ID OPD_BREDI Reviewed; 365 AA. AC P0A434; P13739; P16648; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 02-SEP-2026, entry version 110. DE RecName: Full=Parathion hydrolase; DE EC=3.1.8.1; DE AltName: Full=Phosphotriesterase; DE Short=PTE; DE Flags: Precursor; GN Name=opd; OS Brevundimonas diminuta (Pseudomonas diminuta). OG Plasmid pCMS1. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Caulobacterales; Caulobacteraceae; Brevundimonas. OX NCBI_TaxID=293; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-44. RC STRAIN=MG; RA Serdar C.M., Murdock D.C., Rohde M.F.; RT "Parathion hydrolase gene from Pseudomonas diminuta MG: subcloning, RT complete nucleotide sequence, and expression of the mature portion of the RT enzyme in Escherichia coli."; RL Biotechnology (N.Y.) 7:1151-1155(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MG; RX PubMed=2834339; DOI=10.1128/jb.170.5.2306-2311.1988; RA McDaniel C.S., Harper L.L., Wild J.R.; RT "Cloning and sequencing of a plasmid-borne gene (opd) encoding a RT phosphotriesterase."; RL J. Bacteriol. 170:2306-2311(1988). RN [3] RP METAL BINDING SITES. RX PubMed=8155644; DOI=10.1021/bi00180a022; RA Kuo J.M., Raushel F.M.; RT "Identification of the histidine ligands to the binuclear metal center of RT phosphotriesterase by site-directed mutagenesis."; RL Biochemistry 33:4265-4272(1994). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=7999757; DOI=10.1021/bi00254a008; RA Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.; RT "Three-dimensional structure of phosphotriesterase: an enzyme capable of RT detoxifying organophosphate nerve agents."; RL Biochemistry 33:15001-15007(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND CARBOXYLATION AT LYS-169. RX PubMed=7794910; DOI=10.1021/bi00025a002; RA Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.; RT "Three-dimensional structure of the binuclear metal center of RT phosphotriesterase."; RL Biochemistry 34:7973-7978(1995). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=8634243; DOI=10.1021/bi960325l; RA Vanhooke J.L., Benning M.M., Raushel F.M., Holden H.M.; RT "Three-dimensional structure of the zinc-containing phosphotriesterase with RT the bound substrate analog diethyl 4-methylbenzylphosphonate."; RL Biochemistry 35:6020-6025(1996). CC -!- FUNCTION: Has an unusual substrate specificity for synthetic CC organophosphate triesters and phosphorofluoridates. All of the CC phosphate triesters found to be substrates are synthetic compounds. The CC identity of any naturally occurring substrate for the enzyme is CC unknown. Has no detectable activity with phosphate monoesters or CC diesters and no activity as an esterase or protease. It catalyzes the CC hydrolysis of the insecticide paraoxon at a rate approaching the CC diffusion limit and thus appears to be optimally evolved for utilizing CC this synthetic substrate. CC -!- CATALYTIC ACTIVITY: CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl CC alcohol.; EC=3.1.8.1; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has been experimentally proven. CC -!- BIOTECHNOLOGY: Has attracted interest because of its potential use in CC the detoxification of chemical waste and warfare agents and its ability CC to degrade agricultural pesticides such as parathion. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA98299.