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Protein

Aryldialkylphosphatase

Gene

php

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a low paraoxonase activity. Also active, but with a lower activity, against other organo-phosphorus insecticides such as Dursban, Coumaphos, pNP-butanoate or parathion.1 Publication

Catalytic activityi

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inactivated by EDTA and o-phenanthroline.1 Publication

Kineticsi

  1. KM=0.06 mM for paraoxon (at pH 8.0)1 Publication
  2. KM=0.205 mM for methyl-paraoxon (at pH 8.0)1 Publication

    pH dependencei

    Optimum pH is 7.0-9.0.1 Publication

    Temperature dependencei

    Thermostable.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi22 – 221Iron; via tele nitrogenCombined sources1 Publication
    Metal bindingi24 – 241Iron; via tele nitrogenCombined sources1 Publication
    Metal bindingi137 – 1371Cobalt; via carbamate groupCombined sources1 Publication
    Metal bindingi137 – 1371Iron; via carbamate groupCombined sources1 Publication
    Metal bindingi170 – 1701Cobalt; via pros nitrogenCombined sources1 Publication
    Metal bindingi199 – 1991Cobalt; via tele nitrogenCombined sources1 Publication
    Metal bindingi256 – 2561IronCombined sources1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Cobalt, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-2339-MONOMER.
    BRENDAi3.1.1.25. 6163.
    3.1.1.81. 6163.
    3.1.8.1. 6163.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aryldialkylphosphatase (EC:3.1.8.1)
    Alternative name(s):
    Paraoxonase
    Short name:
    SsoPox
    Phosphotriesterase-like lactonase
    Gene namesi
    Name:php
    Ordered Locus Names:SSO2522
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001974 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314AryldialkylphosphatasePRO_0000388684Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei137 – 1371N6-carboxylysinePROSITE-ProRule annotationCombined sources1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi273057.SSO2522.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53Combined sources
    Beta strandi8 – 114Combined sources
    Helixi13 – 153Combined sources
    Beta strandi18 – 225Combined sources
    Helixi30 – 356Combined sources
    Helixi37 – 393Combined sources
    Helixi42 – 5817Combined sources
    Beta strandi63 – 664Combined sources
    Turni71 – 733Combined sources
    Helixi76 – 8611Combined sources
    Beta strandi89 – 924Combined sources
    Beta strandi94 – 963Combined sources
    Helixi104 – 1063Combined sources
    Helixi111 – 12313Combined sources
    Beta strandi126 – 1305Combined sources
    Beta strandi135 – 1395Combined sources
    Helixi147 – 16317Combined sources
    Beta strandi167 – 1704Combined sources
    Turni173 – 1764Combined sources
    Helixi177 – 18711Combined sources
    Helixi192 – 1943Combined sources
    Beta strandi195 – 1973Combined sources
    Helixi200 – 2023Combined sources
    Helixi206 – 2149Combined sources
    Beta strandi218 – 2214Combined sources
    Turni227 – 2293Combined sources
    Helixi232 – 24413Combined sources
    Helixi247 – 2493Combined sources
    Beta strandi251 – 2533Combined sources
    Beta strandi258 – 2614Combined sources
    Helixi264 – 2663Combined sources
    Helixi268 – 2703Combined sources
    Helixi271 – 2744Combined sources
    Beta strandi279 – 2813Combined sources
    Helixi282 – 2854Combined sources
    Helixi287 – 2937Combined sources
    Helixi298 – 3058Combined sources
    Helixi307 – 3126Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VC5X-ray2.60A/B/C/D1-314[»]
    2VC7X-ray2.05A/B/C/D1-314[»]
    3UF9X-ray2.68A/B/C/D1-314[»]
    4KERX-ray2.60A/B/C/D1-314[»]
    4KESX-ray2.10A/B/C/D1-314[»]
    4KETX-ray2.00A/B/C/D1-314[»]
    4KEUX-ray2.20A/B/C/D1-314[»]
    4KEVX-ray2.65A/B/C/D1-314[»]
    4KEZX-ray1.85A/B/C/D1-314[»]
    4KF1X-ray2.00A/B/C/D1-314[»]
    ProteinModelPortaliQ97VT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ97VT7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphotriesterase family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiarCOG07263. Archaea.
    COG1735. LUCA.
    HOGENOMiHOG000081700.
    InParanoidiQ97VT7.
    KOiK07048.
    OMAiETGVHII.

