IED ID | IndEnz0005000688 |
Enzyme Type ID | lipase000688 |
Protein Name |
Para-nitrobenzyl esterase EC 3.1.1.- Intracellular esterase B PNB carboxy-esterase PNBCE |
Gene Name | pnbA estB BSU34390 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MTHQIVTTQYGKVKGTTENGVHKWKGIPYAKPPVGQWRFKAPEPPEVWEDVLDATAYGSICPQPSDLLSLSYTELPRQSEDCLYVNVFAPDTPSKNLPVMVWIHGGAFYLGAGSEPLYDGSKLAAQGEVIVVTLNYRLGPFGFLHLSSFNEAYSDNLGLLDQAAALKWVRENISAFGGDPDNVTVFGESAGGMSIAALLAMPAAKGLFQKAIMESGASRTMTKEQAASTSAAFLQVLGINEGQLDKLHTVSAEDLLKAADQLRIAEKENIFQLFFQPALDPKTLPEEPEKAIAEGAASGIPLLIGTTRDEGYLFFTPDSDVHSQETLDAALEYLLGKPLAEKVADLYPRSLESQIHMMTDLLFWRPAVAYASAQSHYAPVWMYRFDWHPKKPPYNKAFHALELPFVFGNLDGLERMAKAEITDEVKQLSHTIQSAWITFAKTGNPSTEAVNWPAYHEETRETLILDSEITIENDPESEKRQKLFPSKGE |
Enzyme Length | 489 |
Uniprot Accession Number | P37967 |
Absorption | |
Active Site | ACT_SITE 189; /note=Acyl-ester intermediate; /evidence=ECO:0000255|PROSITE-ProRule:PRU10039; ACT_SITE 310; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 399; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.1.1.- |
Enzyme Function | FUNCTION: Catalyzes hydrolysis of several beta-lactam antibiotic PNB esters to the corresponding free acid and PNB alcohol. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (15); Chain (1); Helix (23); Modified residue (1); Natural variant (11); Sequence conflict (1); Turn (8) |
Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Phosphoprotein;Reference proteome;Serine esterase |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 189; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:17218307 |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (3) |
Cross Reference PDB | 1C7I; 1C7J; 1QE3; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 53,986 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.1.1.1; |