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Protein

Shikimate dehydrogenase (NADP(+))

Gene

aroE

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
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 can also use NAD to oxidize shikimate.UniRule annotation1 Publication

Catalytic activityi

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

Kineticsi

Kcat is 22.8 sec(-1) for dehydrogenase activity with shikimate (at pH 8 and at 25 degrees Celsius). Kcat is 87 sec(-1) for dehydrogenase activity with NAD (at pH 8 and at 25 degrees Celsius).1 Publication

Manual assertion based on experiment ini

  1. KM=73 µM for shikimate (at pH 8 and at 25 degrees Celsius)1 Publication
  2. KM=100 µM for NADP (at pH 8 and at 25 degrees Celsius)1 Publication
  3. KM=10.6 mM for NAD (at pH 8 and at 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. 3-dehydroquinate synthase (aroB)
    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 sitei60ShikimateUniRule annotation1 Publication1
    Active sitei64Proton acceptorUniRule annotation1
    Binding sitei76NADPUniRule annotation1
    Binding sitei85ShikimateUniRule annotation1 Publication1
    Binding sitei100ShikimateUniRule annotation1 Publication1
    Binding sitei209NADP; via carbonyl oxygenUniRule annotation1
    Binding sitei211ShikimateUniRule annotation1
    Sitei211Plays a major role in the catalytic process and a minor role in the substrate binding1 Publication1
    Binding sitei232NADP; via carbonyl oxygenUniRule annotation1
    Binding sitei239ShikimateUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi124 – 128NADPUniRule annotation5
    Nucleotide bindingi148 – 153NADPUniRule annotation6

    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. 10919.
    UniPathwayiUPA00053; UER00087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Shikimate dehydrogenase (NADP(+))1 PublicationUniRule annotation (EC:1.1.1.25UniRule annotation1 Publication)
    Short name:
    SDH1 PublicationUniRule annotation
    Gene namesi
    Name:aroE1 PublicationUniRule annotation
    Ordered Locus Names:SERP1163
    OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
    Taxonomic identifieri176279 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
    Proteomesi
    • UP000000531 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi211Y → F: Leads to a 345-fold decrease in the catalytic efficiency and a 3-fold decrease in the affinity binding for shikimate. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001360371 – 269Shikimate dehydrogenase (NADP(+))Add BLAST269

    Interactioni

    Subunit structurei

    Monomer or homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi176279.SERP1163.

    Structurei

    Secondary structure

    1269
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 9Combined sources8
    Helixi15 – 25Combined sources11
    Beta strandi31 – 36Combined sources6
    Helixi39 – 44Combined sources6
    Helixi45 – 51Combined sources7
    Beta strandi55 – 59Combined sources5
    Turni64 – 67Combined sources4
    Helixi68 – 70Combined sources3
    Beta strandi72 – 74Combined sources3
    Helixi76 – 81Combined sources6
    Beta strandi86 – 90Combined sources5
    Beta strandi93 – 97Combined sources5
    Helixi100 – 111Combined sources12
    Helixi115 – 117Combined sources3
    Beta strandi120 – 123Combined sources4
    Helixi127 – 137Combined sources11
    Beta strandi145 – 147Combined sources3
    Helixi151 – 154Combined sources4
    Beta strandi162 – 164Combined sources3
    Helixi166 – 171Combined sources6
    Helixi173 – 175Combined sources3
    Beta strandi177 – 181Combined sources5
    Beta strandi205 – 209Combined sources5
    Beta strandi212 – 215Combined sources4
    Helixi217 – 224Combined sources8
    Helixi233 – 248Combined sources16
    Helixi254 – 265Combined sources12

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3DONX-ray2.10A1-269[»]
    3DOOX-ray2.20A1-269[»]
    ProteinModelPortaliQ5HNV1.
    SMRiQ5HNV1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5HNV1.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni13 – 15Shikimate bindingUniRule annotation1 Publication3

    Sequence similaritiesi

    Belongs to the shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237875.
    KOiK00014.
    OMAiTTVDGAW.

    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.

    Q5HNV1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKFAVIGNPI SHSLSPLMHH ANFQSLNLEN TYEAINVPVN QFQDIKKIIS
    60 70 80 90 100
    EKSIDGFNVT IPHKERIIPY LDDINEQAKS VGAVNTVLVK DGKWIGYNTD
    110 120 130 140 150
    GIGYVNGLKQ IYEGIEDAYI LILGAGGASK GIANELYKIV RPTLTVANRT
    160 170 180 190 200
    MSRFNNWSLN INKINLSHAE SHLDEFDIII NTTPAGMNGN TDSVISLNRL
    210 220 230 240 250
    ASHTLVSDIV YNPYKTPILI EAEQRGNPIY NGLDMFVHQG AESFKIWTNL
    260
    EPDIKAMKNI VIQKLKGEL
    Length:269
    Mass (Da):29,947
    Last modified:February 15, 2005 - v1
    Checksum:i9F9808764B9C21C4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54512.1.
    RefSeqiWP_001831091.1. NC_002976.3.

    Genome annotation databases

    EnsemblBacteriaiAAW54512; AAW54512; SERP1163.
    KEGGiser:SERP1163.
    PATRICi19613179. VBIStaEpi130894_1132.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000029 Genomic DNA. Translation: AAW54512.1.
    RefSeqiWP_001831091.1. NC_002976.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3DONX-ray2.10A1-269[»]
    3DOOX-ray2.20A1-269[»]
    ProteinModelPortaliQ5HNV1.
    SMRiQ5HNV1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi176279.SERP1163.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAW54512; AAW54512; SERP1163.
    KEGGiser:SERP1163.
    PATRICi19613179. VBIStaEpi130894_1132.

    Phylogenomic databases

    eggNOGiENOG4105E2X. Bacteria.
    COG0169. LUCA.
    HOGENOMiHOG000237875.
    KOiK00014.
    OMAiTTVDGAW.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00087.
    BRENDAi1.1.1.25. 10919.

    Miscellaneous databases

    EvolutionaryTraceiQ5HNV1.

    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_STAEQ
    AccessioniPrimary (citable) accession number: Q5HNV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: February 15, 2005
    Last modified: November 2, 2016
    This is version 87 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

    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.