A0A0N0DH64 · A0A0N0DH64_FUSLA

  • 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 site49-51NAD+ (UniProtKB | ChEBI)
Binding site84-87NAD+ (UniProtKB | ChEBI)
Binding site115-117NAD+ (UniProtKB | ChEBI)
Binding site120NAD+ (UniProtKB | ChEBI)
Binding site1317-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site140-141NAD+ (UniProtKB | ChEBI)
Binding site1477-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1537-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site162NAD+ (UniProtKB | ChEBI)
Binding site1637-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site180-183NAD+ (UniProtKB | ChEBI)
Binding site191NAD+ (UniProtKB | ChEBI)
Binding site195Zn2+ (UniProtKB | ChEBI); catalytic
Binding site195-1987-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2487-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site258Proton acceptor; for 3-dehydroquinate synthase activity
Binding site262-2667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2697-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site269Zn2+ (UniProtKB | ChEBI); catalytic
Active site273Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2857-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site285Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3547-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site819For EPSP synthase activity
Binding site866-873ATP (UniProtKB | ChEBI)
Active site1170Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1198Schiff-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
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
      FLAG1_02044

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Fl201059
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium

Accessions

  • Primary accession
    A0A0N0DH64

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3823-dehydroquinate synthase
Domain78-3563-dehydroquinate synthase
Domain400-831Enolpyruvate transferase
Region1280-1568Shikimate dehydrogenase
Domain1285-1365Shikimate dehydrogenase substrate binding N-terminal
Domain1536-1566SDH C-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
    1,568
  • Mass (Da)
    170,643
  • Last updated
    2015-12-09 v1
  • Checksum
    45D19ADE239AE3BB
MAQAGGQGPTRISILGEPNIIVDHGLWLNFVVDDLLQNIPTSTYVLITDTNLFNSYVLAFQSRFENASQGKDTRLLTYTIPPGEASKSRDTKAEIEDWMLSQQCTRDTVIIALGGGVMGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPKRIYIDLTFLETLPVREFINGMAEVIKTAAIWNETEFSVLEESAAHILECVRSKGEGRLSPIRDVLKRIVIGSAGVKAEVVSSDEREGGLRNLLNFGHSIGHAFEAILTPQLLHGEAVAIGMVKEAELARFLGVLRPGAVARLVKCIASYDLPTSLQDKRVVKLTAGKKCPVDVLLEKMGVDKKNDGKKKKIVLLSAIGKCHEPRASVVDDKTIRTILSSSIQVTPGVPKDLAVTVAPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTQYMLSAIHQLGGASYSWQDAGEVLVVEGKGGNLQASKEPLYLGNAGTASRFLTTVVALASPVQNTTTNVLNGNARMKVRPIGALVDALRSNGLEIEYLGKENSLPLRIDAAGGFKGGDIELSATISSQYVSSILMAAPYAKNPVTLRLVGGKPISQLYIDMTIAMMASFGIDVEVSSKEPNTYHIPKGTYKNPPEYTIESDASSATYPLAVAAITGTKCTIPNIGSKSLQGDARFAVDVLRPMGCTVEQSDYSTTVTGPAPGQLKALAHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIAAMKDQLAKFGVQCNELDDGIEVIGKGQDGGVSTPDVGIHCYDDHRVAMSFSVLAVASPGPVIVTERECVGKTWPGWWDILSQVFKVDMVGHESDDDVHDEEIQEKTLESSVFIIGMRGAGKTTAGNWMAKILGWKFIDLDQELERRAGCTIPEMIRGDRGWDGFRADELALLQDVMEKNKTGHVFSCGGGLVETPEARELLKSYGANGGNVLLVHRDTDQVVEYLNRDKTRPAYTSEILQVYLRRKDFYNECSTHLYYSPHSESSGRQSYIPHDFRQFVQSISGKNTHFKDVLNKDHSFFVSLTVPNVDEAVDLLPEVVVGSDAVELRVDLLQDRSVDSVTRQISTLRASAKKPIVFTLRTESQGGKFPDSAYEEGLELYRLAVRMGMEYIDVEMTLPDDIIKTVTESRGYSRIIASHHDPKGTMSWKNASWIQYYNRALQYGDIIKLVGIARTPEDNFDLARFKARMQEAQKTPMISMNMGKAGKLSRVLNRFLTPVSHPALPFKAAPGQMSAAEIRQALSLLGDLEPHNFYLFGKPIAASRSPALHNTLFKQTGLPHQYHRLETDNIEDVRDVLKSPDFGGASVTIPLKLDIMDKLDELSDAARTIGAVNTVVPFGKPDVDGRRYLLGDNTDWRGMVHALHHAGIDGQDTDNKGAAMVVGSGGTTRAAIFALHSLGFGPIYIAARNQEKADAIAADFPKEYQLEGISEASGAKKVSEHLKVVISTIPADRPIDPTLQELVAIILGRPAPDAERRVLLEMAYKPSHTPIMQLADDAGNWTTIPGLEVLSSQGWYQFELWTGITPLYKDARAAVLGE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JXCE01000018
EMBL· GenBank· DDBJ
KPA45065.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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