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M20392; AAA98299.1; ALT_FRAME; Genomic_DNA. DR PIR; A28214; A28214. DR PDB; 1DPM; X-ray; 2.10 A; A/B=36-363. DR PDB; 1EYW; X-ray; 1.90 A; A=35-365. DR PDB; 1EZ2; X-ray; 1.90 A; A/B=35-365. DR PDB; 1HZY; X-ray; 1.30 A; A/B=34-365. DR PDB; 1I0B; X-ray; 1.30 A; A/B=34-365. DR PDB; 1I0D; X-ray; 1.30 A; A/B=34-365. DR PDB; 1JGM; X-ray; 1.30 A; A/B=30-365. DR PDB; 1PSC; X-ray; 2.00 A; A/B=1-365. DR PDB; 1PTA; X-ray; 2.10 A; A=36-362. DR PDB; 1QW7; X-ray; 1.90 A; A/B=30-365. DR PDB; 2O4M; X-ray; 1.64 A; A/B/C/P=34-364. DR PDB; 2O4Q; X-ray; 1.95 A; A/B/K/P=34-364. DR PDB; 2OB3; X-ray; 1.04 A; A/B=35-364. DR PDB; 2OQL; X-ray; 1.80 A; A/B=35-365. DR PDB; 3CAK; X-ray; 1.83 A; A/B=35-365. DR PDB; 3CS2; X-ray; 1.95 A; A/B/K/P=34-364. DR PDB; 3E3H; X-ray; 2.15 A; A/B=30-365. DR PDB; 3UPM; X-ray; 1.95 A; A/B=35-361. DR PDB; 3UR2; X-ray; 2.00 A; A/B=35-363. DR PDB; 3UR5; X-ray; 1.60 A; A/B=35-361. DR PDB; 3URA; X-ray; 1.88 A; A/B=35-361. DR PDB; 3URB; X-ray; 1.77 A; A/B=35-361. DR PDB; 3URN; X-ray; 1.95 A; A/B=35-361. DR PDB; 3URQ; X-ray; 2.10 A; A/B=35-361. DR PDB; 4E3T; X-ray; 1.65 A; A/B=34-365. DR PDB; 4GY0; X-ray; 1.85 A; A/B=34-365. DR PDB; 4GY1; X-ray; 1.50 A; A/B=34-365. DR PDB; 4ZST; X-ray; 2.01 A; A/B=30-365. DR PDB; 4ZSU; X-ray; 2.01 A; A/B=30-365. DR PDB; 5W6B; X-ray; 1.74 A; A/G=34-365. DR PDB; 5WCQ; X-ray; 1.58 A; A/G=34-365. DR PDB; 6AML; X-ray; 1.46 A; A/G=34-365. DR PDB; 6FFW; X-ray; 1.50 A; A/B=32-365. DR PDB; 6FQE; X-ray; 1.75 A; A/B=34-365. DR PDB; 6FRZ; X-ray; 1.65 A; A/B=32-365. DR PDB; 6FS3; X-ray; 1.75 A; A/B=32-365. DR PDB; 6FU6; X-ray; 1.95 A; A/B=34-365. DR PDB; 6FWE; X-ray; 1.77 A; A=34-365. DR PDB; 6G1J; X-ray; 2.10 A; A=34-365. DR PDB; 6G3M; X-ray; 1.67 A; A=34-365. DR PDB; 6GBJ; X-ray; 1.63 A; A=34-365. DR PDB; 6GBK; X-ray; 1.90 A; A/B=34-365. DR PDB; 6GBL; X-ray; 1.95 A; A/B=34-365. DR PDB; 7P85; X-ray; 1.47 A; A=30-364. DR PDB; 8P7F; X-ray; 2.00 A; A=34-365. DR PDB; 8P7H; X-ray; 1.77 A; A=34-362. DR PDB; 8P7I; X-ray; 1.70 A; A/B=34-365. DR PDB; 8P7K; X-ray; 1.93 A; A/B=34-365. DR PDB; 8P7M; X-ray; 1.85 A; A=34-361. DR PDB; 8P7N; X-ray; 3.20 A; A/B/C/D=34-362. DR PDB; 8P7Q; X-ray; 1.77 A; A=34-365. DR PDB; 8P7R; X-ray; 1.85 A; A=34-365. DR PDB; 8P7S; X-ray; 1.77 A; A=34-361. DR PDB; 8P7T; X-ray; 1.80 A; A=34-365. DR PDB; 8P7U; X-ray; 1.38 A; A=34-364. DR PDB; 8P7V; X-ray; 1.74 A; A=34-364. DR PDB; 9TI1; X-ray; 1.55 A; A/B=34-365. DR PDB; 9TI2; X-ray; 1.69 A; A/B/C/D/E/F=34-365. DR AlphaFoldDB; P0A434; -. DR MDRepo; P0A434; -. DR SMR; P0A434; -. DR DrugBank; DB02138; Diethyl 4-Methylbenzylphosphonate. DR DrugBank; DB02127; Diisopropyl methylphosphonate. DR DrugBank; DB03347; Triethyl phosphate. DR BioCyc; MetaCyc:MONOMER-3322; -. DR BRENDA; 3.1.1.2; 982. DR BRENDA; 3.1.8.1; 982. DR BRENDA; 3.8.2.2; 982. DR SABIO-RK; P0A434; -. DR EvolutionaryTrace; P0A434; -. DR GO; GO:0005886; C:plasma membrane; IDA:CACAO. DR GO; GO:0004063; F:aryldialkylphosphatase activity; IDA:CACAO. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR CDD; cd00530; PTE; 1. DR FunFam; 3.20.20.140:FF:000073; Parathion hydrolase; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR017947; AryldialkylPase_Zn-BS. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001559; Phosphotriesterase. DR InterPro; IPR006311; TAT_signal. DR NCBIfam; NF041153; organophos_OPH; 1. DR PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1. DR PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1. DR Pfam; PF02126; PTE; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1. DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1. DR PROSITE; PS51318; TAT; 1. DR PDBsum; 1DPM; -. DR PDBsum; 1EYW; -. DR PDBsum; 1EZ2; -. DR PDBsum; 1HZY; -. DR PDBsum; 1I0B; -. DR PDBsum; 1I0D; -. DR PDBsum; 1JGM; -. DR PDBsum; 1PSC; -. DR PDBsum; 1PTA; -. DR PDBsum; 1QW7; -. DR PDBsum; 2O4M; -. DR PDBsum; 2O4Q; -. DR PDBsum; 2OB3; -. DR PDBsum; 2OQL; -. DR PDBsum; 3CAK; -. DR PDBsum; 3CS2; -. DR PDBsum; 3E3H; -. DR PDBsum; 3UPM; -. DR PDBsum; 3UR2; -. DR PDBsum; 3UR5; -. DR PDBsum; 3URA; -. DR PDBsum; 3URB; -. DR PDBsum; 3URN; -. DR PDBsum; 