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Protein

Shikimate dehydrogenase (NADP(+))

Gene

aroE

Organism
Aquifex aeolicus (strain VF5)
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).UniRule annotation1 Publication

Catalytic activityi

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

Kineticsi

Kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=42.4 µM for shikimate (at pH 9 and 25 degrees Celsius)1 Publication
  2. KM=42.4 µM for NADP (at pH 9 and 25 degrees Celsius)1 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. no protein annotated in this organism
    2. no protein annotated in this organism
    3. 3-dehydroquinate dehydratase (aroD)
    4. Shikimate dehydrogenase (NADP(+)) (aroE)
    5. Shikimate kinase (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 sitei66ShikimateUniRule annotation1
    Active sitei70Proton acceptorUniRule annotation1 Publication1
    Binding sitei82NADPUniRule annotation1 Publication1
    Binding sitei91ShikimateUniRule annotation1 Publication1
    Binding sitei106ShikimateUniRule annotation1 Publication1
    Binding sitei214NADP; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei216ShikimateUniRule annotation1 Publication1
    Binding sitei235NADP; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei242ShikimateUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi130 – 134NADPUniRule annotation1 Publication5
    Nucleotide bindingi153 – 158NADPUniRule annotation1 Publication6

    GO - Molecular functioni

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

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: UniProtKB-HAMAP
    • cellular amino acid biosynthetic process Source: UniProtKB-KW
    • chorismate biosynthetic process Source: UniProtKB
    • 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

    BRENDAi1.1.1.25. 396.
    UniPathwayiUPA00053; UER00087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate dehydrogenase (NADP(+))1 PublicationUniRule annotation (EC:1.1.1.25UniRule annotation1 Publication)
    Short name:
    SD1 Publication
    Short name:
    SDH1 PublicationUniRule annotation
    Gene namesi
    Name:aroE1 PublicationUniRule annotation
    Ordered Locus Names:aq_901
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    Proteomesi
    • UP000000798 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001359901 – 269Shikimate dehydrogenase (NADP(+))Add BLAST269

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi224324.aq_901.

    Structurei

    Secondary structure

    1269
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi7 – 15Combined sources9
    Helixi21 – 32Combined sources12
    Beta strandi35 – 42Combined sources8
    Helixi45 – 47Combined sources3
    Helixi48 – 58Combined sources11
    Beta strandi62 – 65Combined sources4
    Turni70 – 73Combined sources4
    Helixi74 – 76Combined sources3
    Beta strandi78 – 80Combined sources3
    Helixi82 – 87Combined sources6
    Beta strandi92 – 96Combined sources5
    Beta strandi99 – 103Combined sources5
    Helixi106 – 117Combined sources12
    Helixi121 – 123Combined sources3
    Beta strandi124 – 129Combined sources6
    Helixi133 – 145Combined sources13
    Beta strandi148 – 152Combined sources5
    Helixi156 – 162Combined sources7
    Turni163 – 165Combined sources3
    Beta strandi168 – 170Combined sources3
    Helixi174 – 176Combined sources3
    Helixi178 – 180Combined sources3
    Beta strandi182 – 186Combined sources5
    Helixi202 – 204Combined sources3
    Beta strandi209 – 217Combined sources9
    Helixi220 – 227Combined sources8
    Beta strandi231 – 233Combined sources3
    Helixi236 – 251Combined sources16
    Helixi257 – 268Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2HK7X-ray2.50A/B1-269[»]
    2HK8X-ray2.35A/B/C/D/E/F/G/H1-269[»]
    2HK9X-ray2.20A/B/C/D1-269[»]
    ProteinModelPortaliO67049.
    SMRiO67049.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO67049.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni19 – 21Shikimate bindingUniRule annotation1 Publication3

    Sequence similaritiesi

    Belongs to the shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237875.
    InParanoidiO67049.
    KOiK00014.
    OMAiSIYIDAT.
    OrthoDBiPOG091H02DY.

    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.

    O67049-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MINAQTQLYG VIGFPVKHSL SPVFQNALIR YAGLNAVYLA FEINPEELKK
    60 70 80 90 100
    AFEGFKALKV KGINVTVPFK EEIIPLLDYV EDTAKEIGAV NTVKFENGKA
    110 120 130 140 150
    YGYNTDWIGF LKSLKSLIPE VKEKSILVLG AGGASRAVIY ALVKEGAKVF
    160 170 180 190 200
    LWNRTKEKAI KLAQKFPLEV VNSPEEVIDK VQVIVNTTSV GLKDKDPEIF
    210 220 230 240 250
    NYDLIKKDHV VVDIIYKETK LLKKAKEKGA KLFDGLPMLL WQGIEAFKIW
    260
    NGCEVPYSVA ERSVRDLRG
    Length:269
    Mass (Da):30,106
    Last modified:August 1, 1998 - v1
    Checksum:i3F2E5E490FB9ADB7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07007.1.
    PIRiF70377.
    RefSeqiNP_213611.1. NC_000918.1.
    WP_010880549.1. NC_000918.1.

    Genome annotation databases

    EnsemblBacteriaiAAC07007; AAC07007; aq_901.
    GeneIDi1193591.
    KEGGiaae:aq_901.
    PATRICi20959160. VBIAquAeo85532_0703.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07007.1.
    PIRiF70377.
    RefSeqiNP_213611.1. NC_000918.1.
    WP_010880549.1. NC_000918.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2HK7X-ray2.50A/B1-269[»]
    2HK8X-ray2.35A/B/C/D/E/F/G/H1-269[»]
    2HK9X-ray2.20A/B/C/D1-269[»]
    ProteinModelPortaliO67049.
    SMRiO67049.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224324.aq_901.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC07007; AAC07007; aq_901.
    GeneIDi1193591.
    KEGGiaae:aq_901.
    PATRICi20959160. VBIAquAeo85532_0703.

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237875.
    InParanoidiO67049.
    KOiK00014.
    OMAiSIYIDAT.
    OrthoDBiPOG091H02DY.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00087.
    BRENDAi1.1.1.25. 396.

    Miscellaneous databases

    EvolutionaryTraceiO67049.

    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_AQUAE
    AccessioniPrimary (citable) accession number: O67049
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: November 30, 2016
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    AroE is dependent on the hydrogen ion concentration of the environment. A low pH environment favors the formation of SA and NADP, whereas a high pH condition favors the formation of DHSA and NADPH.1 Publication

    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

    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.