A0A0C3HLM9 · A0A0C3HLM9_OIDMZ

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.

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 site44-46NAD+ (UniProtKB | ChEBI)
Binding site81-84NAD+ (UniProtKB | ChEBI)
Binding site112-114NAD+ (UniProtKB | ChEBI)
Binding site117NAD+ (UniProtKB | ChEBI)
Binding site1287-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site137-138NAD+ (UniProtKB | ChEBI)
Binding site1447-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site159NAD+ (UniProtKB | ChEBI)
Binding site1607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site177-180NAD+ (UniProtKB | ChEBI)
Binding site188NAD+ (UniProtKB | ChEBI)
Binding site192Zn2+ (UniProtKB | ChEBI); catalytic
Binding site192-1957-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2467-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site256Proton acceptor; for 3-dehydroquinate synthase activity
Binding site260-2647-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site267Zn2+ (UniProtKB | ChEBI); catalytic
Active site271Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2837-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site283Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site819For EPSP synthase activity
Binding site866-873ATP (UniProtKB | ChEBI)
Active site1176Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1204Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
Biological Processphosphorylation

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
      OIDMADRAFT_53028

Organism names

  • Taxonomic identifier
  • Strain
    • Zn
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Leotiomycetes > Leotiomycetes incertae sedis > Myxotrichaceae > Oidiodendron

Accessions

  • Primary accession
    A0A0C3HLM9

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane106-127Helical

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3803-dehydroquinate synthase
Domain76-3543-dehydroquinate synthase
Domain406-831Enolpyruvate transferase
Region1053-12733-dehydroquinase
Region1286-1580Shikimate dehydrogenase
Domain1291-1371Shikimate 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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,580
  • Mass (Da)
    172,024
  • Last updated
    2015-04-01 v1
  • Checksum
    1C338C5F5287FE42
MAAPTKISILGRESIVADYGIWGEYIVRDLLSNISSTTYLLVTDTNLGPIYKNTFEKAFSDAAGALSPNPRLLIKEIPPGENSKSRQGKADIEDWMLRNLCGRDTVIIALGGGVVGDLLGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLLGAIWQPTRIYIDLEFLNTLPEREFINGMAEVIKTAAISDEQEFTALENNAASILAAARSKPSTGRFDQVRNVLKQHIVASARHKAYVVTADEHEGGLRNLLNLGHSIGHAIETILTPQILHGECVAIGMVRELELARYLGVLKAVNVSRMIKCLSSYGLPTSLKDPRVKKFTAGKHCSIDQIMVNMALDKKNDGTKKKIVLLSAIGRTYEPKASNVADKDIKAVLAPSIEVKPGVPNSVSIVCSPPGSKSISNRALVLAALGSGTVRIKNLLYSDDTEVMMDALEQLGAASFAWEEEGEVLVVHGNGGRLQATATELYLGNAGTASRFLTTVATLATKGFADYNILTGNNRMKQRPIGDLVNALQANGAGIDYLESTGSLPLKIAASSGLHGGRINLAAKVSSQYVSSLLMCAPYTKEPVTLKLGGKPISQLYIDMTTAMMRSFGINVEKSTTEAYTYHIPQGAYVNPPEYVIESDASSATYPLAVAALTGTTCTVPNIGSASIQGDARFAVKVLRPMGCKVEQTATSTTVTGPKDGVLRPLPNINMEPMTDAFLGASVLAAVAQGEGSNHTTRIYGIANQRVKECNRIEAMREELAKFGVVCREHDDGLEIDGIDRSALRHPVEGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPTYWDMLKQKFGVQLEGKELKESALIEQVRADRTSASIIIIGMRGAGKTTSGRRAAKALNRPFVDLDTELEQAEGKTIPEIITERGWQGFREAELSLFKRALSERPTGYVFACGGGIIESPEVRKILIDYHQVKGHVILVMRDIARVMGFLNIDKSRPAYVEDMMGVWLRRKPWFQECSNIQWYSQQTSSSSELASASEDFGRFLHFVTGKTNPLPTIRKKKLSFFVSLTLPDLRGTGDLLRIVSSGSDAVELRVDLLKDPSSSTELPSLEYVAEQISFYRSRVSVPIIFTIRTKSQGGRFPDNAHEAAFDLIRLAIRSGCEFVDLEITFPDDLLRSIAETKGYSKIIASHHDPQGKLNWSSGSWIQYYNKALQCGDIIKLVGVAKNLNDNAALQEFKDWAEKAHSIPVICINMGDKGQLSRILNRFMTPVSHPRLPFKAAPGQLSAAEIRRALALMGEIRPKKFALFGKPIEASRSPVLHNRLFKIAGLPHNYTRLETDRAQDVKEFIRSPDFGGASITIPLKLDVIPLVDDVLDEAKVIGAINTIVPVEAEDGTTRLIGRNTDWQGMVRCLREVGAYGGEVASNALVVGAGGTARAAVYALHSMGYSPVYLLGRSPTNIENMASTFPADFDIRILTDITEVKTVPRVIISTIPGDKPMDASLREVLCSIFQRGKDIDRVAKGQGVGPHQRVLLEMAYKPSATPLMQLAADSGWVTIPGSEALVGQGIYQFEYWTGISPVYEDAKNAVLGTNGRE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KN832874
EMBL· GenBank· DDBJ
KIN03232.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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