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UniProtKB - P45548 (PHP_ECOLI)

Entry version 141 (02 Jun 2021)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
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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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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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