate {ECO:0000269|PubMed:20931591}; |
Metal Binding | |
Rhea ID | RHEA:21164 |
Cross Reference Brenda |