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

Quinate/shikimate dehydrogenase (NAD(+))

Gene

aroE

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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, and plays a key role in the quinate degradation pathway. Catalyzes the NAD+-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. It can only use NAD.2 Publications

Catalytic activityi

Quinate + NAD+ = 3-dehydroquinate + NADH.2 Publications
Shikimate + NAD+ = 3-dehydroshikimate + NADH.2 Publications

Kineticsi

The catalytic efficiency with quinate is 3.3-fold higher than that with shikimate. With NADP+ instead of NAD+ as cosubstrate, activity decreases by more than 300-fold with either shikimate or quinate as a substrate.2 Publications

Manual assertion based on experiment ini

  1. KM=0.13 mM for NAD (with 16 mM quinate at pH 7.5)1 Publication
  2. KM=0.28 mM for NAD (with 16 mM quinate at pH 9)1 Publication
  3. KM=0.46 mM for NAD (with 60 mM shikimate at pH 9)1 Publication
  4. KM=0.87 mM for NAD (with 60 mM shikimate at pH 7.5)1 Publication
  5. KM=1.56 mM for quinate (at pH 7.5)1 Publication
  6. KM=2.37 mM for quinate (at pH 9)1 Publication
  7. KM=10.16 mM for shikimate(at pH 7.5)1 Publication
  8. KM=10.2 mM for quinate1 Publication
  9. KM=46.6 mM for shikimate1 Publication
  10. KM=53.8 mM for shikimate(at pH 10)1 Publication

    pH dependencei

    Optimum pH is 9-10.2 Publications

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 4 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.Curated
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase (Cgl2178), Phospho-2-dehydro-3-deoxyheptonate aldolase (aroG)
    2. 3-dehydroquinate synthase (aroB)
    3. 3-dehydroquinate dehydratase (aroQ)
    4. Quinate/shikimate dehydrogenase (NAD(+)) (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.

    Pathwayi: 3,4-dihydroxybenzoate biosynthesis

    This protein is involved in the subpathway that synthesizes 3-dehydroquinate from D-quinate (NAD(+) route).Curated This subpathway is part of the pathway 3,4-dihydroxybenzoate biosynthesis, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the pathway 3,4-dihydroxybenzoate biosynthesis and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei69Quinate/shikimateUniRule annotation1 Publication1
    Active sitei73Proton acceptorUniRule annotation1 Publication1
    Binding sitei85NADPUniRule annotation1
    Binding sitei94Quinate/shikimateUniRule annotation1 Publication1
    Binding sitei110Quinate/shikimateUniRule annotation1 Publication1
    Binding sitei158NAD1 Publication1
    Binding sitei163NAD1 Publication1
    Binding sitei213NAD; via carbonyl oxygen1 Publication1
    Binding sitei228NAD; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei230ShikimateUniRule annotation1
    Binding sitei251NAD; via carbonyl oxygenUniRule annotation1 Publication1
    Binding sitei258Quinate/shikimate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi137 – 138NADUniRule annotation1 Publication2
    Nucleotide bindingi203 – 206NAD1 Publication4

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciCORYNE:G18NG-9981-MONOMER.
    MetaCyc:MONOMER-15330.
    BRENDAi1.1.1.24. 960.
    1.1.1.25. 960.
    UniPathwayiUPA00053; UER00087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinate/shikimate dehydrogenase (NAD(+))1 Publication (EC:1.1.1.-2 Publications, EC:1.1.1.242 Publications)
    Short name:
    QSDH1 Publication
    Gene namesi
    Name:aroEUniRule annotation
    Synonyms:qsuD1 Publication
    OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
    Taxonomic identifieri196627 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
    Proteomesi
    • UP000000582 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001360011 – 283Quinate/shikimate dehydrogenase (NAD(+))Add BLAST283

    Expressioni

    Inductioni

    By shikimate, quinate and QsuR.By similarity

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation2 Publications

    Protein-protein interaction databases

    STRINGi196627.cg0504.

