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P0A434

- OPD_BREDI

UniProt

P0A434 - OPD_BREDI

Protein

Parathion hydrolase

Gene

opd

Organism
Brevundimonas diminuta (Pseudomonas diminuta)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (15 Mar 2005)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

    An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551Zinc 1
    Metal bindingi57 – 571Zinc 1
    Metal bindingi169 – 1691Zinc 1; via carbamate group
    Metal bindingi169 – 1691Zinc 2; via carbamate group
    Metal bindingi201 – 2011Zinc 2
    Metal bindingi230 – 2301Zinc 2
    Metal bindingi301 – 3011Zinc 1

    GO - Molecular functioni

    1. aryldialkylphosphatase activity Source: UniProtKB-EC
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-3322.
    SABIO-RKP0A434.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Parathion hydrolase (EC:3.1.8.1)
    Alternative name(s):
    Phosphotriesterase
    Short name:
    PTE
    Gene namesi
    Name:opd
    Encoded oniPlasmid pCMS10 Publication
    OrganismiBrevundimonas diminuta (Pseudomonas diminuta)
    Taxonomic identifieri293 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeBrevundimonas

    Subcellular locationi

    GO - Cellular componenti

    1. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Biotechnological usei

    Has attracted interest because of its potential use in the detoxification of chemical waste and warfare agents and its ability to degrade agricultural pesticides such as parathion.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Tat-type signal1 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini30 – 365336Parathion hydrolasePRO_0000029860Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei169 – 1691N6-carboxylysine1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    365
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 393
    Beta strandi42 – 443
    Helixi46 – 494
    Beta strandi51 – 566
    Beta strandi58 – 603
    Turni61 – 644
    Helixi65 – 684
    Helixi70 – 734
    Helixi76 – 9217
    Beta strandi97 – 1004
    Helixi104 – 1063
    Helixi110 – 12011
    Beta strandi123 – 1253
    Beta strandi127 – 1293
    Helixi136 – 1394
    Helixi143 – 15513
    Turni159 – 1624
    Beta strandi166 – 1716
    Beta strandi173 – 1753
    Helixi178 – 19417
    Beta strandi198 – 2014
    Helixi204 – 2063
    Helixi208 – 21811
    Helixi223 – 2253
    Beta strandi226 – 2283
    Helixi231 – 2333
    Helixi237 – 2459
    Beta strandi249 – 2524
    Helixi255 – 2584
    Helixi266 – 2727
    Helixi277 – 28913
    Turni290 – 2923
    Helixi293 – 2953
    Beta strandi296 – 2983
    Beta strandi304 – 3063
    Beta strandi308 – 3103
    Helixi313 – 3208
    Helixi324 – 3263
    Helixi327 – 3304
    Helixi332 – 3387
    Helixi343 – 3508
    Helixi352 – 3587

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DPMX-ray2.10A/B36-363[»]
    1EYWX-ray1.90A35-365[»]
    1EZ2X-ray1.90A/B35-365[»]
    1HZYX-ray1.30A/B34-365[»]
    1I0BX-ray1.30A/B34-365[»]
    1I0DX-ray1.30A/B34-365[»]
    1JGMX-ray1.30A/B30-365[»]
    1PSCX-ray2.00A/B1-365[»]
    1PTAX-ray2.10A36-362[»]
    1QW7X-ray1.90A/B30-365[»]
    2O4MX-ray1.64A/B/C/P34-364[»]
    2O4QX-ray1.95A/B/K/P34-364[»]
    2OB3X-ray1.04A/B35-364[»]
    2OQLX-ray1.80A/B35-365[»]
    3CAKX-ray1.83A/B35-365[»]
    3CS2X-ray1.95A/B/K/P34-364[»]
    3E3HX-ray2.15A/B30-365[»]
    3UPMX-ray1.95A/B35-361[»]
    3UR2X-ray2.00A/B35-363[»]
    3UR5X-ray1.60A/B35-361[»]
    3URAX-ray1.88A/B35-361[»]
    3URBX-ray1.77A/B35-361[»]
    3URNX-ray1.95A/B35-361[»]
    3URQX-ray2.10A/B35-361[»]
    4E3TX-ray1.65A/B34-365[»]
    4GY0X-ray1.85A/B34-365[»]
    4GY1X-ray1.50A/B34-365[»]
    ProteinModelPortaliP0A434.
    SMRiP0A434. Positions 34-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A434.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphotriesterase family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR017947. AryldialkylPase_Zn-BS.
    IPR001559. Aryldialkylphosphatase.
    IPR006311. TAT_signal.
    [Graphical view]
    PANTHERiPTHR10819. PTHR10819. 1 hit.
    PfamiPF02126. PTE. 1 hit.
    [Graphical view]
    PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
    PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0A434-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQTRRVVLKS AAAAGTLLGG LAGCASVAGS IGTGDRINTV RGPITISEAG    50
    FTLTHEHICG SSAGFLRAWP EFFGSRKALA EKAVRGLRRA RAAGVRTIVD 100
    VSTFDIGRDV SLLAEVSRAA DVHIVAATGL WFDPPLSMRL RSVEELTQFF 150
    LREIQYGIED TGIRAGIIKV ATTGKATPFQ ELVLKAAARA SLATGVPVTT 200
    HTAASQRDGE QQAAIFESEG LSPSRVCIGH SDDTDDLSYL TALAARGYLI 250
    GLDHIPHSAI GLEDNASASA LLGIRSWQTR ALLIKALIDQ GYMKQILVSN 300
    DWLFGFSSYV TNIMDVMDRV NPDGMAFIPL RVIPFLREKG VPQETLAGIT 350
    VTNPARFLSP TLRAS 365
    Length:365
    Mass (Da):39,004
    Last modified:March 15, 2005 - v1
    Checksum:i41FF8E4B029B46DC
    GO

