Skip Header

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

3-dehydroquinate synthase

Gene

aroB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • NAD+1 Publication
  • Co2+1 Publication, Zn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Displays higher activity with Co2+, however, Zn2+ may be the physiological metal cofactor.1 Publication

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.
    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.

    GO - Molecular functioni

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

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: EcoliWiki
    • chorismate biosynthetic process Source: GO_Central
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    Cobalt, NAD, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:AROB-MONOMER.
    ECOL316407:JW3352-MONOMER.
    MetaCyc:AROB-MONOMER.
    BRENDAi4.2.3.4. 2026.
    UniPathwayiUPA00053; UER00085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-dehydroquinate synthase (EC:4.2.3.41 Publication)
    Gene namesi
    Name:aroB
    Ordered Locus Names:b3389, JW3352
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10074. aroB.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Chemistry

    ChEMBLiCHEMBL3554.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3623623-dehydroquinate synthasePRO_0000140737Add
    BLAST

    Proteomic databases

    EPDiP07639.
    PaxDbiP07639.
    PRIDEiP07639.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi4259296. 37 interactions.
    DIPiDIP-9150N.
    IntActiP07639. 9 interactions.
    MINTiMINT-1261041.
    STRINGi511145.b3389.

    Chemistry

    BindingDBiP07639.

    Structurei

    3D structure databases

    ProteinModelPortaliP07639.
    SMRiP07639. Positions 1-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the dehydroquinate synthase family.Curated

    Phylogenomic databases

    eggNOGiENOG4105D49. Bacteria.
    COG0337. LUCA.
    HOGENOMiHOG000007970.
    InParanoidiP07639.
    KOiK01735.
    OMAiTHLGYGN.
    PhylomeDBiP07639.

    Family and domain databases

    HAMAPiMF_00110. DHQ_synthase. 1 hit.
    InterProiIPR016037. DHQ_synth_AroB.
    IPR030963. DHQ_synth_fam.
    IPR030960. DHQS/DOIS.
    [Graphical view]
    PfamiPF01761. DHQ_synthase. 1 hit.
    [Graphical view]
    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.
    PATRICi32122210. VBIEscCol129921_3482.

    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. Positions 1-361.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259296. 37 interactions.
    DIPiDIP-9150N.
    IntActiP07639. 9 interactions.
    MINTiMINT-1261041.
    STRINGi511145.b3389.

    Chemistry

    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.
    PATRICi32122210. VBIEscCol129921_3482.

    Organism-specific databases

    EchoBASEiEB0072.
    EcoGeneiEG10074. aroB.

    Phylogenomic databases

    eggNOGiENOG4105D49. Bacteria.
    COG0337. LUCA.
    HOGENOMiHOG000007970.
    InParanoidiP07639.
    KOiK01735.
    OMAiTHLGYGN.
    PhylomeDBiP07639.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00085.
    BioCyciEcoCyc:AROB-MONOMER.
    ECOL316407:JW3352-MONOMER.
    MetaCyc:AROB-MONOMER.
    BRENDAi4.2.3.4. 2026.

    Miscellaneous databases

    PROiP07639.

    Family and domain databases

    HAMAPiMF_00110. DHQ_synthase. 1 hit.
    InterProiIPR016037. DHQ_synth_AroB.
    IPR030963. DHQ_synth_fam.
    IPR030960. DHQS/DOIS.
    [Graphical view]
    PfamiPF01761. DHQ_synthase. 1 hit.
    [Graphical view]
    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 historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: September 7, 2016
    This is version 148 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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.