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

Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic

Gene

EMB3004

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-dehydroquinate = 3-dehydroshikimate + H2O.
Shikimate + NADP+ = 3-dehydroshikimate + NADPH.

Kineticsi

  1. KM=685 µM for shikimate1 Publication
  2. KM=131 µM for NADP1 Publication

    Pathwayi: chorismate biosynthesis

    This protein is involved in step 3 and 4 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. Phospho-2-dehydro-3-deoxyheptonate aldolase, Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic (DHS2), Phospho-2-dehydro-3-deoxyheptonate aldolase (At4g33510), Phospho-2-dehydro-3-deoxyheptonate aldolase (At4g33510), Phospho-2-dehydro-3-deoxyheptonate aldolase (F12K8.24), Phospho-2-dehydro-3-deoxyheptonate aldolase (AXX17_At1g23540), Phospho-2-dehydro-3-deoxyheptonate aldolase, Phospho-2-dehydro-3-deoxyheptonate aldolase (DHS2), Phospho-2-dehydro-3-deoxyheptonate aldolase (AXX17_At4g38330), Phospho-2-dehydro-3-deoxyheptonate aldolase (AXX17_At4g45420), Phospho-2-dehydro-3-deoxyheptonate aldolase 1, chloroplastic (DHS1)
    2. 3-dehydroquinate synthase, chloroplastic (DHQS)
    3. Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic (EMB3004)
    4. Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic (EMB3004)
    5. Shikimate kinase 2, chloroplastic (SK2), Shikimate kinase 1, chloroplastic (SK1)
    6. 3-phosphoshikimate 1-carboxyvinyltransferase (F27K7.11), 3-phosphoshikimate 1-carboxyvinyltransferase, 3-phosphoshikimate 1-carboxyvinyltransferase (AXX17_At2g42890), 3-phosphoshikimate 1-carboxyvinyltransferase (AXX17_At1g42980), 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic (At2g45300)
    7. Chorismate synthase (At1g48850), Chorismate synthase, chloroplastic (EMB1144), Chorismate synthase (AXX17_At1g42970), Chorismate synthase (EMB1144), Chorismate synthase (EMB1144)
    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
    Active sitei214Proton acceptor; for 3-dehydroquinate dehydratase activity1
    Active sitei241Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity1
    Binding sitei279Substrate; for 3-dehydroquinate dehydratase activity1
    Binding sitei336Substrate; for shikimate dehydrogenase activity1
    Binding sitei338Substrate; for shikimate dehydrogenase activity1
    Active sitei385For shikimate dehydrogenase activity1
    Binding sitei406Substrate; for shikimate dehydrogenase activity1
    Active sitei423For shikimate dehydrogenase activity1
    Binding sitei550Substrate; for shikimate dehydrogenase activity1
    Binding sitei578Substrate; for shikimate dehydrogenase activity1
    Binding sitei582Substrate; for shikimate dehydrogenase activity1

    GO - Molecular functioni

    GO - Biological processi

    • aromatic amino acid family biosynthetic process Source: UniProtKB-KW
    • cellular amino acid biosynthetic process Source: UniProtKB-KW
    • chorismate biosynthetic process Source: GO_Central
    • embryo development ending in seed dormancy Source: TAIR
    • shikimate metabolic process Source: TAIR

    Keywords - Molecular functioni

    Lyase, Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciARA:AT3G06350-MONOMER.
    MetaCyc:AT3G06350-MONOMER.
    BRENDAi4.2.1.10. 399.
    SABIO-RKQ9SQT8.
    UniPathwayiUPA00053; UER00086.
    UPA00053; UER00087.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
    Short name:
    DHQ-SDH protein
    Alternative name(s):
    DHQase-SORase
    Protein EMBRYO DEFECTIVE 3004
    Including the following 2 domains:
    Dehydroquinate dehydratase (EC:4.2.1.10)
    Short name:
    DHQ
    Shikimate dehydrogenase (EC:1.1.1.25)
    Short name:
    SDH
    Gene namesi
    Name:EMB3004
    Ordered Locus Names:At3g06350
    ORF Names:F24P17.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 3

    Organism-specific databases

    TAIRiAT3G06350.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi336S → A: 13-fold decrease in substrate affinity but almost no change in activity. 1 Publication1
    Mutagenesisi338S → A: 10-fold decrease in activity, and 9-fold decrease in substrate affinity. 1 Publication1
    Mutagenesisi385K → A: Strongly reduced shikimate dehydrogenase activity, but minor change in substrate affinity. 1 Publication1
    Mutagenesisi385K → N: Strongly reduced shikimate dehydrogenase activity, but no change in substrate affinity. 1 Publication1
    Mutagenesisi423D → A: Loss of shikimate dehydrogenase activity. 1 Publication1
    Mutagenesisi423D → N: Reduced shikimate dehydrogenase activity, but no change in substrate affinity. 1 Publication1
    Mutagenesisi550Y → F or A: 100-fold decrease in activity, and 2-fold decrease in substrate affinity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Transit peptidei1 – 66ChloroplastSequence analysisAdd BLAST66
    ChainiPRO_000025064567 – 603Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplasticAdd BLAST537

    Proteomic databases

    PaxDbiQ9SQT8.
    PRIDEiQ9SQT8.