    Sequence cautioni

    The sequence AAA98299.1 differs from that shown. Reason: Frameshift at several positions.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20392 Genomic DNA. Translation: AAA98299.1. Frameshift.
    PIRiA28214.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M20392 Genomic DNA. Translation: AAA98299.1 . Frameshift.
    PIRi A28214.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DPM X-ray 2.10 A/B 36-363 [» ]
    1EYW X-ray 1.90 A 35-365 [» ]
    1EZ2 X-ray 1.90 A/B 35-365 [» ]
    1HZY X-ray 1.30 A/B 34-365 [» ]
    1I0B X-ray 1.30 A/B 34-365 [» ]
    1I0D X-ray 1.30 A/B 34-365 [» ]
    1JGM X-ray 1.30 A/B 30-365 [» ]
    1PSC X-ray 2.00 A/B 1-365 [» ]
    1PTA X-ray 2.10 A 36-362 [» ]
    1QW7 X-ray 1.90 A/B 30-365 [» ]
    2O4M X-ray 1.64 A/B/C/P 34-364 [» ]
    2O4Q X-ray 1.95 A/B/K/P 34-364 [» ]
    2OB3 X-ray 1.04 A/B 35-364 [» ]
    2OQL X-ray 1.80 A/B 35-365 [» ]
    3CAK X-ray 1.83 A/B 35-365 [» ]
    3CS2 X-ray 1.95 A/B/K/P 34-364 [» ]
    3E3H X-ray 2.15 A/B 30-365 [» ]
    3UPM X-ray 1.95 A/B 35-361 [» ]
    3UR2 X-ray 2.00 A/B 35-363 [» ]
    3UR5 X-ray 1.60 A/B 35-361 [» ]
    3URA X-ray 1.88 A/B 35-361 [» ]
    3URB X-ray 1.77 A/B 35-361 [» ]
    3URN X-ray 1.95 A/B 35-361 [» ]
    3URQ X-ray 2.10 A/B 35-361 [» ]
    4E3T X-ray 1.65 A/B 34-365 [» ]
    4GY0 X-ray 1.85 A/B 34-365 [» ]
    4GY1 X-ray 1.50 A/B 34-365 [» ]
    ProteinModelPortali P0A434.
    SMRi P0A434. Positions 34-364.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-3322.
    SABIO-RK P0A434.

    Miscellaneous databases

    EvolutionaryTracei P0A434.

    Family and domain databases

    InterProi IPR017947. AryldialkylPase_Zn-BS.
    IPR001559. Aryldialkylphosphatase.
    IPR006311. TAT_signal.
    [Graphical view ]
    PANTHERi PTHR10819. PTHR10819. 1 hit.
    Pfami PF02126. PTE. 1 hit.
    [Graphical view ]
    PROSITEi PS01322. PHOSPHOTRIESTERASE_1. 1 hit.
    PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Parathion hydrolase gene from Pseudomonas diminuta MG: subcloning, complete nucleotide sequence, and expression of the mature portion of the enzyme in Escherichia coli."
      Serdar C.M., Murdock D.C., Rohde M.F.
      Biotechnology (N.Y.) 7:1151-1155(1989)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-44.
      Strain: MG.
    2. "Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase."
      McDaniel C.S., Harper L.L., Wild J.R.
      J. Bacteriol. 170:2306-2311(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: MG.
    3. "Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis."
      Kuo J.M., Raushel F.M.
      Biochemistry 33:4265-4272(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: METAL BINDING SITES.
    4. "Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents."
      Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.
      Biochemistry 33:15001-15007(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    5. "Three-dimensional structure of the binuclear metal center of phosphotriesterase."
      Benning M.M., Kuo J.M., Raushel F.M., Holden H.M.
      Biochemistry 34:7973-7978(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), CARBAMYLATION AT LYS-169.
    6. "Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate."
      Vanhooke J.L., Benning M.M., Raushel F.M., Holden H.M.
      Biochemistry 35:6020-6025(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiOPD_BREDI
    AccessioniPrimary (citable) accession number: P0A434
    Secondary accession number(s): P13739, P16648
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: March 15, 2005
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Plasmid

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3