3URQ; -. DR PDBsum; 4E3T; -. DR PDBsum; 4GY0; -. DR PDBsum; 4GY1; -. DR PDBsum; 4ZST; -. DR PDBsum; 4ZSU; -. DR PDBsum; 5W6B; -. DR PDBsum; 5WCQ; -. DR PDBsum; 6AML; -. DR PDBsum; 6FFW; -. DR PDBsum; 6FQE; -. DR PDBsum; 6FRZ; -. DR PDBsum; 6FS3; -. DR PDBsum; 6FU6; -. DR PDBsum; 6FWE; -. DR PDBsum; 6G1J; -. DR PDBsum; 6G3M; -. DR PDBsum; 6GBJ; -. DR PDBsum; 6GBK; -. DR PDBsum; 6GBL; -. DR PDBsum; 7P85; -. DR PDBsum; 8P7F; -. DR PDBsum; 8P7H; -. DR PDBsum; 8P7I; -. DR PDBsum; 8P7K; -. DR PDBsum; 8P7M; -. DR PDBsum; 8P7N; -. DR PDBsum; 8P7Q; -. DR PDBsum; 8P7R; -. DR PDBsum; 8P7S; -. DR PDBsum; 8P7T; -. DR PDBsum; 8P7U; -. DR PDBsum; 8P7V; -. DR PDBsum; 9TI1; -. DR PDBsum; 9TI2; -. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Direct protein sequencing; Hydrolase; KW Membrane; Metal-binding; Plasmid; Signal; Zinc. FT SIGNAL 1..29 FT /note="Tat-type signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, FT ECO:0000269|Ref.1" FT CHAIN 30..365 FT /note="Parathion hydrolase" FT /id="PRO_0000029860" FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /note="via carbamate group" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 230 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT BINDING 301 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:7794910, FT ECO:0007744|PDB:1DPM, ECO:0007744|PDB:1EYW, FT ECO:0007744|PDB:1EZ2, ECO:0007744|PDB:1HZY, FT ECO:0007744|PDB:2O4M, ECO:0007744|PDB:2O4Q, FT ECO:0007744|PDB:2OB3, ECO:0007744|PDB:2OQL" FT MOD_RES 169 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679, FT ECO:0000269|PubMed:7794910, ECO:0007744|PDB:1DPM, FT ECO:0007744|PDB:1EYW, ECO:0007744|PDB:1EZ2, FT ECO:0007744|PDB:1HZY, ECO:0007744|PDB:2O4M, FT ECO:0007744|PDB:2O4Q, ECO:0007744|PDB:2OB3, FT ECO:0007744|PDB:2OQL" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:6FRZ" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 46..49 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:8P7F" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 76..92 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 110..120 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 136..139 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 143..151 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 152..156 FT /evidence="ECO:0007829|PDB:2OB3" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:1HZY" FT HELIX 163..165 FT /evidence="ECO:0007829|PDB:6AML" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 178..194 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 208..218 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 237..245 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 255..259 FT /evidence="ECO:0007829|PDB:6AML" FT HELIX 266..272 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:8P7F" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:2OB3" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 313..320 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 328..332 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 333..338 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 343..347 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 348..352 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 353..358 FT /evidence="ECO:0007829|PDB:2OB3" FT HELIX 362..364 FT /evidence="ECO:0007829|PDB:1HZY" SQ SEQUENCE 365 AA; 39004 MW; 41FF8E4B029B46DC CRC64; MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG FTLTHEHICG SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD VSTFDIGRDV SLLAEVSRAA DVHIVAATGL WFDPPLSMRL RSVEELTQFF LREIQYGIED TGIRAGIIKV ATTGKATPFQ ELVLKAAARA SLATGVPVTT HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL TALAARGYLI GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT VTNPARFLSP TLRAS //