    PTM databases

    iPTMnetiQ9SQT8.

    Expressioni

    Gene expression databases

    GenevisibleiQ9SQT8. AT.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT3G06350.1.

    Structurei

    Secondary structure

    1603
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi95 – 100Combined sources6
    Helixi105 – 118Combined sources14
    Beta strandi121 – 126Combined sources6
    Helixi127 – 129Combined sources3
    Helixi135 – 145Combined sources11
    Beta strandi150 – 153Combined sources4
    Helixi157 – 159Combined sources3
    Beta strandi161 – 163Combined sources3
    Helixi167 – 180Combined sources14
    Beta strandi183 – 188Combined sources6
    Helixi189 – 198Combined sources10
    Turni199 – 201Combined sources3
    Beta strandi208 – 214Combined sources7
    Helixi222 – 233Combined sources12
    Turni234 – 236Combined sources3
    Beta strandi238 – 245Combined sources8
    Helixi249 – 251Combined sources3
    Helixi252 – 261Combined sources10
    Beta strandi266 – 272Combined sources7
    Helixi273 – 276Combined sources4
    Helixi277 – 280Combined sources4
    Turni282 – 286Combined sources5
    Beta strandi288 – 291Combined sources4
    Beta strandi293 – 295Combined sources3
    Helixi307 – 312Combined sources6
    Helixi316 – 318Combined sources3
    Beta strandi324 – 332Combined sources9
    Helixi338 – 348Combined sources11
    Beta strandi352 – 359Combined sources8
    Helixi363 – 369Combined sources7
    Beta strandi375 – 380Combined sources6
    Helixi385 – 391Combined sources7
    Beta strandi393 – 395Combined sources3
    Helixi397 – 402Combined sources6
    Beta strandi406 – 410Combined sources5
    Turni412 – 414Combined sources3
    Beta strandi417 – 420Combined sources4
    Helixi423 – 434Combined sources12
    Beta strandi456 – 459Combined sources4
    Helixi463 – 475Combined sources13
    Beta strandi480 – 485Combined sources6
    Helixi486 – 495Combined sources10
    Beta strandi499 – 502Combined sources4
    Turni503 – 508Combined sources6
    Beta strandi514 – 519Combined sources6
    Turni536 – 538Combined sources3
    Helixi539 – 541Combined sources3
    Beta strandi542 – 547Combined sources6
    Beta strandi551 – 554Combined sources4
    Helixi556 – 562Combined sources7
    Turni563 – 565Combined sources3
    Beta strandi567 – 569Combined sources3
    Helixi571 – 587Combined sources17
    Helixi593 – 603Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GPTX-ray1.95A90-603[»]
    2O7QX-ray2.20A90-603[»]
    2O7SX-ray1.78A90-603[»]
    ProteinModelPortaliQ9SQT8.
    SMRiQ9SQT8.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9SQT8.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni96 – 3133-dehydroquinate dehydrataseAdd BLAST218
    Regioni328 – 558Shikimate dehydrogenaseAdd BLAST231

    Sequence similaritiesi

    In the N-terminal section; belongs to the type-I 3-dehydroquinase family.Curated
    In the C-terminal section; belongs to the shikimate dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG0692. Eukaryota.
    COG0169. LUCA.
    COG0710. LUCA.
    HOGENOMiHOG000237875.
    InParanoidiQ9SQT8.
    KOiK13832.
    OMAiGYEMFIE.
    OrthoDBiEOG093606TB.
    PhylomeDBiQ9SQT8.

    Family and domain databases

    CDDicd00502. DHQase_I. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_00214. AroD. 1 hit.
    MF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR001381. DHquinase_I.
    IPR016040. NAD(P)-bd_dom.
    IPR011342. Shikimate_DH.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF01487. DHquinase_I. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    PF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01093. aroD. 1 hit.
    TIGR00507. aroE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SQT8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAASSTNARL TNPPRLLSKP RLSPTSVANL RFPAADFSTR FFADSSSPRL
    60 70 80 90 100
    RSVPFPVVFS DQRRRRSMEP SNVYVASNST EMEIGSHDIV KNPSLICAPV
    110 120 130 140 150
    MADSIDKMVI ETSKAHELGA DLVEIRLDWL KDFNPLEDLK TIIKKSPLPT
    160 170 180 190 200
    LFTYRPKWEG GQYEGDENER RDVLRLAMEL GADYIDVELQ VASEFIKSID
    210 220 230 240 250
    GKKPGKFKVI VSSHNYQNTP SVEDLDGLVA RIQQTGADIV KIATTAVDIA
    260 270 280 290 300
    DVARMFHITS KAQVPTIGLV MGERGLMSRI LCSKFGGYLT FGTLDSSKVS
    310 320 330 340 350
    APGQPTIKDL LDLYNFRRIG PDTKVYGIIG KPVSHSKSPI VHNQAFKSVD
    360 370 380 390 400
    FNGVYVHLLV DNLVSFLQAY SSSDFAGFSC TIPHKEAALQ CCDEVDPLAK
    410 420 430 440 450
    SIGAVNTILR RKSDGKLLGY NTDCIGSISA IEDGLRSSGD PSSVPSSSSP
    460 470 480 490 500
    LASKTVVVIG AGGAGKALAY GAKEKGAKVV IANRTYERAL ELAEAIGGKA
    510 520 530 540 550
    LSLTDLDNYH PEDGMVLANT TSMGMQPNVE ETPISKDALK HYALVFDAVY
    560 570 580 590 600
    TPRITRLLRE AEESGAITVS GSEMFVRQAY EQFEIFTGLP APKELYWQIM

