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 dehydratase

Gene

aroD

Organism
Salmonella typhi
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. 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

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by (2R)-2-methyl-3-dehydroquinic acid.1 Publication

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei21 – 2113-dehydroquinateUniRule annotation2 Publications
    Binding sitei82 – 8213-dehydroquinateUniRule annotation1 Publication
    Active sitei143 – 1431Proton donor/acceptorUniRule annotation1 Publication
    Active sitei170 – 1701Schiff-base intermediate with substrateUniRule annotation2 Publications
    Binding sitei213 – 21313-dehydroquinateUniRule annotation3 Publications
    Binding sitei232 – 23213-dehydroquinateUniRule annotation2 Publications
    Binding sitei236 – 23613-dehydroquinateUniRule annotation3 Publications

    GO - Molecular functioni

    • 3-dehydroquinate dehydratase activity Source: UniProtKB

    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

    SABIO-RKP24670.
    UniPathwayiUPA00053; UER00086.

    Names & Taxonomyi

    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
    Gene namesi
    Name:aroD1 PublicationUniRule annotation
    Ordered Locus Names:STY1760, t1231
    OrganismiSalmonella typhi
    Taxonomic identifieri90370 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000002670 Componenti: Chromosome UP000000541 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2522523-dehydroquinate dehydratasePRO_0000138805Add
    BLAST

    Interactioni

    Subunit structurei

    Dimer of dimers.UniRule annotation3 Publications

    Protein-protein interaction databases

    STRINGi220341.STY1760.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Beta strandi9 – 113Combined sources
    Beta strandi13 – 153Combined sources
    Beta strandi17 – 226Combined sources
    Helixi27 – 3711Combined sources
    Beta strandi43 – 486Combined sources
    Helixi49 – 513Combined sources
    Turni53 – 564Combined sources
    Helixi58 – 7114Combined sources
    Beta strandi77 – 804Combined sources
    Helixi84 – 863Combined sources
    Helixi94 – 10613Combined sources
    Beta strandi111 – 1166Combined sources
    Helixi117 – 1193Combined sources
    Helixi121 – 13313Combined sources
    Beta strandi137 – 14610Combined sources
    Helixi151 – 16313Combined sources
    Beta strandi167 – 1737Combined sources
    Helixi178 – 19417Combined sources
    Beta strandi201 – 2044Combined sources
    Helixi206 – 2149Combined sources
    Helixi216 – 2194Combined sources
    Beta strandi223 – 2253Combined sources
    Beta strandi227 – 2304Combined sources
    Helixi239 – 25113Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP24670.
    SMRiP24670. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24670.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 4833-dehydroquinate bindingUniRule annotation3 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0710.
    HOGENOMiHOG000105514.
    KOiK03785.
    OMAiLFTFRSK.
    OrthoDBiEOG6P33BK.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00214. AroD.
    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.

    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
    Checksum:iF9D4D4C86D18F17B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti156 – 1561L → S in CAA38418 (PubMed:2045778).Curated

    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.

    Genome annotation databases

    EnsemblBacteriaiAAO68886; AAO68886; t1231.
    CAD02002; CAD02002; CAD02002.
    GeneIDi1248131.
    KEGGisty:STY1760.
    PATRICi18541418. VBISalEnt120419_1771.

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP24670.
    SMRiP24670. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi220341.STY1760.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAO68886; AAO68886; t1231.
    CAD02002; CAD02002; CAD02002.
    GeneIDi1248131.
    KEGGisty:STY1760.
    PATRICi18541418. VBISalEnt120419_1771.

    Phylogenomic databases

    eggNOGiCOG0710.
    HOGENOMiHOG000105514.
    KOiK03785.
    OMAiLFTFRSK.
    OrthoDBiEOG6P33BK.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00086.
    SABIO-RKP24670.

    Miscellaneous databases

    EvolutionaryTraceiP24670.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00214. AroD.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Molecular cloning and characterization of the aroD gene encoding 3-dehydroquinase from Salmonella typhi."
      Servos S., Chatfield S., Hone D., Levine M., Dimitriadis G., Pickard D., Dougan G., Fairweather N., Charles I.G.
      J. Gen. Microbiol. 137:147-152(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 700931 / Ty2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CT18.
    3. "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
      Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
      J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700931 / Ty2.
    4. "The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction."
      Gourley D.G., Shrive A.K., Polikarpov I., Krell T., Coggins J.R., Hawkins A.R., Isaacs N.W., Sawyer L.
      Nat. Struct. Biol. 6:521-525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROQUINATE, SUBUNIT, ACTIVE SITE.
    5. "Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity."
      Lee W.H., Perles L.A., Nagem R.A., Shrive A.K., Hawkins A., Sawyer L., Polikarpov I.
      Acta Crystallogr. D 58:798-804(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH 3-DEHYDROSHIKIMATE, ACTIVE SITE, SUBUNIT.
    6. "Insights into substrate binding and catalysis in bacterial type I dehydroquinase."
      Maneiro M., Peon A., Lence E., Otero J.M., Van Raaij M.J., Thompson P., Hawkins A.R., Gonzalez-Bello C.
      Biochem. J. 462:415-424(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiAROD_SALTI
    AccessioniPrimary (citable) accession number: P24670
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: December 5, 2001
    Last modified: May 27, 2015
    This is version 118 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

    3D-structure, Complete 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

    External Data

    Dasty 3

    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 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.