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P58687

- AROD_SALTY

UniProt

P58687 - AROD_SALTY

Protein

3-dehydroquinate dehydratase

Gene

aroD

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (31 Jan 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    3-dehydroquinate = 3-dehydroshikimate + H2O.2 PublicationsUniRule 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

    BioCyciSENT99287:GCTI-1368-MONOMER.
    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:STM1358
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi170 – 1701K → M: Abolishes enzyme activity. 1 Publication
    Mutagenesisi232 – 2321S → A: Reduces enzyme activity 50-fold. 1 Publication
    Mutagenesisi236 – 2361Q → A: Nearly abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2522523-dehydroquinate dehydratasePRO_0000138806Add
    BLAST

    Proteomic databases

    PRIDEiP58687.

    Interactioni

    Subunit structurei

    Homodimer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi99287.STM1358.

    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
    Helixi207 – 2104
    Helixi211 – 2144
    Helixi216 – 2194
    Beta strandi223 – 2253
    Beta strandi227 – 2293
    Helixi239 – 25113

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L2IX-ray1.85A/B1-252[»]
    3LB0X-ray1.65A/B1-252[»]
    3M7WX-ray1.95A/B/C/D/E/F1-252[»]
    3NNTX-ray1.60A/B1-252[»]
    3O1NX-ray1.03A/B1-252[»]
    3OEXX-ray1.90A/B/C/D1-252[»]
    3S42X-ray1.45A/B1-252[»]
    4GFSX-ray1.80A/B1-252[»]
    4GUFX-ray1.50A/B1-252[»]
    4GUGX-ray1.62A/B1-252[»]
    4GUHX-ray1.95A/B1-252[»]
    4GUIX-ray1.78A/B1-252[»]
    4GUJX-ray1.50A/B1-252[»]
    4IUOX-ray1.80A/B1-252[»]
    ProteinModelPortaliP58687.
    SMRiP58687. Positions 1-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP58687.

    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

    HOGENOMiHOG000105514.
    KOiK03785.
    OMAiEGMPKII.
    OrthoDBiEOG6P33BK.
    PhylomeDBiP58687.

    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.

    P58687-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTVTVRDLV VGEGAPKIIV SLMGKTITDV KSEALAYREA DFDILEWRVD    50
    HFANVTTAES VLEAAGAIRE IITDKPLLFT FRSAKEGGEQ ALTTGQYIDL 100
    NRAAVDSGLV DMIDLELFTG DDEVKATVGY AHQHNVAVIM SNHDFHKTPA 150
    AEEIVQRLRK MQELGADIPK IAVMPQTKAD VLTLLTATVE MQERYADRPI 200
    ITMSMSKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVA DLRTVLTILH 250
    QA 252
    Length:252
    Mass (Da):27,325
    Last modified:January 31, 2002 - v1
    Checksum:i10BB561E38EA0A75
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL20283.1.
    RefSeqiNP_460324.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL20283; AAL20283; STM1358.
    GeneIDi1252876.
    KEGGistm:STM1358.
    PATRICi32381199. VBISalEnt20916_1442.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE006468 Genomic DNA. Translation: AAL20283.1 .
    RefSeqi NP_460324.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L2I X-ray 1.85 A/B 1-252 [» ]
    3LB0 X-ray 1.65 A/B 1-252 [» ]
    3M7W X-ray 1.95 A/B/C/D/E/F 1-252 [» ]
    3NNT X-ray 1.60 A/B 1-252 [» ]
    3O1N X-ray 1.03 A/B 1-252 [» ]
    3OEX X-ray 1.90 A/B/C/D 1-252 [» ]
    3S42 X-ray 1.45 A/B 1-252 [» ]
    4GFS X-ray 1.80 A/B 1-252 [» ]
    4GUF X-ray 1.50 A/B 1-252 [» ]
    4GUG X-ray 1.62 A/B 1-252 [» ]
    4GUH X-ray 1.95 A/B 1-252 [» ]
    4GUI X-ray 1.78 A/B 1-252 [» ]
    4GUJ X-ray 1.50 A/B 1-252 [» ]
    4IUO X-ray 1.80 A/B 1-252 [» ]
    ProteinModelPortali P58687.
    SMRi P58687. Positions 1-252.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM1358.

    Proteomic databases

    PRIDEi P58687.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL20283 ; AAL20283 ; STM1358 .
    GeneIDi 1252876.
    KEGGi stm:STM1358.
    PATRICi 32381199. VBISalEnt20916_1442.

    Phylogenomic databases

    HOGENOMi HOG000105514.
    KOi K03785.
    OMAi EGMPKII.
    OrthoDBi EOG6P33BK.
    PhylomeDBi P58687.

    Enzyme and pathway databases

    UniPathwayi UPA00053 ; UER00086 .
    BioCyci SENT99287:GCTI-1368-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P58687.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    2. "New insights into the mechanism of the Schiff base hydrolysis catalyzed by type I dehydroquinate dehydratase from S. enterica: a theoretical study."
      Yao Y., Li Z.S.
      Org. Biomol. Chem. 10:7037-7044(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.
    3. "A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding."
      Light S.H., Minasov G., Shuvalova L., Peterson S.N., Caffrey M., Anderson W.F., Lavie A.
      Biochemistry 50:2357-2363(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.03 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF SER-232 AND GLN-236.
    4. "Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates."
      Light S.H., Minasov G., Shuvalova L., Duban M.E., Caffrey M., Anderson W.F., Lavie A.
      J. Biol. Chem. 286:3531-3539(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF WILD-TYPE AND MUTANT MET-170 IN COMPLEX WITH 3-DEHYDROQUINIC ACID, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, MUTAGENESIS OF LYS-170.

    Entry informationi

    Entry nameiAROD_SALTY
    AccessioniPrimary (citable) accession number: P58687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 90 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

    3D-structure, Complete proteome, 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

    External Data

    Dasty 3