ID OPD_SPHSA Reviewed; 365 AA. AC P0A433; P13739; P16648; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 27-MAR-2024, entry version 86. 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 Sphingobium fuliginis (strain ATCC 27551). OG Plasmid pPDL2. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=336203; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 30-53. RX PubMed=2556372; DOI=10.1128/jb.171.12.6740-6746.1989; RA Mulbry W.W., Karns J.S.; RT "Parathion hydrolase specified by the Flavobacterium opd gene: relationship RT between the gene and protein."; RL J. Bacteriol. 171:6740-6746(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-365, AND CARBOXYLATION AT RP LYS-169. RX PubMed=15369336; DOI=10.1021/ja0358798; RA Hill C.M., Li W.S., Thoden J.B., Holden H.M., Raushel F.M.; RT "Enhanced degradation of chemical warfare agents through molecular RT engineering of the phosphotriesterase active site."; RL J. Am. Chem. Soc. 125:8990-8991(2003). 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 (By similarity). {ECO:0000250}. 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00679}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00679}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane CC protein {ECO:0000250}. CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has been experimentally proven. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}. 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; M29593; AAA24930.1; -; Genomic_DNA. DR PIR; A43720; A43720. DR PDB; 1P6B; X-ray; 1.90 A; A/B=30-365. DR PDB; 1P6C; X-ray; 2.00 A; A/B=30-365. DR PDBsum; 1P6B; -. DR PDBsum; 1P6C; -. DR AlphaFoldDB; P0A433; -. DR SMR; P0A433; -. DR DrugBank; DB02437; (5r)-5-Amino-6-Hydroxyhexylcarbamic Acid. DR DrugBank; DB02138; Diethyl 4-Methylbenzylphosphonate. DR DrugBank; DB02127; Diisopropyl methylphosphonate. DR DrugBank; DB03822; Ethyl dihydrogen phosphate. DR DrugBank; DB03801; Lysine Nz-Carboxylic Acid. DR DrugBank; DB02192; Phenylethyl alcohol. DR DrugBank; DB03347; Triethyl phosphate. DR BioCyc; MetaCyc:MONOMER-3321; -. DR BRENDA; 3.1.8.1; 2302. DR BRENDA; 3.1.8.2; 16550. DR EvolutionaryTrace; P0A433; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:UniProtKB-EC. 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|PubMed:2556372" FT CHAIN 30..365 FT /note="Parathion hydrolase" FT /id="PRO_0000029861" FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" 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:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" 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:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" FT BINDING 230 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" FT BINDING 301 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:15369336, FT ECO:0007744|PDB:1P6B, ECO:0007744|PDB:1P6C" FT MOD_RES 169 FT /note="N6-carboxylysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00679, FT ECO:0000269|PubMed:15369336, ECO:0007744|PDB:1P6B, FT ECO:0007744|PDB:1P6C" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 51..56 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 65..68 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 70..73 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 76..92 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 104..106 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 110..120 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 136..139 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 143..155 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 178..194 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 198..201 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 208..218 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 237..245 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 266..272 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:1P6B" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 313..320 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:1P6B" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 343..350 FT /evidence="ECO:0007829|PDB:1P6B" FT HELIX 352..358 FT /evidence="ECO:0007829|PDB:1P6B" 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 //