A0AAN6E2W7 · A0AAN6E2W7_9EURO

  • Protein
    Pentafunctional AROM polypeptide
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.

Type
IDPosition(s)Description
Binding site50-52NAD+ (UniProtKB | ChEBI)
Binding site87-90NAD+ (UniProtKB | ChEBI)
Binding site120-122NAD+ (UniProtKB | ChEBI)
Binding site125NAD+ (UniProtKB | ChEBI)
Binding site1367-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site145-146NAD+ (UniProtKB | ChEBI)
Binding site1527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1587-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site167NAD+ (UniProtKB | ChEBI)
Binding site1687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site185-188NAD+ (UniProtKB | ChEBI)
Binding site196NAD+ (UniProtKB | ChEBI)
Binding site200Zn2+ (UniProtKB | ChEBI); catalytic
Binding site200-2037-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site266Proton acceptor; for 3-dehydroquinate synthase activity
Binding site270-2747-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2777-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Active site281Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2937-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site293Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site829For EPSP synthase activity
Binding site876-883ATP (UniProtKB | ChEBI)
Active site1188Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1217Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

Keywords

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
      EDD36DRAFT_462019

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • JF 03-4F
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Exophiala

Accessions

  • Primary accession
    A0AAN6E2W7

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3903-dehydroquinate synthase
Domain82-3643-dehydroquinate synthase
Domain410-841Enolpyruvate transferase
Region869-1061Shikimate kinase
Region1300-1602Shikimate dehydrogenase
Domain1305-1385Shikimate 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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,602
  • Mass (Da)
    173,847
  • Last updated
    2024-10-02 v1
  • Checksum
    78297967234767EE
MPLVNGTAKEVRISLLGKESIIINFGLWRNYVASDLLNNLESSTYVLFTDTNLGSLYIESFQEAFKSAAQQAGKSSRLLVHEIPPGESSKSRQTKDDIEDWLLSQSPPCGRDTVIIALGGGVVGDLMGFVAATYMRGIRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLVGAIWQPQRIYIDLDFLGTLPRRELVNGMAEVVKTAAISEEEEFVALEKNAERIMAAVNGDISQGTARFKDIESILLRIISASAKFKAHVVTIDERETGLRNLLNFGHSIGHAMEAFLTPQVLHGECVAIGMVKEAELARHLGILSGVAVGRLQKCIAAYGLPTRLDDERVRKLSGGKRCTVDGMLKKMGVDKKNDGAKKKVVLLSAIGHTHEQKASVVSDSDLRVVLSPSIEVLPGVPSDLNVVCAPPGSKSISNRALVLAALGQGTCRIRNLLTSADTEVMLEALTRLGAATFSWEDDGEVLVVNGNGGHLEASHHPLYLGNAGTAARFLTTVVTLTRQNQVASTILTGNARMKQRPIGDLVDALKANGAGVEYLESNGCLPLNITASGGFNGGEIKLAAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPVSQPYIDMTIAMMSSFGVHVRKSETEEHTYHIPQGTYRNPSEYVVESDASSATYPLAIAAITGTTCTIPNIGSSSLQGDSRFATDVLRPMGCEVKQTSTSTTVTGPRNGRLTPLSNIDMEPMTDAFLTASVLAAVAQGGSSNTTRIYGIANQRVKECNRIQAMEDELAKFGVTCRQFDDGIEVDGIDRTQLKQPKGGVHCYDDHRVAMSFSVLALATPEPTLILEKECTGKTWPGWWDTMARQFNVKLQGVELDSSTQPTKKKLNRSTASVFIIGMRGAGKTTSGRWAARSLRKRLIDLDTELESREKRTIPEIIRESGWEYFRERELALLKAVIKEKPNDYVFACGGGIVEAPEARQLLIEWHQKTGNVLLVQRDINQVMDFLQIDKTRPAYVEDMMGVWLRRKPWFEQCSNIVYYSQSIPNEQMSEAAEDFDRFLQMVTGKIDILSQLKRKPESFFVALTFPDLRPHLKSLPEVCLGSDAVELRVDLLVDPESTSKIPSPEYVTAQLSLLRATVPLPVVFTIRTSAQGGKFPDNAHNEYLNLCTLAIRMGCEFVDLEVASFPESILNPILEKKNSSYSKIIASHHDPQARLSWSRPGSWIAIYNRCLQYGDIVKLIGVAKTIDDNFTLRNFKKWSASQHPDLPLIAINMGRAGQASRILNGFMTPVSHPALPFKAAPGQLSATEIRQGLSLLGEITPKQFYLFGSPISASKSPALHNRLFKETGLPHTYSAYETTSLDEIKSKIRSEDFGGASVTIPLKLDVMPLLDEVDPSARLIGAVNTIVPVVGPTGKTTLVGRNTDFLGMMDCLRAAGASTALGDAQQSGLVIGGGGTARAAIHTLHSMGYKPIHLIGRDRAKIEELAASFPSEYELVVLDTAGEVKQQLATPPTIAIATIPASIPIDAALGNALQEILETSVPASIMLKGQGSAAPARILLELAYKPAHTAVMQMAESAGGWKTVQGLETLVTQGEWQFEYWTGIRVRGLGGRISREVVLGSGA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MU404351
EMBL· GenBank· DDBJ
KAI1617159.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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