A0A066X883 · A0A066X883_COLSU

Function

function

The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site53-55NAD+ (UniProtKB | ChEBI)
Binding site87-90NAD+ (UniProtKB | ChEBI)
Binding site118-120NAD+ (UniProtKB | ChEBI)
Binding site123NAD+ (UniProtKB | ChEBI)
Binding site1347-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site143-144NAD+ (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site165NAD+ (UniProtKB | ChEBI)
Binding site1667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site183-186NAD+ (UniProtKB | ChEBI)
Binding site194NAD+ (UniProtKB | ChEBI)
Binding site198Zn2+ (UniProtKB | ChEBI); catalytic
Binding site198-2017-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2517-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site261Proton acceptor; for 3-dehydroquinate synthase activity
Binding site265-2697-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2727-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site272Zn2+ (UniProtKB | ChEBI); catalytic
Active site276Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2887-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site288Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3577-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site820For EPSP synthase activity
Binding site868-875ATP (UniProtKB | ChEBI)
Active site1172Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1200Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-dehydroquinate dehydratase activity
Molecular Function3-dehydroquinate synthase activity
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionshikimate 3-dehydrogenase (NADP+) activity
Molecular Functionshikimate kinase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Pentafunctional AROM polypeptide

Including 5 domains:

  • Recommended name
    3-dehydroquinate synthase
  • EC number
  • Short names
    DHQS
  • Recommended name
    3-phosphoshikimate 1-carboxyvinyltransferase
  • EC number
  • Alternative names
    • 5-enolpyruvylshikimate-3-phosphate synthase
      (EPSP synthase
      ; EPSPS
      )
  • Recommended name
    Shikimate kinase
  • EC number
  • Short names
    SK
  • Recommended name
    3-dehydroquinate dehydratase
  • EC number
  • Short names
    3-dehydroquinase
  • Recommended name
    Shikimate dehydrogenase
  • EC number

Gene names

    • ORF names
      CSUB01_11632

Organism names

  • Taxonomic identifier
  • Strain
    • TX430BB
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Glomerellaceae > Colletotrichum > Colletotrichum graminicola species complex

Accessions

  • Primary accession
    A0A066X883

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3853-dehydroquinate synthase
Domain81-3593-dehydroquinate synthase
Domain407-832Enolpyruvate transferase
Region1282-1579Shikimate dehydrogenase
Domain1287-1367Shikimate dehydrogenase substrate binding N-terminal

Sequence similarities

Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 3rd section; belongs to the shikimate kinase family.
In the 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
In the N-terminal section; belongs to the dehydroquinate synthase family.
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,579
  • Mass (Da)
    170,469
  • Last updated
    2014-09-03 v1
  • Checksum
    5DE9D2AE01281746
MGLANGSSSGTGPARITILGKDNIVVDHGLWLNFVTHDLLENLKTSTYVVITDTNLYDTYIPPFQEVFNVAAPASTRLLTYAIPPGEVSKSRQTKASIEDWMLSQKCTRDTVIIALGGGVIGDMIGYVAATFMRGVRLVQVPTTLLSMVDSSIGGKTAIDTPAGKNLVGAFWQPLRIYIDLAFLETLPTREFINGMAEVVKTAAIWDEEEFTMLESNAPTILAAVKSQGSQRLSPIRDILKRIVLGSARVKAQVVSSDEREGGLRNLLNFGHSIGHAYEALLTPQLLHGEAVAIGMVKEAELARYLGVLRPGAVARLVKCIASYELPTSVHDKKVIKLTAGKACPVDVLLEKMAVDKKNDGAKKKIVLLSAIGRTHEQKASVVEDGAIRVVLSPATEVIPGVPKSHDTTVTPPGSKSISNRALVLAALGQGTCRITNLLHSDDTEYMLSAIAQLGGATYAWEDAGEVLAVQGKGGRLSASKEPLYLGNAGTASRFLTTVVALCAPSDVSSTVLTGNARMKVRPIGPLVDALRANGLGIKYLGQDKSLPLQVDAANGFEGGVIELAATISSQYVSSILMAAPYAKNPVTLRLIGGKPISQFYIDMTIAMMRTFGVNVTKSAEEPNTYHIPKAVYQNPPEYVVESDASSATYPLAIAAITGTTCTVPNIGSESLQGDSRFAVDVLRPMGCTVEQTGTSTTVTGPPIGSLKAIEHVDMEPMTDAFLTASVLAAVASGTTKISGIANQRVKECNRIGAMREQLAKFGVDTDEFDDGIIVTGRSVQSLQGPTEDIFCYDDHRVAMSFSVLSVVAPKPVTILERECTGKTWPGWWDTLSQSFKVSLDGVDQHPQGVVTGPSAKTRKDKSVFIIGMRGAGKTTAGRWMANTLKRPFIDLDEELERRAGMTIPQMIRGTRGWDGFRADELELLRDVLEKHSHGYIFSCGGGIVETPEARKLLIAHCRNDGTVLLVHRNTKEVVDYLLQDKSRPAYREDIEDVYYRRKPFFEECSNFEYFSPHPPGTMATRDPPLDFRRFVNALCGEEIQVKKALAKDPSFFVSLTVPEVASALALIPAVVVGSDAVELRVDLLQDYSEESVAHQVALLRSVADVPIIFTLRTRAQGGRFPDDAYDQGLGLYQKAIRMGVEFIDVEMTLPEHIIQAVVENKGPCRIIASHHDPQGKLSWKNGSWIPFYNKALQWGDVIKLVGVAQHMDDNYALAQFKSEMLSSHKTPIIALNMGTAGKLSRVLNGCLTPVSHPALPFKAAPGQLSAAEIRQALALLGGISPQSFYLFGKPISASRSPALHNTLFALTGLPHRYLLKETDHAADVREVIRAPDFGGASVTIPLKLDIMKEIDEVSEAARIIGAVNTIIPVRDRGDSTAKLVGDNTDWSGMVHSLQSAGVAARSASGVECSAMVIGSGGTTRAAIFALHALGFGPIYALARNSSNLETLKASFPPEYRIEPLKSASDASTLPSSPTVIVSTIPADKPVDPSLRETLVTVLRHEPATEEKRVLLEMAYQPRHTPLMQLAEEAGWATIPGLEVLSAQGWYQFRKWTDITPLYQTARAAVLGEEATETVGRKV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMSE01001182
EMBL· GenBank· DDBJ
KDN63894.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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