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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

  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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661ShikimateUniRule annotation
    Active sitei70 – 701Proton acceptorUniRule annotation1 Publication
    Binding sitei82 – 821NADPUniRule annotation1 Publication
    Binding sitei91 – 911ShikimateUniRule annotation1 Publication
    Binding sitei106 – 1061ShikimateUniRule annotation1 Publication
    Binding sitei214 – 2141NADP; via carbonyl oxygenUniRule annotation1 Publication
    Binding sitei216 – 2161ShikimateUniRule annotation1 Publication
    Binding sitei235 – 2351NADP; via carbonyl oxygenUniRule annotation1 Publication
    Binding sitei242 – 2421ShikimateUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi130 – 1345NADPUniRule annotation1 Publication
    Nucleotide bindingi153 – 1586NADPUniRule annotation1 Publication

    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
    • 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

    BioCyciAAEO224324:GJBH-643-MONOMER.
    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Shikimate dehydrogenase (NADP(+))PRO_0000135990Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi224324.aq_901.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 159Combined sources
    Helixi21 – 3212Combined sources
    Beta strandi35 – 428Combined sources
    Helixi45 – 473Combined sources
    Helixi48 – 5811Combined sources
    Beta strandi62 – 654Combined sources
    Turni70 – 734Combined sources
    Helixi74 – 763Combined sources
    Beta strandi78 – 803Combined sources
    Helixi82 – 876Combined sources
    Beta strandi92 – 965Combined sources
    Beta strandi99 – 1035Combined sources
    Helixi106 – 11712Combined sources
    Helixi121 – 1233Combined sources
    Beta strandi124 – 1296Combined sources
    Helixi133 – 14513Combined sources
    Beta strandi148 – 1525Combined sources
    Helixi156 – 1627Combined sources
    Turni163 – 1653Combined sources
    Beta strandi168 – 1703Combined sources
    Helixi174 – 1763Combined sources
    Helixi178 – 1803Combined sources
    Beta strandi182 – 1865Combined sources
    Helixi202 – 2043Combined sources
    Beta strandi209 – 2179Combined sources
    Helixi220 – 2278Combined sources
    Beta strandi231 – 2333Combined sources
    Helixi236 – 25116Combined sources
    Helixi257 – 26812Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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. Positions 1-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO67049.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 213Shikimate bindingUniRule annotation1 Publication

    Sequence similaritiesi

    Belongs to the shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237875.
    InParanoidiO67049.
    KOiK00014.
    OMAiSIYIDAT.
    OrthoDBiEOG64R67G.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE.
    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
    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. Positions 1-269.
    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.
    OrthoDBiEOG64R67G.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00087.
    BioCyciAAEO224324:GJBH-643-MONOMER.
    BRENDAi1.1.1.25. 396.

    Miscellaneous databases

    EvolutionaryTraceiO67049.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: VF5.
    2. "Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism."
      Gan J., Wu Y., Prabakaran P., Gu Y., Li Y., Andrykovitch M., Liu H., Gong Y., Yan H., Ji X.
      Biochemistry 46:9513-9522(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SHIKIMATE AND NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, REACTION MECHANISM, SUBUNIT.

    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: December 9, 2015
    This is version 114 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.