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Protein

3-dehydroquinate dehydratase

Gene

aroQ

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a trans-dehydration via an enolate intermediate.By similarity

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.

Kineticsi

  1. KM=1100 µM for 3-dehydroquinate (at pH 8 and 25 degrees Celsius)

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 3 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 (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase (SCO3210)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. no protein annotated in this organism
    5. Shikimate kinase (aroK)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase 1 (aroA1), 3-phosphoshikimate 1-carboxyvinyltransferase 2 (aroA2)
    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
    Sitei24 – 241Transition state stabilizer
    Active sitei29 – 291Proton acceptor
    Binding sitei80 – 801Substrate
    Binding sitei86 – 861Substrate
    Binding sitei93 – 931Substrate
    Active sitei107 – 1071Proton donor
    Binding sitei118 – 1181Substrate

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Enzyme and pathway databases

    BRENDAi4.2.1.10. 5998.
    SABIO-RKP15474.
    UniPathwayiUPA00053; UER00086.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-dehydroquinate dehydratase (EC:4.2.1.10)
    Short name:
    3-dehydroquinase
    Alternative name(s):
    Type II DHQase
    Gene namesi
    Name:aroQ
    Ordered Locus Names:SCO1961
    ORF Names:SCC54.21c
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 241R → A: Reduces Kcat 30000-fold. Reduces KM for 3-dehydroquinate 6-fold. 1 Publication
    Mutagenesisi24 – 241R → K: Reduces Kcat 2700-fold. Reduces KM for 3-dehydroquinate 4-fold. 1 Publication
    Mutagenesisi24 – 241R → Q: Reduces Kcat 3100-fold. Reduces KM for 3-dehydroquinate 8-fold. 1 Publication

    Chemistry

    ChEMBLiCHEMBL5276.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 1571563-dehydroquinate dehydratasePRO_0000159930Add
    BLAST

    Proteomic databases

    PRIDEiP15474.

    Interactioni

    Subunit structurei

    Homododecamer.3 Publications

    Protein-protein interaction databases

    STRINGi100226.SCO1961.

    Chemistry

    BindingDBiP15474.

    Structurei

    Secondary structure

    1
    157
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni5 – 73Combined sources
    Beta strandi10 – 145Combined sources
    Helixi18 – 203Combined sources
    Turni21 – 233Combined sources
    Helixi26 – 294Combined sources
    Helixi34 – 4613Combined sources
    Turni47 – 493Combined sources
    Beta strandi52 – 565Combined sources
    Helixi60 – 7314Combined sources
    Beta strandi75 – 806Combined sources
    Helixi84 – 874Combined sources
    Helixi89 – 968Combined sources
    Beta strandi103 – 1097Combined sources
    Helixi111 – 1133Combined sources
    Helixi116 – 1183Combined sources
    Helixi123 – 1253Combined sources
    Beta strandi128 – 1347Combined sources
    Helixi137 – 15014Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D0IX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GTZX-ray1.60A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU0X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU1X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1V1JX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    2BT4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    2CJFX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    ProteinModelPortaliP15474.
    SMRiP15474. Positions 2-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15474.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 1092Substrate binding

    Sequence similaritiesi

    Belongs to the type-II 3-dehydroquinase family.Curated

    Phylogenomic databases

    eggNOGiENOG4108Z38. Bacteria.
    COG0757. LUCA.
    HOGENOMiHOG000217278.
    InParanoidiP15474.
    KOiK03786.
    OMAiWIQEAGD.
    OrthoDBiPOG091H03XJ.
    PhylomeDBiP15474.

    Family and domain databases

    CDDicd00466. DHQase_II. 1 hit.
    Gene3Di3.40.50.9100. 1 hit.
    HAMAPiMF_00169. AroQ. 1 hit.
    InterProiIPR001874. DHquinase_II.
    IPR018509. DHquinase_II_CS.
    [Graphical view]
    PANTHERiPTHR21272. PTHR21272. 1 hit.
    PfamiPF01220. DHquinase_II. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001399. DHquinase_II. 1 hit.
    ProDomiPD004527. DHquinase_II. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF52304. SSF52304. 1 hit.
    TIGRFAMsiTIGR01088. aroQ. 1 hit.
    PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15474-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPRSLANAPI MILNGPNLNL LGQRQPEIYG SDTLADVEAL CVKAAAAHGG
    60 70 80 90 100
    TVDFRQSNHE GELVDWIHEA RLNHCGIVIN PAAYSHTSVA ILDALNTCDG
    110 120 130 140 150
    LPVVEVHISN IHQREPFRHH SYVSQRADGV VAGCGVQGYV FGVERIAALA

    GAGSARA
    Length:157
    Mass (Da):16,682
    Last modified:January 23, 2007 - v3
    Checksum:i61D9F95C7E2C67EB
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ001493 Genomic DNA. Translation: CAA04787.1.
    AL939110 Genomic DNA. Translation: CAB38151.1.
    PIRiS08196.
    T35990.
    RefSeqiNP_626225.1. NC_003888.3.
    WP_003976858.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAB38151; CAB38151; CAB38151.
    GeneIDi1097395.
    KEGGisco:SCO1961.
    PATRICi23733554. VBIStrCoe124346_1987.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ001493 Genomic DNA. Translation: CAA04787.1.
    AL939110 Genomic DNA. Translation: CAB38151.1.
    PIRiS08196.
    T35990.
    RefSeqiNP_626225.1. NC_003888.3.
    WP_003976858.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D0IX-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GTZX-ray1.60A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU0X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1GU1X-ray1.80A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    1V1JX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L2-157[»]
    2BT4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    2CJFX-ray1.95A/B/C/D/E/F/G/H/I/J/K/L1-157[»]
    ProteinModelPortaliP15474.
    SMRiP15474. Positions 2-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO1961.

    Chemistry

    BindingDBiP15474.
    ChEMBLiCHEMBL5276.

    Proteomic databases

    PRIDEiP15474.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB38151; CAB38151; CAB38151.
    GeneIDi1097395.
    KEGGisco:SCO1961.
    PATRICi23733554. VBIStrCoe124346_1987.

    Phylogenomic databases

    eggNOGiENOG4108Z38. Bacteria.
    COG0757. LUCA.
    HOGENOMiHOG000217278.
    InParanoidiP15474.
    KOiK03786.
    OMAiWIQEAGD.
    OrthoDBiPOG091H03XJ.
    PhylomeDBiP15474.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00086.
    BRENDAi4.2.1.10. 5998.
    SABIO-RKP15474.

    Miscellaneous databases

    EvolutionaryTraceiP15474.
    PROiP15474.

    Family and domain databases

    CDDicd00466. DHQase_II. 1 hit.
    Gene3Di3.40.50.9100. 1 hit.
    HAMAPiMF_00169. AroQ. 1 hit.
    InterProiIPR001874. DHquinase_II.
    IPR018509. DHquinase_II_CS.
    [Graphical view]
    PANTHERiPTHR21272. PTHR21272. 1 hit.
    PfamiPF01220. DHquinase_II. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001399. DHquinase_II. 1 hit.
    ProDomiPD004527. DHquinase_II. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF52304. SSF52304. 1 hit.
    TIGRFAMsiTIGR01088. aroQ. 1 hit.
    PROSITEiPS01029. DEHYDROQUINASE_II. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROQ_STRCO
    AccessioniPrimary (citable) accession number: P15474
    Secondary accession number(s): O33608
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: September 7, 2016
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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