IED ID | IndEnz0010000387 |
Enzyme Type ID | esterase000387 |
Protein Name |
Esterase FrsA EC 3.1.1.1 |
Gene Name | frsA VV1_0328 |
Organism | Vibrio vulnificus (strain CMCP6) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Vibrionales Vibrionaceae Vibrio Vibrio vulnificus Vibrio vulnificus (strain CMCP6) |
Enzyme Sequence | MSEEVSKNLSETLFVKHKQAKETSALTQYMPTSQSLLDEIKEKNGFSWYRNLRRLQWVWQGVDPIEQEQVLARIASSKHSRTDEQWLDTVMGYHSGNWAYEWTRLGMEHQKRAGEMTNEAASEALFSASLCYSIAGYPHLKSDNLAIQAQVLANSAYLEAAKKSKYIIKQLEIPFEKGKITAHLHLTNTDKPHPVVIVSAGLDSLQTDMWRLFRDHLAKHDIAMLTVDMPSVGYSSKYPLTEDYSRLHQAVLNELFSIPYVDHHRVGLIGFRFGGNAMVRLSFLEQEKIKACVILGAPIHDIFASPQKLQQMPKMYLDVLASRLGKSVVDIYSLSGQMAAWSLKVQGFLSSRKTKVPILAMSLEGDPVSPYSDNQMVAFFSTYGKAKKISSKTITQGYEQSLDLAIKWLEDELLR |
Enzyme Length | 415 |
Uniprot Accession Number | Q8DF91 |
Absorption | |
Active Site | |
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:0000255|HAMAP-Rule:MF_01063, ECO:0000269|PubMed:30951551}; |
DNA Binding | |
EC Number | 3.1.1.1 |
Enzyme Function | FUNCTION: Catalyzes the hydrolysis of esters (PubMed:30951551). In vitro, prefers short chain alkanoate ester as substrate. Displays highest activity towards p-nitrophenyl acetate (pNPA). Has weaker activity towards p-nitrophenyl butyrate (pNPB) (PubMed:30951551). {ECO:0000269|PubMed:30951551}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:30951551}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0-9.5. {ECO:0000269|PubMed:30951551}; |
Pathway | |
nucleotide Binding | |
Features | Beta strand (14); Chain (1); Helix (22); Turn (2) |
Keywords | 3D-structure;Hydrolase;Serine esterase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 3MVE; 3OUR; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 47,013 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.6 mM for pNPA {ECO:0000269|PubMed:30951551}; Note=kcat is 0.67 sec(-1) with pNPA as substrate. {ECO:0000269|PubMed:30951551}; |
Metal Binding | |
Rhea ID | RHEA:21164 |
Cross Reference Brenda |