| IED ID | IndEnz0010001050 |
| Enzyme Type ID | esterase001050 |
| Protein Name |
Phosphotriesterase homology protein EC 3.1.-.- |
| Gene Name | php yhfV b3379 JW3342 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSFDPTGYTLAHEHLHIDLSGFKNNVDCRLDQYAFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGIDGTELKAGIIAEIGTSEGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQLALLQAHGVDLSRVTVGHCDLKDNLDNILKMIDLGAYVQFDTIGKNSYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDYLLTTFIPQLRQSGFSQADVDVMLRENPSQFFQ |
| Enzyme Length | 292 |
| Uniprot Accession Number | P45548 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activity is higher in the enzyme containing Mn(2+) than that containing Zn(2+). {ECO:0000269|PubMed:30277746}. |
| Binding Site | BINDING 280; /note="Beta-D-glucose"; /evidence="ECO:0000269|PubMed:30277746, ECO:0007744|PDB:4LEF"; BINDING 284; /note="Beta-D-glucose"; /evidence="ECO:0000269|PubMed:30277746, ECO:0007744|PDB:4LEF" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.-.- |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of phosphorylated glyceryl acetates in which the presence of a phosphate group is required for the enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative suggesting it acts on phosphoglycerol substrates with a butyrate leaving group. Also active with aromatic acetates and propionates. No activity with various sugar phosphates, with various nitrophenylphosphate or nitrophenylphosphonate derivatives, or with phosphorylated or non-phosphorylated sugar lactones tested. Does not hydrolyze non-phosphorylated carboxyesters with long chain leaving groups (PubMed:30277746). No general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities detected when tested with the following non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate (PubMed:9548740). {ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (9); Binding site (2); Chain (1); Helix (21); Metal binding (7); Region (2); Turn (1) |
| Keywords | 3D-structure;Direct protein sequencing;Hydrolase;Metal-binding;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1BF6; 4LEF; |
| Mapped Pubmed ID | 16606699; 30277746; |
| Motif | |
| Gene Encoded By | |
| Mass | 32,915 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 mM for 2-naphthyl acetate (in the presence of 1.0 mM MnCl(2), at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:30277746}; KM=5.5 mM for (2S)-1,2-diacetyl glycerol-3-phosphate (in the presence of 1.0 mM MnCl(2), at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:30277746}; KM=6.0 mM for rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate (in the presence of 1.0 mM MnCl(2), at pH 8.0 and 30 degrees Celsius) {ECO:0000269|PubMed:30277746}; Note=kcat is 2.5 sec(-1) with 2-naphthyl acetate as substrate. kcat is 27 sec(-1) with (2S)-1,2-diacetyl glycerol-3-phosphate as substrate. kcat is 28 sec(-1) with rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate as substrate. {ECO:0000269|PubMed:30277746}; |
| Metal Binding | METAL 12; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 14; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 125; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 125; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 158; /note="Zinc 2; via pros nitrogen"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 186; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF"; METAL 243; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:30277746, ECO:0000269|PubMed:9548740, ECO:0007744|PDB:1BF6, ECO:0007744|PDB:4LEF" |
| Rhea ID | |
| Cross Reference Brenda |