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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

  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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei60 – 601ShikimateUniRule annotation1 Publication
    Active sitei64 – 641Proton acceptorUniRule annotation
    Binding sitei76 – 761NADPUniRule annotation
    Binding sitei85 – 851ShikimateUniRule annotation1 Publication
    Binding sitei100 – 1001ShikimateUniRule annotation1 Publication
    Binding sitei209 – 2091NADP; via carbonyl oxygenUniRule annotation
    Binding sitei211 – 2111ShikimateUniRule annotation
    Sitei211 – 2111Plays a major role in the catalytic process and a minor role in the substrate binding1 Publication
    Binding sitei232 – 2321NADP; via carbonyl oxygenUniRule annotation
    Binding sitei239 – 2391ShikimateUniRule annotation1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi124 – 1285NADPUniRule annotation
    Nucleotide bindingi148 – 1536NADPUniRule annotation

    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

    BioCyciSEPI176279:GJJB-1190-MONOMER.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111Y → F: Leads to a 345-fold decrease in the catalytic efficiency and a 3-fold decrease in the affinity binding for shikimate. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 269269Shikimate dehydrogenase (NADP(+))PRO_0000136037Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer or homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi176279.SERP1163.

    Structurei

    Secondary structure

    1
    269
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 98Combined sources
    Helixi15 – 2511Combined sources
    Beta strandi31 – 366Combined sources
    Helixi39 – 446Combined sources
    Helixi45 – 517Combined sources
    Beta strandi55 – 595Combined sources
    Turni64 – 674Combined sources
    Helixi68 – 703Combined sources
    Beta strandi72 – 743Combined sources
    Helixi76 – 816Combined sources
    Beta strandi86 – 905Combined sources
    Beta strandi93 – 975Combined sources
    Helixi100 – 11112Combined sources
    Helixi115 – 1173Combined sources
    Beta strandi120 – 1234Combined sources
    Helixi127 – 13711Combined sources
    Beta strandi145 – 1473Combined sources
    Helixi151 – 1544Combined sources
    Beta strandi162 – 1643Combined sources
    Helixi166 – 1716Combined sources
    Helixi173 – 1753Combined sources
    Beta strandi177 – 1815Combined sources
    Beta strandi205 – 2095Combined sources
    Beta strandi212 – 2154Combined sources
    Helixi217 – 2248Combined sources
    Helixi233 – 24816Combined sources
    Helixi254 – 26512Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ5HNV1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 153Shikimate bindingUniRule annotation1 Publication

    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DONX-ray2.10A1-269[»]
    3DOOX-ray2.20A1-269[»]
    ProteinModelPortaliQ5HNV1.
    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.
    BioCyciSEPI176279:GJJB-1190-MONOMER.
    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: September 7, 2016
    This is version 85 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.