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Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). 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 a lys-170 at the active site.UniRule annotation4 Publications

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation2 Publications

Enzyme regulationi

Inhibited by sodium borohydride.1 Publication

Kineticsi

Kcat is 142 sec(-1) for dehydratase activity with 3-dehydroquinate (at pH 7 and 25 degrees Celsius).1 Publication

  1. KM=17 µM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius)1 Publication
  2. KM=18 µM for 3-dehydroquinate (at pH 7 and 25 degrees Celsius)1 Publication

    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, Tyr-sensitive (aroF), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroD)
    4. Quinate/shikimate dehydrogenase (ydiB), Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK)
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 2113-dehydroquinateUniRule annotation
    Binding sitei82 – 8213-dehydroquinateUniRule annotation
    Active sitei143 – 1431Proton donor/acceptorUniRule annotation1 Publication
    Active sitei170 – 1701Schiff-base intermediate with substrateUniRule annotation1 Publication
    Binding sitei213 – 21313-dehydroquinateUniRule annotation
    Binding sitei232 – 23213-dehydroquinateUniRule annotation
    Binding sitei236 – 23613-dehydroquinateUniRule annotation

    GO - Molecular functioni

    • 3-dehydroquinate dehydratase activity Source: UniProtKB
    • identical protein binding Source: EcoCyc

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciEcoCyc:AROD-MONOMER.
    ECOL316407:JW1683-MONOMER.
    MetaCyc:AROD-MONOMER.
    UniPathwayiUPA00053; UER00086.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-dehydroquinate dehydratase1 PublicationUniRule annotation (EC:4.2.1.10UniRule annotation2 Publications)
    Short name:
    3-dehydroquinase1 PublicationUniRule annotation
    Alternative name(s):
    Type I DHQase1 PublicationUniRule annotation
    Type I dehydroquinase1 PublicationUniRule annotation
    Short name:
    DHQ1UniRule annotation
    Gene namesi
    Name:aroD1 PublicationUniRule annotation
    Ordered Locus Names:b1693, JW1683
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10076. aroD.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi143 – 1431H → A: Loss of dehydratase activity. 1 Publication
    Mutagenesisi146 – 1461H → A: It retains full catalytic activity. 1 Publication
    Mutagenesisi170 – 1701K → A: Loss of dehydratase activity, but it is still able to bind substrate. 1 Publication
    Mutagenesisi205 – 2051M → L: It has little effect on the catalytic efficiency and affinity for 3-dehydroquinate. 1 Publication

    Chemistry

    ChEMBLiCHEMBL4709.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2522523-dehydroquinate dehydratasePRO_0000138794Add
    BLAST

    Proteomic databases

    PaxDbiP05194.
    PRIDEiP05194.

    2D gel databases

    SWISS-2DPAGEP05194.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    GO - Molecular functioni

    • identical protein binding Source: EcoCyc

    Protein-protein interaction databases

    IntActiP05194. 6 interactions.
    STRINGi511145.b1693.

    Chemistry

    BindingDBiP05194.

    Structurei

    3D structure databases

    ProteinModelPortaliP05194.
    SMRiP05194. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 4833-dehydroquinate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the type-I 3-dehydroquinase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105FF2. Bacteria.
    COG0710. LUCA.
    HOGENOMiHOG000105514.
    InParanoidiP05194.
    KOiK03785.
    OMAiLFTFRSK.
    PhylomeDBiP05194.

    Family and domain databases

    CDDicd00502. DHQase_I. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00214. AroD. 1 hit.
    InterProiIPR018508. 3-dehydroquinate_DH_AS.
    IPR013785. Aldolase_TIM.
    IPR001381. DHquinase_I.
    [Graphical view]
    PfamiPF01487. DHquinase_I. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01093. aroD. 1 hit.
    PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P05194-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD
    60 70 80 90 100
    HYADLSNVES VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL
    110 120 130 140 150
    NRAAIDSGLV DMIDLELFTG DDQVKETVAY AHAHDVKVVM SNHDFHKTPE
    160 170 180 190 200
    AEEIIARLRK MQSFDADIPK IALMPQSTSD VLTLLAATLE MQEQYADRPI
    210 220 230 240 250
    ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVN DLRTVLTILH

    QA
    Length:252
    Mass (Da):27,467
    Last modified:October 1, 1994 - v2
    Checksum:i0D4E7FAEAD5FCD48
    GO

    Mass spectrometryi

    Molecular mass is 27467 Da from positions 1 - 252. Determined by ESI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X59503 Genomic DNA. Translation: CAA42091.1.
    X04306 Genomic DNA. Translation: CAA27849.1. Sequence problems.
    U00096 Genomic DNA. Translation: AAC74763.1.
    AP009048 Genomic DNA. Translation: BAA15448.1.
    PIRiS14750. DWECDQ.
    RefSeqiNP_416208.1. NC_000913.3.
    WP_000860201.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74763; AAC74763; b1693.
    BAA15448; BAA15448; BAA15448.
    GeneIDi946210.
    KEGGiecj:JW1683.
    eco:b1693.
    PATRICi32118692. VBIEscCol129921_1764.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X59503 Genomic DNA. Translation: CAA42091.1.
    X04306 Genomic DNA. Translation: CAA27849.1. Sequence problems.
    U00096 Genomic DNA. Translation: AAC74763.1.
    AP009048 Genomic DNA. Translation: BAA15448.1.
    PIRiS14750. DWECDQ.
    RefSeqiNP_416208.1. NC_000913.3.
    WP_000860201.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP05194.
    SMRiP05194. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiP05194. 6 interactions.
    STRINGi511145.b1693.

    Chemistry

    BindingDBiP05194.
    ChEMBLiCHEMBL4709.

    2D gel databases

    SWISS-2DPAGEP05194.

    Proteomic databases

    PaxDbiP05194.
    PRIDEiP05194.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74763; AAC74763; b1693.
    BAA15448; BAA15448; BAA15448.
    GeneIDi946210.
    KEGGiecj:JW1683.
    eco:b1693.
    PATRICi32118692. VBIEscCol129921_1764.

    Organism-specific databases

    EchoBASEiEB0074.
    EcoGeneiEG10076. aroD.

    Phylogenomic databases

    eggNOGiENOG4105FF2. Bacteria.
    COG0710. LUCA.
    HOGENOMiHOG000105514.
    InParanoidiP05194.
    KOiK03785.
    OMAiLFTFRSK.
    PhylomeDBiP05194.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00086.
    BioCyciEcoCyc:AROD-MONOMER.
    ECOL316407:JW1683-MONOMER.
    MetaCyc:AROD-MONOMER.

    Miscellaneous databases

    PROiP05194.

    Family and domain databases

    CDDicd00502. DHQase_I. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00214. AroD. 1 hit.
    InterProiIPR018508. 3-dehydroquinate_DH_AS.
    IPR013785. Aldolase_TIM.
    IPR001381. DHquinase_I.
    [Graphical view]
    PfamiPF01487. DHquinase_I. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01093. aroD. 1 hit.
    PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROD_ECOLI
    AccessioniPrimary (citable) accession number: P05194
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 1, 1994
    Last modified: September 7, 2016
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

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