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Protein

Anthranilate synthase component 1

Gene

trpE

Organism
Serratia marcescens
Status
Reviewed-Annotation score:

Annotation score:4 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

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (Probable).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ 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

Feedback inhibited by tryptophan.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (C7M65_09250), Anthranilate synthase component 1 (DMW43_22350), Anthranilate synthase component 1 (BVG97_10575), Anthranilate synthase component 1 (BVG93_10630), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (A8A12_03220), Anthranilate synthase component 1 (C2M04_04200), Anthranilate synthase component 1 (AR325_16160), Anthranilate synthase component 1 (B1A42_12945), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (C3463_02895), Anthranilate synthase component 1 (BHU62_22585), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (DCX33_08130), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG), Anthranilate synthase component 1 (trpE)
  2. Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpGD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD)
  3. Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), N-(5'-phosphoribosyl)anthranilate isomerase (trpF), N-(5'-phosphoribosyl)anthranilate isomerase (trpF), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC)
  4. Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpC), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpF), Multifunctional fusion protein (trpC)
  5. Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase beta chain (trpB), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei39TryptophanCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 bindingi360Magnesium1 Publication1
Binding sitei448Chorismate1 Publication1
Binding sitei468Chorismate1 Publication1
Binding sitei484Chorismate; via amide nitrogen1 Publication1
Metal bindingi497Magnesium1 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 functionLyase
Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.3.27 5690

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00035;UER00040

<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_and_taxonomy_section">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:
Anthranilate synthase component 1 (EC:4.1.3.27)
Short name:
AS
Short name:
ASI
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:trpE
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiSerratia marcescens
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri615 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001541111 – 519Anthranilate synthase component 1Add BLAST519

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P00897

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
trpGP009002EBI-1031345,EBI-1031352

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P00897, 1 interactor

<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

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P00897

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

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SMRi
P00897

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P00897

<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>Regioni290 – 292Tryptophan bindingCombined sources1 Publication3
Regioni327 – 328Chorismate binding1 Publication2
Regioni482 – 484Chorismate binding1 Publication3

<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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.120.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005801 ADC_synthase
IPR019999 Anth_synth_I-like
IPR006805 Anth_synth_I_N
IPR005257 Anth_synth_I_TrpE
IPR015890 Chorismate_C

The PANTHER Classification System

More...
PANTHERi
PTHR11236:SF22 PTHR11236:SF22, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04715 Anth_synt_I_N, 1 hit
PF00425 Chorismate_bind, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001373 TrpE, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00095 ANTSNTHASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56322 SSF56322, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00565 trpE_proteo, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P00897-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNTKPQLTLL KVQASYRGDP TTLFHQLCGA RPATLLLESA EINDKQNLQS
60 70 80 90 100
LLVIDSALPI TALGHTVSVQ ALTANGPALL PVLDEALPPE VRNQARPNGR
110 120 130 140 150
ELTFPAIDAV QDEDARLRSL SVFDALRTLL TLVDSPADER EAVMLGGLFA
160 170 180 190 200
YDLVAGFENL PAVRQDQRCP DFCFYLAETL LVLDHQRGSA RLQASVFSEQ
210 220 230 240 250
ASEAQRLQHR LEQLQAELQQ PPQPIPHQKL ENMQLSCNQS DEEYGAVVSE
260 270 280 290 300
LQEAIRQGEI FQVVPSRRFS LPCPAPLGPY QTLKDNNPSP YMFFMQDDDF
310 320 330 340 350
TLFGASPESA LKYDAGNRQI EIYPIAGTRP RGRRADGSLD LDLDSRIELE
360 370 380 390 400
MRTDHKELAE HLMLVDLARN DLARICQAGS RYVADLTKVD RYSFVMHLVS
410 420 430 440 450
RVVGTLRADL DVLHAYQACM NMGTLSGAPK VRAMQLIAAL RSTRRGSYGG
460 470 480 490 500
RVGYFTAHRH LDTCIVIRSA YVEDGHRTVQ AGAGVVQDSI RRREADETRN
510
KARAVLRAIA TAHHAKEVF
Length:519
Mass (Da):57,658
Last modified:August 14, 2001 - v2
<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:iD3B59D47619FB0C1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti502 – 504ARA → PVP in AAA57308 (PubMed:7007652).Curated3

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
AY027546 Genomic DNA Translation: AAA57308.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A01117

<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
AY027546 Genomic DNA Translation: AAA57308.2
PIRiA01117

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
1I7QX-ray1.95A/C1-519[»]
1I7SX-ray2.40A/C1-519[»]
ProteinModelPortaliP00897
SMRiP00897
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00897, 1 interactor

Proteomic databases

PRIDEiP00897

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00035;UER00040

BRENDAi4.1.3.27 5690

Miscellaneous databases

EvolutionaryTraceiP00897

Family and domain databases

Gene3Di3.60.120.10, 1 hit
InterProiView protein in InterPro
IPR005801 ADC_synthase
IPR019999 Anth_synth_I-like
IPR006805 Anth_synth_I_N
IPR005257 Anth_synth_I_TrpE
IPR015890 Chorismate_C
PANTHERiPTHR11236:SF22 PTHR11236:SF22, 1 hit
PfamiView protein in Pfam
PF04715 Anth_synt_I_N, 1 hit
PF00425 Chorismate_bind, 1 hit
PIRSFiPIRSF001373 TrpE, 1 hit
PRINTSiPR00095 ANTSNTHASEI
SUPFAMiSSF56322 SSF56322, 1 hit
TIGRFAMsiTIGR00565 trpE_proteo, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiTRPE_SERMA
<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: P00897
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 14, 2001
Last modified: December 5, 2018
This is version 119 of the entry and version 2 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

Documents

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