| IED ID | IndEnz0010000428 |
| Enzyme Type ID | esterase000428 |
| Protein Name |
Parathion hydrolase EC 3.1.8.1 Phosphotriesterase PTE |
| Gene Name | opd |
| Organism | Brevundimonas diminuta (Pseudomonas diminuta) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Caulobacterales Caulobacteraceae Brevundimonas Brevundimonas diminuta (Pseudomonas diminuta) |
| Enzyme Sequence | MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS |
| Enzyme Length | 365 |
| Uniprot Accession Number | P0A434 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; |
| DNA Binding | |
| EC Number | 3.1.8.1 |
| Enzyme Function | FUNCTION: Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (16); Chain (1); Frameshift (1); Helix (26); Metal binding (7); Modified residue (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Direct protein sequencing;Hydrolase;Membrane;Metal-binding;Plasmid;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. |
| Modified Residue | MOD_RES 169; /note="N6-carboxylysine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00679, ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" |
| Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. |
| Signal Peptide | SIGNAL 1..29; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|Ref.1" |
| Structure 3D | X-ray crystallography (55) |
| Cross Reference PDB | 1DPM; 1EYW; 1EZ2; 1HZY; 1I0B; 1I0D; 1JGM; 1PSC; 1PTA; 1QW7; 2O4M; 2O4Q; 2OB3; 2OQL; 3CAK; 3CS2; 3E3H; 3UPM; 3UR2; 3UR5; 3URA; 3URB; 3URN; 3URQ; 4E3T; 4GY0; 4GY1; 4ZST; 4ZSU; 5W6B; 5WCQ; 6AML; 6FEE; 6FEF; 6FEI; 6FEV; 6FFW; 6FOR; 6FQE; 6FRZ; 6FS3; 6FU0; 6FU6; 6FVK; 6FVP; 6FW1; 6FWE; 6G0M; 6G1J; 6G23; 6G3L; 6G3M; 6GBJ; 6GBK; 6GBL; |
| Mapped Pubmed ID | 10871616; 11258882; 16188223; 18434422; 18702530; 22809162; 23212386; 26274608; 30270109; |
| Motif | |
| Gene Encoded By | Plasmid pCMS1 |
| Mass | 39,004 |
| Kinetics | |
| Metal Binding | METAL 55; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 57; /note="Zinc 1; via tele nitrogen"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 169; /note="Zinc 1; via carbamate group"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 169; /note="Zinc 2; via carbamate group"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 201; /note="Zinc 2; via pros nitrogen"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 230; /note="Zinc 2; via tele nitrogen"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL"; METAL 301; /note="Zinc 1"; /evidence="ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" |
| Rhea ID | |
| Cross Reference Brenda | 3.1.1.2;3.1.8.1;3.1.8.2; |