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Entry version 141 (02 Jun 2021)
Sequence version 1 (01 Nov 1995)
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Protein

Phosphotriesterase homology protein

Gene

php

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the hydrolysis of phosphorylated glyceryl acetates in which the presence of a phosphate group is required for the enzymatic hydrolysis. Hydrolyzes a dibutyl glycerol derivative suggesting it acts on phosphoglycerol substrates with a butyrate leaving group. Also active with aromatic acetates and propionates. No activity with various sugar phosphates, with various nitrophenylphosphate or nitrophenylphosphonate derivatives, or with phosphorylated or non-phosphorylated sugar lactones tested. Does not hydrolyze non-phosphorylated carboxyesters with long chain leaving groups (PubMed:30277746).

No general esterase, aminopeptidase, sulfatase, phosphatase, carbonic anhydrase, phosphodiesterase, and phosphotriesterase activities detected when tested with the following non-specific substrates: p-nitrophenyl acetate, L-alanine nitroanilide, p-nitrophenyl sulfate, bis(p-nitrophenyl) phosphate, paraoxon, and p-nitrophenyl phosphate (PubMed:9548740).

2 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activity is higher in the enzyme containing Mn2+ than that containing Zn2+.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 2.5 sec(-1) with 2-naphthyl acetate as substrate. kcat is 27 sec(-1) with (2S)-1,2-diacetyl glycerol-3-phosphate as substrate. kcat is 28 sec(-1) with rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate as substrate.1 Publication
  1. KM=1.8 mM for 2-naphthyl acetate (in the presence of 1.0 mM MnCl2, at pH 8.0 and 30 degrees Celsius)1 Publication
  2. KM=5.5 mM for (2S)-1,2-diacetyl glycerol-3-phosphate (in the presence of 1.0 mM MnCl2, at pH 8.0 and 30 degrees Celsius)1 Publication
  3. KM=6.0 mM for rac-(2R,2S)-1,2-diacetyl glycerol-3-phosphate (in the presence of 1.0 mM MnCl2, at pH 8.0 and 30 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi12Zinc 1; via tele nitrogenCombined sources2 Publications1
    Metal bindingi14Zinc 1; via tele nitrogenCombined sources2 Publications1
    Metal bindingi125Zinc 1Combined sources2 Publications1
    Metal bindingi125Zinc 2Combined sources2 Publications1
    Metal bindingi158Zinc 2; via pros nitrogenCombined sources2 Publications1
    Metal bindingi186Zinc 2; via tele nitrogenCombined sources2 Publications1
    Metal bindingi243Zinc 1Combined sources2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei280Beta-D-glucoseCombined sources1 Publication1
    Binding sitei284Beta-D-glucoseCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:G7731-MONOMER

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Phosphotriesterase homology protein2 Publications (EC:3.1.-.-1 Publication)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:php2 Publications
    Synonyms:yhfV
    Ordered Locus Names:b3379, JW3342
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002053621 – 292Phosphotriesterase homology proteinAdd BLAST292

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P45548

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P45548

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    4260764, 9 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-10504N

    Protein interaction database and analysis system

    More...
    IntActi
    P45548, 2 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b3379

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1292
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P45548

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P45548

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni148 – 149Beta-D-glucose bindingCombined sources1 Publication2
    Regioni176 – 191Beta-D-glucose bindingCombined sources1 PublicationAdd BLAST16

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family.PROSITE-ProRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG1735, Bacteria

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_054760_1_1_6

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P45548

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P45548

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00530, PTE, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017947, AryldialkylPase_Zn-BS
    IPR032466, Metal_Hydrolase
    IPR001559, Phosphotriesterase

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10819, PTHR10819, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02126, PTE, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF016839, PhP, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51556, SSF51556, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01322, PHOSPHOTRIESTERASE_1, 1 hit
    PS51347, PHOSPHOTRIESTERASE_2, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    P45548-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSFDPTGYTL AHEHLHIDLS GFKNNVDCRL DQYAFICQEM NDLMTRGVRN
    60 70 80 90 100
    VIEMTNRYMG RNAQFMLDVM RETGINVVAC TGYYQDAFFP EHVATRSVQE
    110 120 130 140 150
    LAQEMVDEIE QGIDGTELKA GIIAEIGTSE GKITPLEEKV FIAAALAHNQ
    160 170 180 190 200
    TGRPISTHTS FSTMGLEQLA LLQAHGVDLS RVTVGHCDLK DNLDNILKMI
    210 220 230 240 250
    DLGAYVQFDT IGKNSYYPDE KRIAMLHALR DRGLLNRVML SMDITRRSHL
    260 270 280 290
    KANGGYGYDY LLTTFIPQLR QSGFSQADVD VMLRENPSQF FQ
    Length:292
    Mass (Da):32,915
    Last modified:November 1, 1995 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1480C6858E5E8230
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    U18997 Genomic DNA Translation: AAA58176.1
    U00096 Genomic DNA Translation: AAC76404.1
    AP009048 Genomic DNA Translation: BAE77912.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    F65132

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417838.1, NC_000913.3
    WP_000007010.1, NZ_SSZK01000008.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC76404; AAC76404; b3379
    BAE77912; BAE77912; BAE77912

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    947891

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW3342
    eco:b3379

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.3351

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U18997 Genomic DNA Translation: AAA58176.1
    U00096 Genomic DNA Translation: AAC76404.1
    AP009048 Genomic DNA Translation: BAE77912.1
    PIRiF65132
    RefSeqiNP_417838.1, NC_000913.3
    WP_000007010.1, NZ_SSZK01000008.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1BF6X-ray1.70A/B2-292[»]
    4LEFX-ray1.84A/B/C/D/E/F/G/H1-292[»]
    SMRiP45548
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi4260764, 9 interactors
    DIPiDIP-10504N
    IntActiP45548, 2 interactors
    STRINGi511145.b3379

    Proteomic databases

    PaxDbiP45548
    PRIDEiP45548

    Genome annotation databases

    EnsemblBacteriaiAAC76404; AAC76404; b3379
    BAE77912; BAE77912; BAE77912
    GeneIDi947891
    KEGGiecj:JW3342
    eco:b3379
    PATRICifig|1411691.4.peg.3351

    Organism-specific databases

    EchoBASE - an integrated post-genomic database for E. coli

    More...
    EchoBASEi
    EB2753

    Phylogenomic databases

    eggNOGiCOG1735, Bacteria
    HOGENOMiCLU_054760_1_1_6
    InParanoidiP45548
    PhylomeDBiP45548

    Enzyme and pathway databases

    BioCyciEcoCyc:G7731-MONOMER

    Miscellaneous databases

    EvolutionaryTraceiP45548

    Protein Ontology

    More...
    PROi
    PR:P45548

    Family and domain databases

    CDDicd00530, PTE, 1 hit
    InterProiView protein in InterPro
    IPR017947, AryldialkylPase_Zn-BS
    IPR032466, Metal_Hydrolase
    IPR001559, Phosphotriesterase
    PANTHERiPTHR10819, PTHR10819, 1 hit
    PfamiView protein in Pfam
    PF02126, PTE, 1 hit
    PIRSFiPIRSF016839, PhP, 1 hit
    SUPFAMiSSF51556, SSF51556, 1 hit
    PROSITEiView protein in PROSITE
    PS01322, PHOSPHOTRIESTERASE_1, 1 hit
    PS51347, PHOSPHOTRIESTERASE_2, 1 hit

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPHP_ECOLI
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P45548
    Secondary accession number(s): Q2M744
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: June 2, 2021
    This is version 141 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, 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
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