A0AAI9SXM2 · A0AAI9SXM2_9ASCO

  • Protein
    Pentafunctional AROM polypeptide
  • Gene
    ARO1
  • 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.

TypeIDPosition(s)Description
Binding site42-44NAD+ (UniProtKB | ChEBI)
Binding site80-83NAD+ (UniProtKB | ChEBI)
Binding site111-113NAD+ (UniProtKB | ChEBI)
Binding site116NAD+ (UniProtKB | ChEBI)
Binding site1277-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site136-137NAD+ (UniProtKB | ChEBI)
Binding site1437-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1497-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site158NAD+ (UniProtKB | ChEBI)
Binding site1597-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site176-179NAD+ (UniProtKB | ChEBI)
Binding site187NAD+ (UniProtKB | ChEBI)
Binding site191Zn2+ (UniProtKB | ChEBI); catalytic
Binding site191-1947-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2437-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site253Proton acceptor; for 3-dehydroquinate synthase activity
Binding site257-2617-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2647-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site264Zn2+ (UniProtKB | ChEBI); catalytic
Active site268Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2807-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site280Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3517-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site870-877ATP (UniProtKB | ChEBI)
Active site1170Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1199Schiff-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

    • Name
      ARO1
    • ORF names
      KGF56_002561

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 10844
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Candida/Lodderomyces clade > Candida

Accessions

  • Primary accession
    A0AAI9SXM2

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3793-dehydroquinate synthase
Domain74-3533-dehydroquinate synthase
Domain403-838Enolpyruvate transferase
Region1279-1553Shikimate dehydrogenase
Domain1284-1365Shikimate dehydrogenase substrate binding N-terminal
Domain1399-1477Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain1521-1551SDH C-terminal

Sequence similarities

Belongs to the EPSP synthase family.
In the 2nd section; belongs to the EPSP synthase family.
In the 2nd section; belongs to the type-I 3-dehydroquinase 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 shikimate kinase 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
    1,553
  • Mass (Da)
    170,556
  • Last updated
    2024-07-24 v1
  • Checksum
    A00BD5EEC87E3C54
MKIEKVPILGKETIHIGYQIQSHIVNEIIKELASSTYVIITDTNMCQTGTYEKLKTSFEETLQKERPQSRLLTYLVPPGENNKNRKTKAQVEDFLLQQGCTRDTVILAVGGGVIGDMIGFVAATFMRGVRVVQIPTTLLAMVDSSVGGKTAIDTELGKNFIGAFHQPEYVFCDVSFLQTLPTRQLINGMAEVVKTATIWDEEEFTRLEKFSKQFVAEVSSPEKNLENIKTDLIKTVLGSVRVKALVVSADEKEGGLRNLLNFGHTIGHAIEAILTPEALHGECVSIGMIKEAELSRYLGILPPAAVARLSKCLTAYNLPVSVDDKNFAKIVGAKKNNLEIDTLIKKMSIDKKNDGSKIKCVLLEKIGKCFDSKAHQISKEDLRFVLTDEVLVHPFKDFPSSITITPPGSKSISNRALILAALGKGTVRIKNLLHSDDTKYMLDALVLLKGATVSFEDETVVVTGNGGDLFACKEELYLGNAGTASRFLTAVASLVKESSKNDNVVVLTGNSRMQERPIGPLVDSLKANGSEIEYLNKQGSLPLKIVASPSASASAAAGKGFKGGKITLAATTSSQYVSAILMCAPYANEEVTLTLVGGKPISQLYIDMTCAMMKEFGVEVVKSTTEEYTYHIPRTTYKNPSEYIVESDASSATYPLAFAALTNSSCTIPNIGSSSLQGDARFAVDVLKPMGCAVVQTEHSTTVTGPPIGELVALSSVDMEPMTDAFLTASVVAAVAQGKTTITGIANQRVKECNRIKAMCDELAKFGVEASEISDGIVISGVDPTDLKTPPLDPGVKTYDDHRVAMSFSLLAGLCKKPVLILERSTTGKTWPGWWDILHSQFKTTLEGYQGKAVVGAGEQNGDKSVIVIGMRAAGKSTLSKWLADFLGFKLLDLDHHLESKLGQDIKSLIKEKGWEYFREQETIVLKECLANYSRGYVLATGGGIVECEQPRSTLIDYMANGGIVLHLHRDLDETVAFLNSDATRPSYSHEIKDVWLRREKWYHECSNYYFYSTHCTTQEDFATLKRTFLKFIAKIAGLDTFEIPKGRSSFVTLTYPDLKACMSLIKDVTAGSNAVELRVDLLASTQPEYVAEQIGVLRKSVDLPILYTIRTASQGGRFPDDKDDEMRNLLLFGLKMGVDLVDLQLTCSNTTISKVSEQRGYTKILASHHDFSGDLKWDNSQWQDKYNYGKAINADVIKLVGKATTFDDNLKLEHFRKENTEKPLIAINMGPRGKLSRVLNTILTPVTHDLITDKPTGVGQLSLEEINRAFYQIGGFVEEKFWVVGSPVGHSRSPALHNAAYKALGLPYKFDKFDTDNAEKVYNELMLEPNFGGLAITIPLKIDMMTYCTELSESSKIIGAINTIVPAKNGFLGDNTDWIGIANSFKQNGFIEGKSVSGLVIGGGGTSRAAIYALHKLGCEKIYLLNRTESKLLDLIKNFPSEYNLEIISLNLEEIETRDISLIVSCVPGDKPLDEKLITRLEKILKNNSESILLEAAYKPRFTPIMQLAREKYKCRVIPGVEMLINQGDAQFKIHTGYPAPYSIIREAVLED

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHUZD010000091
EMBL· GenBank· DDBJ
KAI3404616.2
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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