    Family and domain databases

    InterProiIPR017947. AryldialkylPase_Zn-BS.
    IPR032466. Metal_Hydrolase.
    IPR001559. Phosphotriesterase.
    [Graphical view]
    PANTHERiPTHR10819. PTHR10819. 1 hit.
    PfamiPF02126. PTE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
    PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q97VT7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRIPLVGKDS IESKDIGFTL IHEHLRVFSE AVRQQWPHLY NEDEEFRNAV
    60 70 80 90 100
    NEVKRAMQFG VKTIVDPTVM GLGRDIRFME KVVKATGINL VAGTGIYIYI
    110 120 130 140 150
    DLPFYFLNRS IDEIADLFIH DIKEGIQGTL NKAGFVKIAA DEPGITKDVE
    160 170 180 190 200
    KVIRAAAIAN KETKVPIITH SNAHNNTGLE QQRILTEEGV DPGKILIGHL
    210 220 230 240 250
    GDTDNIDYIK KIADKGSFIG LDRYGLDLFL PVDKRNETTL RLIKDGYSDK
    260 270 280 290 300
    IMISHDYCCT IDWGTAKPEY KPKLAPRWSI TLIFEDTIPF LKRNGVNEEV
    310
    IATIFKENPK KFFS
    Length:314
    Mass (Da):35,565
    Last modified:October 1, 2001 - v1
    Checksum:iB5A28F80C3CB1A31
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK42653.1.
    AY775568 Genomic DNA. Translation: AAW47234.1.
    PIRiF90424.
    RefSeqiWP_009988477.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK42653; AAK42653; SSO2522.
    GeneIDi25402775.
    KEGGisso:SSO2522.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK42653.1.
    AY775568 Genomic DNA. Translation: AAW47234.1.
    PIRiF90424.
    RefSeqiWP_009988477.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VC5X-ray2.60A/B/C/D1-314[»]
    2VC7X-ray2.05A/B/C/D1-314[»]
    3UF9X-ray2.68A/B/C/D1-314[»]
    4KERX-ray2.60A/B/C/D1-314[»]
    4KESX-ray2.10A/B/C/D1-314[»]
    4KETX-ray2.00A/B/C/D1-314[»]
    4KEUX-ray2.20A/B/C/D1-314[»]
    4KEVX-ray2.65A/B/C/D1-314[»]
    4KEZX-ray1.85A/B/C/D1-314[»]
    4KF1X-ray2.00A/B/C/D1-314[»]
    ProteinModelPortaliQ97VT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO2522.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK42653; AAK42653; SSO2522.
    GeneIDi25402775.
    KEGGisso:SSO2522.

    Phylogenomic databases

    eggNOGiarCOG07263. Archaea.
    COG1735. LUCA.
    HOGENOMiHOG000081700.
    InParanoidiQ97VT7.
    KOiK07048.
    OMAiETGVHII.

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-2339-MONOMER.
    BRENDAi3.1.1.25. 6163.
    3.1.1.81. 6163.
    3.1.8.1. 6163.

    Miscellaneous databases

    EvolutionaryTraceiQ97VT7.

    Family and domain databases

    InterProiIPR017947. AryldialkylPase_Zn-BS.
    IPR032466. Metal_Hydrolase.
    IPR001559. Phosphotriesterase.
    [Graphical view]
    PANTHERiPTHR10819. PTHR10819. 1 hit.
    PfamiPF02126. PTE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51556. SSF51556. 1 hit.
    PROSITEiPS01322. PHOSPHOTRIESTERASE_1. 1 hit.
    PS51347. PHOSPHOTRIESTERASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties."
      Merone L., Mandrich L., Rossi M., Manco G.
      Extremophiles 9:297-305(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: DSM 5833 / MT-4.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Structural basis for natural lactonase and promiscuous phosphotriesterase activities."
      Elias M., Dupuy J., Merone L., Mandrich L., Porzio E., Moniot S., Rochu D., Lecomte C., Rossi M., Masson P., Manco G., Chabriere E.
      J. Mol. Biol. 379:1017-1028(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), COFACTOR, METAL-BINDING SITES, SUBUNIT, CARBAMYLATION AT LYS-137.
      Strain: DSM 5833 / MT-4.

    Entry informationi

    Entry nameiPHP_SULSO
    AccessioniPrimary (citable) accession number: Q97VT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: October 1, 2001
    Last modified: December 9, 2015
    This is version 81 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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.