A0A017S5L2 · A0A017S5L2_ASPRC

Function

function

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

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 site114-116NAD+ (UniProtKB | ChEBI)
Binding site119NAD+ (UniProtKB | ChEBI)
Binding site1307-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site139-140NAD+ (UniProtKB | ChEBI)
Binding site1467-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site161NAD+ (UniProtKB | ChEBI)
Binding site1627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site179-182NAD+ (UniProtKB | ChEBI)
Binding site190NAD+ (UniProtKB | ChEBI)
Binding site194Zn2+ (UniProtKB | ChEBI); catalytic
Binding site194-1977-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site260Proton acceptor; for 3-dehydroquinate synthase activity
Binding site264-2687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2717-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Active site275Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2877-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site287Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site824For EPSP synthase activity
Binding site871-878ATP (UniProtKB | ChEBI)
Active site1180Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1208Schiff-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
      EURHEDRAFT_415450

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 135680
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus

Accessions

  • Primary accession
    A0A017S5L2

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3843-dehydroquinate synthase
Domain77-3583-dehydroquinate synthase
Region397-842EPSP synthase
Domain406-836Enolpyruvate transferase
Region864-1056Shikimate kinase
Region1057-12773-dehydroquinase
Region1290-1582Shikimate dehydrogenase
Domain1295-1375Shikimate dehydrogenase substrate binding N-terminal
Domain1548-1578SDH 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
    1,582
  • Mass (Da)
    171,118
  • Last updated
    2014-06-11 v1
  • Checksum
    8F5B99AD27E315D1
MSEPTKISILGRESIISDFGIWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAAGITPAPRLLVYYAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRYVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGSIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALENNAEVILNAVRSEVKPGQSRFEGIQDIIKARILASARHKAYVVSADEREGGLRNLLNWGHSIGHAIEAILTPQVLHGECVAIGMVKEAELARHVGVLKGVAVARVVKCIAAYGLPTSLKDAQIRKLTAGKHCSVEQLLFNMALDKKNDGPKKKVVLLSAIGRTHEPQASVVSNEEIGVVLAPSVEVQPGVAPALSVTCAPPGSKSISNRALVLAALASGTCRVKNLLHSDDTEVMLNALERLGAATFSWEDEGEVLVVNGKGGNLEATPSPLYLGNAGTASRFLTSVATLANASSADSSILTGNNRMKQRPIGDLVDALTANGAEIEYQEKKGSLPLKIAASGGFAGGSINLAAKVSSQYVSSLLMCAPYAKEPVTLRLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYVNPAEYVVESDASSATYPLSIAAITGTTCTVPNIGSKSLQGDARFAVDVLRPMGCTVEQTAASTTVTGVPGGALKPLPNVDMEPMTDAFLTASVLAAVAQGDNSKHTTRIYGIANQRVKECNRIQAMKDELAKFGVVCREHDDGLEIDGVDRSTLRQPAGGIFCYDDHRVAFSFSVLSLVAPQSTLILERECVGKTWPGWWDTLRQLFAVKLEGKELTEAESPALTRAEKASASVFIVGMRGAGKTTTGHWIAQTLNRPFVDLDTELESSEGITIPDIIKQRGWQGFRDAELNILQRMMKERTTGYVFACGGGVVEIPEARKLLIDYHKGKGNVLLVMRDIKQVMDFLSIDQTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHSGSGALALPSEDFKRFLHVVTGQQDSLNVMKKKKESFFVSLTLPDLRPSGDILDQVSIGSDAVELRVDLLKDPSSDNDVPSVDYVAEQVSFLRSRISLPLIFTIRTQSQGGCFPDDAHDAAMQLYKLALRSGSEFVDLEIAFPDEMLRAVTEMKGHSKIIASHHDPKGELSWANMSWMKFYNRALEYGDVIKLVGVAKNLDDNTSLRKFKTWAEEAHDVPLIAINMGDNGQLSRILNGFMTPVSHPALPFKAAPGQLSATEIRRGLSLMGEIKAKKFAVFGSPVSASRSPILHNTLFNYMGLPHEYGRLETTNVEDVKDFIRSPDFGGASVTIPLKLDIMPLLDEVAEAAEIIGAVNTIVPVSNGEGKPARLVGYNTDWQGMQLSLRNAGVGNAAGDASAAVVGGGGTARAAIYALHQMGYSPIYIFGRSPAKLESMVSTFPTSYNIRVVEDVSKLDTVPNVAIGTIPGDKPIDPAMRENLCHLFDRTEQVDPDHIKSIDKSPRVLLEMAYKPAVTPLMQLANDSGWNTVPGLEVLVGQGVFQFKHWTDISPPYNDARDAVLGNSS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KK088437
EMBL· GenBank· DDBJ
EYE92328.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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