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

Shikimate dehydrogenase (NADP(+))

Gene

aroE

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

Functioni

Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD.UniRule annotation2 Publications

Catalytic activityi

Shikimate + NADP+ = 3-dehydroshikimate + NADPH.UniRule annotation1 Publication

Kineticsi

Kcat is 14.2 min(-1) for dehydrogenase activity with NADP or shikimate.1 Publication

Manual assertion based on experiment ini

  1. KM=56 µM for NADP1 Publication
  2. KM=65 µM for shikimate1 Publication

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
    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.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei61ShikimateUniRule annotation1
    Active sitei65Proton acceptorUniRule annotation1
    Binding sitei77NADPUniRule annotation1
    Binding sitei86ShikimateUniRule annotation1
    Binding sitei102ShikimateUniRule annotation1
    Binding sitei213NADP; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei215ShikimateUniRule annotation1
    Binding sitei237NADP; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei244ShikimateUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi126 – 130NADPUniRule annotation1 Publication5
    Nucleotide bindingi149 – 154NADPUniRule annotation1 Publication6

    GO - Molecular functioni

    • NADP binding Source: EcoCyc
    • nucleotide binding Source: EcoCyc
    • shikimate 3-dehydrogenase (NADP+) activity Source: EcoCyc

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
    • cellular amino acid biosynthetic process Source: UniProtKB-KW
    • chorismate biosynthetic process Source: EcoCyc
    • shikimate metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:AROE-MONOMER.
    ECOL316407:JW3242-MONOMER.
    MetaCyc:AROE-MONOMER.
    SABIO-RKP15770.
    UniPathwayiUPA00053; UER00087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate dehydrogenase (NADP(+))1 Publication (EC:1.1.1.251 Publication)
    Short name:
    SD1 Publication
    Short name:
    SDHUniRule annotation
    Gene namesi
    Name:aroE1 PublicationUniRule annotation
    Ordered Locus Names:b3281, JW3242
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10077. aroE.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: EcoCyc
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001360021 – 272Shikimate dehydrogenase (NADP(+))Add BLAST272

    Proteomic databases

    PaxDbiP15770.
    PRIDEiP15770.

    Interactioni

    Subunit structurei

    Monomer or homodimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi4261870. 136 interactors.
    DIPiDIP-9153N.
    IntActiP15770. 6 interactors.
    MINTiMINT-1246863.
    STRINGi511145.b3281.

    Structurei

    Secondary structure

    1272
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 10Combined sources8
    Helixi16 – 27Combined sources12
    Beta strandi33 – 37Combined sources5
    Helixi43 – 52Combined sources10
    Beta strandi57 – 60Combined sources4
    Helixi65 – 71Combined sources7
    Beta strandi73 – 75Combined sources3
    Helixi77 – 82Combined sources6
    Beta strandi86 – 90Combined sources5
    Beta strandi96 – 99Combined sources4
    Helixi102 – 112Combined sources11
    Beta strandi121 – 125Combined sources5
    Helixi129 – 140Combined sources12
    Beta strandi144 – 148Combined sources5
    Helixi152 – 161Combined sources10
    Helixi163 – 165Combined sources3
    Beta strandi166 – 170Combined sources5
    Helixi174 – 176Combined sources3
    Beta strandi182 – 186Combined sources5
    Helixi191 – 193Combined sources3
    Helixi201 – 203Combined sources3
    Beta strandi209 – 213Combined sources5
    Helixi221 – 228Combined sources8
    Beta strandi233 – 235Combined sources3
    Helixi238 – 253Combined sources16
    Helixi259 – 270Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NYTX-ray1.50A/B/C/D1-271[»]
    ProteinModelPortaliP15770.
    SMRiP15770.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15770.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni14 – 16Shikimate bindingUniRule annotation3

    Sequence similaritiesi

    Belongs to the shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237876.
    InParanoidiP15770.
    KOiK00014.
    OMAiFGNPIKH.
    PhylomeDBiP15770.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR011342. Shikimate_DH.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF01488. Shikimate_DH. 1 hit.
    PF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00507. aroE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P15770-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    METYAVFGNP IAHSKSPFIH QQFAQQLNIE HPYGRVLAPI NDFINTLNAF
    60 70 80 90 100
    FSAGGKGANV TVPFKEEAFA RADELTERAA LAGAVNTLMR LEDGRLLGDN
    110 120 130 140 150
    TDGVGLLSDL ERLSFIRPGL RILLIGAGGA SRGVLLPLLS LDCAVTITNR
    160 170 180 190 200
    TVSRAEELAK LFAHTGSIQA LSMDELEGHE FDLIINATSS GISGDIPAIP
    210 220 230 240 250
    SSLIHPGIYC YDMFYQKGKT PFLAWCEQRG SKRNADGLGM LVAQAAHAFL
    260 270
    LWHGVLPDVE PVIKQLQEEL SA
    Length:272
    Mass (Da):29,414
    Last modified:April 1, 1990 - v1
    Checksum:i62D3797ECA1EC1E8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00710 Genomic DNA. Translation: CAA68700.1.
    U18997 Genomic DNA. Translation: AAA58078.1.
    U00096 Genomic DNA. Translation: AAC76306.1.
    AP009048 Genomic DNA. Translation: BAE78010.1.
    PIRiS00252.
    RefSeqiNP_417740.1. NC_000913.3.
    WP_000451243.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76306; AAC76306; b3281.
    BAE78010; BAE78010; BAE78010.
    GeneIDi947776.
    KEGGiecj:JW3242.
    eco:b3281.
    PATRICi32121996. VBIEscCol129921_3375.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Y00710 Genomic DNA. Translation: CAA68700.1.
    U18997 Genomic DNA. Translation: AAA58078.1.
    U00096 Genomic DNA. Translation: AAC76306.1.
    AP009048 Genomic DNA. Translation: BAE78010.1.
    PIRiS00252.
    RefSeqiNP_417740.1. NC_000913.3.
    WP_000451243.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1NYTX-ray1.50A/B/C/D1-271[»]
    ProteinModelPortaliP15770.
    SMRiP15770.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4261870. 136 interactors.
    DIPiDIP-9153N.
    IntActiP15770. 6 interactors.
    MINTiMINT-1246863.
    STRINGi511145.b3281.

    Proteomic databases

    PaxDbiP15770.
    PRIDEiP15770.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC76306; AAC76306; b3281.
    BAE78010; BAE78010; BAE78010.
    GeneIDi947776.
    KEGGiecj:JW3242.
    eco:b3281.
    PATRICi32121996. VBIEscCol129921_3375.

    Organism-specific databases

    EchoBASEiEB0075.
    EcoGeneiEG10077. aroE.

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237876.
    InParanoidiP15770.
    KOiK00014.
    OMAiFGNPIKH.
    PhylomeDBiP15770.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00087.
    BioCyciEcoCyc:AROE-MONOMER.
    ECOL316407:JW3242-MONOMER.
    MetaCyc:AROE-MONOMER.
    SABIO-RKP15770.

    Miscellaneous databases

    EvolutionaryTraceiP15770.
    PROiP15770.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR011342. Shikimate_DH.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF01488. Shikimate_DH. 1 hit.
    PF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR00507. aroE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROE_ECOLI
    AccessioniPrimary (citable) accession number: P15770
    Secondary accession number(s): Q2M6U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: November 2, 2016
    This is version 156 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, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.