    SKY
    Length:603
    Mass (Da):65,796
    Last modified:May 1, 2000 - v1
    Checksum:i4DAAB35F594E7CB6
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti491E → K in BAD94599 (Ref. 5) Curated1
    Sequence conflicti557L → Q in AAS76684 (Ref. 3) Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC011623 Genomic DNA. Translation: AAF08579.1.
    CP002686 Genomic DNA. Translation: AEE74381.1.
    BT012197 mRNA. Translation: AAS76684.1.
    AY736474 mRNA. Translation: AAW63134.1.
    AK220988 mRNA. Translation: BAD94599.1.
    RefSeqiNP_187286.1. NM_111510.4.
    UniGeneiAt.43031.

    Genome annotation databases

    EnsemblPlantsiAT3G06350.1; AT3G06350.1; AT3G06350.
    GeneIDi819809.
    GrameneiAT3G06350.1; AT3G06350.1; AT3G06350.
    KEGGiath:AT3G06350.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC011623 Genomic DNA. Translation: AAF08579.1.
    CP002686 Genomic DNA. Translation: AEE74381.1.
    BT012197 mRNA. Translation: AAS76684.1.
    AY736474 mRNA. Translation: AAW63134.1.
    AK220988 mRNA. Translation: BAD94599.1.
    RefSeqiNP_187286.1. NM_111510.4.
    UniGeneiAt.43031.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GPTX-ray1.95A90-603[»]
    2O7QX-ray2.20A90-603[»]
    2O7SX-ray1.78A90-603[»]
    ProteinModelPortaliQ9SQT8.
    SMRiQ9SQT8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT3G06350.1.

    PTM databases

    iPTMnetiQ9SQT8.

    Proteomic databases

    PaxDbiQ9SQT8.
    PRIDEiQ9SQT8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT3G06350.1; AT3G06350.1; AT3G06350.
    GeneIDi819809.
    GrameneiAT3G06350.1; AT3G06350.1; AT3G06350.
    KEGGiath:AT3G06350.

    Organism-specific databases

    TAIRiAT3G06350.

    Phylogenomic databases

    eggNOGiKOG0692. Eukaryota.
    COG0169. LUCA.
    COG0710. LUCA.
    HOGENOMiHOG000237875.
    InParanoidiQ9SQT8.
    KOiK13832.
    OMAiGYEMFIE.
    OrthoDBiEOG093606TB.
    PhylomeDBiQ9SQT8.

    Enzyme and pathway databases

    UniPathwayiUPA00053; UER00086.
    UPA00053; UER00087.
    BioCyciARA:AT3G06350-MONOMER.
    MetaCyc:AT3G06350-MONOMER.
    BRENDAi4.2.1.10. 399.
    SABIO-RKQ9SQT8.

    Miscellaneous databases

    EvolutionaryTraceiQ9SQT8.
    PROiQ9SQT8.

    Gene expression databases

    GenevisibleiQ9SQT8. AT.

    Family and domain databases

    CDDicd00502. DHQase_I. 1 hit.
    Gene3Di3.20.20.70. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_00214. AroD. 1 hit.
    MF_00222. Shikimate_DH_AroE. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR001381. DHquinase_I.
    IPR016040. NAD(P)-bd_dom.
    IPR011342. Shikimate_DH.
    IPR013708. Shikimate_DH-bd_N.
    IPR022893. Shikimate_DH_fam.
    IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
    [Graphical view]
    PfamiPF01487. DHquinase_I. 1 hit.
    PF01488. Shikimate_DH. 1 hit.
    PF08501. Shikimate_dh_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR01093. aroD. 1 hit.
    TIGR00507. aroE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDHQSD_ARATH
    AccessioniPrimary (citable) accession number: Q9SQT8
    Secondary accession number(s): Q3ZLP7, Q56ZH7, Q6NLY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: May 1, 2000
    Last modified: November 30, 2016
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. 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.