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi5 – 13Combined sources9
    Helixi19 – 29Combined sources11
    Beta strandi34 – 40Combined sources7
    Turni44 – 48Combined sources5
    Helixi51 – 60Combined sources10
    Beta strandi65 – 68Combined sources4
    Turni73 – 76Combined sources4
    Helixi77 – 79Combined sources3
    Beta strandi80 – 83Combined sources4
    Helixi85 – 90Combined sources6
    Beta strandi95 – 98Combined sources4
    Beta strandi104 – 107Combined sources4
    Helixi109 – 121Combined sources13
    Beta strandi128 – 133Combined sources6
    Helixi137 – 148Combined sources12
    Beta strandi152 – 157Combined sources6
    Helixi161 – 175Combined sources15
    Beta strandi180 – 182Combined sources3
    Helixi188 – 194Combined sources7
    Beta strandi195 – 200Combined sources6
    Helixi216 – 218Combined sources3
    Beta strandi224 – 227Combined sources4
    Beta strandi231 – 234Combined sources4
    Helixi236 – 243Combined sources8
    Beta strandi247 – 249Combined sources3
    Helixi252 – 267Combined sources16
    Helixi273 – 281Combined sources9

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NLOX-ray1.64A1-283[»]
    3JYOX-ray1.00A1-283[»]
    3JYPX-ray1.16A1-283[»]
    3JYQX-ray1.16A1-283[»]
    ProteinModelPortaliQ9X5C9.
    SMRiQ9X5C9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9X5C9.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni17 – 19Quinate/shikimate bindingUniRule annotation1 Publication3

    Sequence similaritiesi

    Belongs to the shikimate dehydrogenase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0169. LUCA.
    HOGENOMiHOG000237875.
    KOiK00014.
    OMAiLNITYPC.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    [Graphical view]
    PfamiPF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9X5C9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD
    60 70 80 90 100
    LKTLLDAALY LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA
    110 120 130 140 150
    TGHTTGHNTD VSGFGRGMEE GLPNAKLDSV VQVGAGGVGN AVAYALVTHG
    160 170 180 190 200
    VQKLQVADLD TSRAQALADV INNAVGREAV VGVDARGIED VIAAADGVVN
    210 220 230 240 250
    ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA ARALGCETLD
    260 270 280
    GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL
    Length:283
    Mass (Da):29,697
    Last modified:July 26, 2002 - v2
    Checksum:i2DBCE25D186DAF74
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti29A → P in AAD30993 (Ref. 1) Curated1
    Sequence conflicti135 – 143AGGVGNAVA → RRRRKRSR in AAD30993 (Ref. 1) Curated9
    Sequence conflicti211Missing in AAD30993 (Ref. 1) Curated1
    Sequence conflicti272 – 273DV → T in AAD30993 (Ref. 1) Curated2

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF124518 Genomic DNA. Translation: AAD30993.1.
    BA000036 Genomic DNA. Translation: BAB97817.1.
    BX927149 Genomic DNA. Translation: CAF19140.1.
    RefSeqiNP_599671.1. NC_003450.3.
    WP_011013640.1. NC_006958.1.

    Genome annotation databases

    EnsemblBacteriaiBAB97817; BAB97817; BAB97817.
    CAF19140; CAF19140; cg0504.
    GeneIDi1021203.
    KEGGicgb:cg0504.
    cgl:NCgl0409.
    PATRICi21492904. VBICorGlu203724_0423.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF124518 Genomic DNA. Translation: AAD30993.1.
    BA000036 Genomic DNA. Translation: BAB97817.1.
    BX927149 Genomic DNA. Translation: CAF19140.1.
    RefSeqiNP_599671.1. NC_003450.3.
    WP_011013640.1. NC_006958.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2NLOX-ray1.64A1-283[»]
    3JYOX-ray1.00A1-283[»]
    3JYPX-ray1.16A1-283[»]
    3JYQX-ray1.16A1-283[»]
    ProteinModelPortaliQ9X5C9.
    SMRiQ9X5C9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi196627.cg0504.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAB97817; BAB97817; BAB97817.
    CAF19140; CAF19140; cg0504.
    GeneIDi1021203.
    KEGGicgb:cg0504.
    cgl:NCgl0409.
    PATRICi21492904. VBICorGlu203724_0423.

    Phylogenomic databases

    eggNOGiCOG0169. LUCA.
    HOGENOMiHOG000237875.
    KOiK00014.
    OMAiLNITYPC.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00087.
    BioCyciCORYNE:G18NG-9981-MONOMER.
    MetaCyc:MONOMER-15330.
    BRENDAi1.1.1.24. 960.
    1.1.1.25. 960.

    Miscellaneous databases

    EvolutionaryTraceiQ9X5C9.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    HAMAPiMF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR016040. NAD(P)-bd_dom.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    [Graphical view]
    PfamiPF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAROE_CORGL
    AccessioniPrimary (citable) accession number: Q9X5C9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 26, 2002
    Last modified: November 2, 2016
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Has a different substrate and cosubstrate specificities relative to all other known bacterial shikimate/quinate dehydrogenases.2 Publications

    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.