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 27-MAR-2024, entry version 104.
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; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC 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};
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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 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 AlphaFoldDB; 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; 3.1.8.2; 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 GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR CDD; cd00530; PTE; 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 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.
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..155
FT /evidence="ECO:0007829|PDB:2OB3"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1HZY"
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 TURN 290..292
FT /evidence="ECO:0007829|PDB:1PTA"
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 327..330
FT /evidence="ECO:0007829|PDB:2OB3"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:2OB3"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:2OB3"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:2OB3"
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
//
