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Protein

3-dehydroquinate synthase

Gene

aroB

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

Functioni

Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).UniRule annotation1 Publication

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.UniRule annotation1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=0.6 µM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 6.5)1 Publication
  2. KM=5.5 µM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 8.5)1 Publication

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 2 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, Phe-sensitive (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), Quinate/shikimate dehydrogenase (ydiB)
    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)DescriptionActionsGraphical viewLength
    Binding sitei142NAD; via carbonyl oxygenUniRule annotation1
    Binding sitei151NADUniRule annotation1
    Metal bindingi184Cobalt or zincUniRule annotation1
    Metal bindingi247Cobalt or zinc; via tele nitrogenUniRule annotation1
    Metal bindingi264Cobalt or zinc; via tele nitrogenUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi71 – 76NADUniRule annotation6
    Nucleotide bindingi105 – 109NADUniRule annotation5
    Nucleotide bindingi129 – 130NADUniRule annotation2
    Nucleotide bindingi169 – 172NADUniRule annotation4

    GO - Molecular functioni

    • 3-dehydroquinate synthase activity Source: EcoCyc
    • NAD+ binding Source: EcoCyc
    • zinc ion binding Source: EcoCyc

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: GO_Central
    • chorismate biosynthetic process Source: UniProtKB-UniPathway

    Keywordsi

    Molecular functionLyase
    Biological processAmino-acid biosynthesis, Aromatic amino acid biosynthesis
    LigandCobalt, Metal-binding, NAD, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:AROB-MONOMER
    MetaCyc:AROB-MONOMER
    BRENDAi4.2.3.4 2026
    UniPathwayi
    UPA00053;UER00085

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-dehydroquinate synthaseUniRule annotationCurated (EC:4.2.3.4UniRule annotation1 Publication)
    Short name:
    DHQSUniRule annotationCurated
    Gene namesi
    Name:aroBUniRule annotation
    Ordered Locus Names:b3389, JW3352
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10074 aroB

    Subcellular locationi

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL3554

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001407371 – 3623-dehydroquinate synthaseAdd BLAST362

    Proteomic databases

    EPDiP07639
    PaxDbiP07639
    PRIDEiP07639

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fixXP686462EBI-550843,EBI-1113234

    Protein-protein interaction databases

    BioGridi4259296, 55 interactors
    DIPiDIP-9150N
    IntActiP07639, 9 interactors
    STRINGi316385.ECDH10B_3564

    Chemistry databases

    BindingDBiP07639

    Structurei

    3D structure databases

    ProteinModelPortaliP07639
    SMRiP07639
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.UniRule annotationCurated

    Phylogenomic databases

    eggNOGiENOG4105D49 Bacteria
    COG0337 LUCA
    HOGENOMiHOG000007970
    InParanoidiP07639
    KOiK01735
    PhylomeDBiP07639

    Family and domain databases

    HAMAPiMF_00110 DHQ_synthase, 1 hit
    InterProiView protein in InterPro
    IPR016037 DHQ_synth_AroB
    IPR030963 DHQ_synth_fam
    IPR030960 DHQS/DOIS
    PfamiView protein in Pfam
    PF01761 DHQ_synthase, 1 hit
    PIRSFiPIRSF001455 DHQ_synth, 1 hit
    TIGRFAMsiTIGR01357 aroB, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P07639-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MERIVVTLGE RSYPITIASG LFNEPASFLP LKSGEQVMLV TNETLAPLYL
    60 70 80 90 100
    DKVRGVLEQA GVNVDSVILP DGEQYKSLAV LDTVFTALLQ KPHGRDTTLV
    110 120 130 140 150
    ALGGGVVGDL TGFAAASYQR GVRFIQVPTT LLSQVDSSVG GKTAVNHPLG
    160 170 180 190 200
    KNMIGAFYQP ASVVVDLDCL KTLPPRELAS GLAEVIKYGI ILDGAFFNWL
    210 220 230 240 250
    EENLDALLRL DGPAMAYCIR RCCELKAEVV AADERETGLR ALLNLGHTFG
    260 270 280 290 300
    HAIEAEMGYG NWLHGEAVAA GMVMAARTSE RLGQFSSAET QRIITLLKRA
    310 320 330 340 350
    GLPVNGPREM SAQAYLPHML RDKKVLAGEM RLILPLAIGK SEVRSGVSHE
    360
    LVLNAIADCQ SA
    Length:362
    Mass (Da):38,881
    Last modified:April 1, 1988 - v1
    Checksum:iF67496010D5C9182
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03867 Genomic DNA Translation: CAA27495.1
    Z19601 Genomic DNA Translation: CAA79666.1
    U18997 Genomic DNA Translation: AAA58186.1
    U00096 Genomic DNA Translation: AAC76414.1
    AP009048 Genomic DNA Translation: BAE77902.1
    X15162 Genomic DNA Translation: CAA33252.1
    PIRiA24863 SYECQ
    RefSeqiNP_417848.1, NC_000913.3
    WP_000439848.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC76414; AAC76414; b3389
    BAE77902; BAE77902; BAE77902
    GeneIDi947927
    KEGGiecj:JW3352
    eco:b3389
    PATRICifig|1411691.4.peg.3341

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X03867 Genomic DNA Translation: CAA27495.1
    Z19601 Genomic DNA Translation: CAA79666.1
    U18997 Genomic DNA Translation: AAA58186.1
    U00096 Genomic DNA Translation: AAC76414.1
    AP009048 Genomic DNA Translation: BAE77902.1
    X15162 Genomic DNA Translation: CAA33252.1
    PIRiA24863 SYECQ
    RefSeqiNP_417848.1, NC_000913.3
    WP_000439848.1, NZ_LN832404.1

    3D structure databases

    ProteinModelPortaliP07639
    SMRiP07639
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259296, 55 interactors
    DIPiDIP-9150N
    IntActiP07639, 9 interactors
    STRINGi316385.ECDH10B_3564

    Chemistry databases

    BindingDBiP07639
    ChEMBLiCHEMBL3554

    Proteomic databases

    EPDiP07639
    PaxDbiP07639
    PRIDEiP07639

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76414; AAC76414; b3389
    BAE77902; BAE77902; BAE77902
    GeneIDi947927
    KEGGiecj:JW3352
    eco:b3389
    PATRICifig|1411691.4.peg.3341

    Organism-specific databases

    EchoBASEiEB0072
    EcoGeneiEG10074 aroB

    Phylogenomic databases

    eggNOGiENOG4105D49 Bacteria
    COG0337 LUCA
    HOGENOMiHOG000007970
    InParanoidiP07639
    KOiK01735
    PhylomeDBiP07639

    Enzyme and pathway databases

    UniPathwayi
    UPA00053;UER00085

    BioCyciEcoCyc:AROB-MONOMER
    MetaCyc:AROB-MONOMER
    BRENDAi4.2.3.4 2026

    Miscellaneous databases

    PROiPR:P07639

    Family and domain databases

    HAMAPiMF_00110 DHQ_synthase, 1 hit
    InterProiView protein in InterPro
    IPR016037 DHQ_synth_AroB
    IPR030963 DHQ_synth_fam
    IPR030960 DHQS/DOIS
    PfamiView protein in Pfam
    PF01761 DHQ_synthase, 1 hit
    PIRSFiPIRSF001455 DHQ_synth, 1 hit
    TIGRFAMsiTIGR01357 aroB, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROB_ECOLI
    AccessioniPrimary (citable) accession number: P07639
    Secondary accession number(s): Q2M754
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: November 7, 2018
    This is version 160 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

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