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P24670

- AROD_SALTI

UniProt

P24670 - AROD_SALTI

Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Salmonella typhi
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (05 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei82 – 821Substrate
    Active sitei143 – 1431Proton donor/acceptor
    Active sitei170 – 1701Schiff-base intermediate with substrate
    Binding sitei213 – 2131Substrate
    Binding sitei232 – 2321Substrate
    Binding sitei236 – 2361Substrate

    GO - Molecular functioni

    1. 3-dehydroquinate dehydratase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
    2. chorismate biosynthetic process Source: UniProtKB-UniPathway

    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 dehydrataseUniRule annotation (EC:4.2.1.10UniRule annotation)
    Short name:
    3-dehydroquinaseUniRule annotation
    Alternative name(s):
    Type I DHQaseUniRule annotation
    Gene namesi
    Name:aroDUniRule annotation
    Ordered Locus Names:STY1760, t1231
    OrganismiSalmonella typhi
    Taxonomic identifieri90370 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000000541: Chromosome, UP000002670: Chromosome

    PTM / Processingi

    Molecule processing

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

    Interactioni

    Subunit structurei

    Homodimer.2 PublicationsUniRule annotation

    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 – 63
    Beta strandi9 – 113
    Beta strandi13 – 153
    Beta strandi17 – 226
    Helixi27 – 3711
    Beta strandi43 – 486
    Helixi49 – 513
    Turni53 – 564
    Helixi58 – 7114
    Beta strandi77 – 804
    Helixi84 – 863
    Helixi94 – 10714
    Beta strandi111 – 1166
    Helixi117 – 1193
    Helixi121 – 13313
    Beta strandi137 – 14610
    Helixi151 – 16313
    Beta strandi167 – 1737
    Helixi178 – 19417
    Beta strandi201 – 2044
    Turni206 – 2094
    Helixi210 – 2145
    Helixi216 – 2194
    Beta strandi223 – 2253
    Beta strandi227 – 2304
    Helixi239 – 25012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GQNX-ray1.78A1-252[»]
    1L9WX-ray2.10A/B/C/D1-252[»]
    1QFEX-ray2.10A/B1-252[»]
    ProteinModelPortaliP24670.
    SMRiP24670. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24670.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni46 – 483Substrate binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0710.
    HOGENOMiHOG000105514.
    KOiK03785.
    OMAiEGMPKII.
    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

    MKTVTVKNLI IGEGMPKIIV SLMGRDINSV KAEALAYREA TFDILEWRVD    50
    HFMDIASTQS VLTAARVIRD AMPDIPLLFT FRSAKEGGEQ TITTQHYLTL 100
    NRAAIDSGLV DMIDLELFTG DADVKATVDY AHAHNVYVVM SNHDFHQTPS 150
    AEEMVLRLRK MQALGADIPK IAVMPQSKHD VLTLLTATLE MQQHYADRPV 200
    ITMSMAKEGV ISRLAGEVFG SAATFGAVKQ ASAPGQIAVN DLRSVLMILH 250
    NA 252
    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:
    EMBL
    GenBank
    DDBJ
    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.
    NP_805037.1. NC_004631.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54546 Genomic DNA. Translation: CAA38418.1 .
    AL513382 Genomic DNA. Translation: CAD02002.1 .
    AE014613 Genomic DNA. Translation: AAO68886.1 .
    PIRi S15652.
    RefSeqi NP_456161.1. NC_003198.1.
    NP_805037.1. NC_004631.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GQN X-ray 1.78 A 1-252 [» ]
    1L9W X-ray 2.10 A/B/C/D 1-252 [» ]
    1QFE X-ray 2.10 A/B 1-252 [» ]
    ProteinModelPortali P24670.
    SMRi P24670. Positions 1-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 220341.STY1760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO68886 ; AAO68886 ; t1231 .
    CAD02002 ; CAD02002 ; CAD02002 .
    GeneIDi 1248131.
    KEGGi sty:STY1760.
    PATRICi 18541418. VBISalEnt120419_1771.

    Phylogenomic databases

    eggNOGi COG0710.
    HOGENOMi HOG000105514.
    KOi K03785.
    OMAi EGMPKII.
    OrthoDBi EOG6P33BK.

    Enzyme and pathway databases

    UniPathwayi UPA00053 ; UER00086 .
    SABIO-RK P24670.

    Miscellaneous databases

    EvolutionaryTracei P24670.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00214. AroD.
    InterProi IPR018508. 3-dehydroquinate_DH_AS.
    IPR013785. Aldolase_TIM.
    IPR001381. DHquinase_I.
    [Graphical view ]
    Pfami PF01487. DHquinase_I. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01093. aroD. 1 hit.
    PROSITEi PS01028. DEHYDROQUINASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 114 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