Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P24670 (AROD_SALTI)

Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Salmonella typhi
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

Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of Lys-170 at the active site.UniRule annotation1 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 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

Inhibited by (2R)-2-methyl-3-dehydroquinic acid.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 1.1 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius).1 Publication
  1. KM=24 µM for 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius)1 Publication

    <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: chorismate biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroD)
    4. Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase 1 (aroK), Shikimate kinase 2 (aroL)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
    7. Chorismate synthase (aroC)
    This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate 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 sitei213-dehydroquinateUniRule annotation2 Publications1
    Binding sitei823-dehydroquinateUniRule annotation1 Publication1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei143Proton donor/acceptorUniRule annotation1 Publication1
    Active sitei170Schiff-base intermediate with substrateUniRule annotation2 Publications1
    Binding sitei2133-dehydroquinateUniRule annotation3 Publications1
    Binding sitei2323-dehydroquinateUniRule annotation2 Publications1
    Binding sitei2363-dehydroquinateUniRule annotation3 Publications1

    <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

    • 3-dehydroquinate dehydratase activity Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the 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 functionLyase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
    LigandSchiff base

    Enzyme and pathway databases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P24670

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

    More...    UniPathwayi
    UPA00053;UER00086

    <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:
    3-dehydroquinate dehydratase1 PublicationUniRule annotation (EC:4.2.1.10UniRule annotation1 Publication)
    Short name:
    3-dehydroquinase1 PublicationUniRule annotation
    Alternative name(s):
    Type I DHQaseUniRule annotation
    Type I dehydroquinase1 PublicationUniRule annotation
    Short name:
    DHQ11 PublicationUniRule annotation
    <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:aroD1 PublicationUniRule annotation
    Ordered Locus Names:STY1760, t1231
    <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>OrganismiSalmonella typhi
    <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 identifieri90370 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Salmonella ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
    • UP000002670 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
    • UP000000541 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001388051 – 2523-dehydroquinate dehydrataseAdd BLAST252

    Proteomic databases

    PRoteomics IDEntifications database

    More...    PRIDEi    		P24670

    <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

    Dimer of dimers.UniRule annotation3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		220341.STY1760

    <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

    1252
    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    		P24670

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

    More...    SMRi    		P24670

    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    		P24670

    <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>Regioni46 – 483-dehydroquinate bindingUniRule annotation3 Publications3

    <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 type-I 3-dehydroquinase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4105FF2 Bacteria
    COG0710 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000105514

    KEGG Orthology (KO)

    More...    KOi    		K03785

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd00502 DHQase_I, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		3.20.20.70, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00214 AroD, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR018508 3-dehydroquinate_DH_AS
    IPR013785 Aldolase_TIM
    IPR001381 DHquinase_I

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF01487 DHquinase_I, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR01093 aroD, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS01028 DEHYDROQUINASE_I, 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.

    P24670-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKTVTVKNLI IGEGMPKIIV SLMGRDINSV KAEALAYREA TFDILEWRVD 
            60         70         80         90        100
    HFMDIASTQS VLTAARVIRD AMPDIPLLFT FRSAKEGGEQ TITTQHYLTL 
           110        120        130        140        150
    NRAAIDSGLV DMIDLELFTG DADVKATVDY AHAHNVYVVM SNHDFHQTPS 
           160        170        180        190        200
    AEEMVLRLRK MQALGADIPK IAVMPQSKHD VLTLLTATLE MQQHYADRPV 
           210        220        230        240        250
    ITMSMAKEGV ISRLAGEVFG SAATFGAVKQ ASAPGQIAVN DLRSVLMILH 

    NA
    Length:252
    Mass (Da):27,649
    Last modified:December 5, 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:iF9D4D4C86D18F17B
    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 conflicti156L → S in CAA38418 (PubMed:2045778).Curated1

    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
    		X54546 Genomic DNA Translation: CAA38418.1
    AL513382 Genomic DNA Translation: CAD02002.1
    AE014613 Genomic DNA Translation: AAO68886.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S15652

    NCBI Reference Sequences

    More...    RefSeqi    		NP_456161.1, NC_003198.1
    WP_000860215.1, NZ_UFRG01000003.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		AAO68886; AAO68886; t1231
    CAD02002; CAD02002; CAD02002

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		1248131

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		stt:t1231
    sty:STY1760

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|220341.7.peg.1771

    <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
    		X54546 Genomic DNA Translation: CAA38418.1
    AL513382 Genomic DNA Translation: CAD02002.1
    AE014613 Genomic DNA Translation: AAO68886.1
    PIRiS15652
    RefSeqiNP_456161.1, NC_003198.1
    WP_000860215.1, NZ_UFRG01000003.1

    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
    1GQNX-ray1.78A1-252[»]
    1L9WX-ray2.10A/B/C/D1-252[»]
    1QFEX-ray2.10A/B1-252[»]
    4CLMX-ray1.40A/B1-252[»]
    4CNNX-ray1.00A/B1-252[»]
    4CNOX-ray1.50A/B/C/D1-252[»]
    4CNPX-ray1.15A/B1-252[»]
    4UIOX-ray1.35A1-252[»]
    ProteinModelPortaliP24670
    SMRiP24670
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi220341.STY1760

    Proteomic databases

    PRIDEiP24670

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO68886; AAO68886; t1231
    CAD02002; CAD02002; CAD02002
    GeneIDi1248131
    KEGGistt:t1231
    sty:STY1760
    PATRICifig|220341.7.peg.1771

    Phylogenomic databases

    eggNOGiENOG4105FF2 Bacteria
    COG0710 LUCA
    HOGENOMiHOG000105514
    KOiK03785

    Enzyme and pathway databases

    UniPathwayi
    UPA00053;UER00086

    SABIO-RKiP24670

    Miscellaneous databases

    EvolutionaryTraceiP24670

    Family and domain databases

    CDDicd00502 DHQase_I, 1 hit
    Gene3Di3.20.20.70, 1 hit
    HAMAPiMF_00214 AroD, 1 hit
    InterProiView protein in InterPro
    IPR018508 3-dehydroquinate_DH_AS
    IPR013785 Aldolase_TIM
    IPR001381 DHquinase_I
    PfamiView protein in Pfam
    PF01487 DHquinase_I, 1 hit
    TIGRFAMsiTIGR01093 aroD, 1 hit
    PROSITEiView protein in PROSITE
    PS01028 DEHYDROQUINASE_I, 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 nameiAROD_SALTI
    <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: P24670
    <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: March 1, 1992
    Last sequence update: December 5, 2001
    Last modified: December 5, 2018
    This is version 141 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, Complete proteome

    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
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again