A0A1Y2GE11 · A0A1Y2GE11_9FUNG

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 site87-90NAD+ (UniProtKB | ChEBI)
Binding site118-120NAD+ (UniProtKB | ChEBI)
Binding site123NAD+ (UniProtKB | ChEBI)
Binding site1347-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site143-144NAD+ (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site165NAD+ (UniProtKB | ChEBI)
Binding site1667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site194NAD+ (UniProtKB | ChEBI)
Binding site198Zn2+ (UniProtKB | ChEBI); catalytic
Binding site198-2017-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site270Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2817-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site281Zn2+ (UniProtKB | ChEBI); catalytic
Active site285Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2977-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site297Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site838For EPSP synthase activity
Binding site905-912ATP (UniProtKB | ChEBI)
Active site1224Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1253Schiff-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
      BCR41DRAFT_425027

Organism names

  • Taxonomic identifier
  • Strain
    • NRRL 3116
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Lobosporangium

Accessions

  • Primary accession
    A0A1Y2GE11

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-3943-dehydroquinate synthase
Domain81-3683-dehydroquinate synthase
Domain419-850Enolpyruvate transferase
Region857-891Disordered
Compositional bias876-891Polar residues
Region1336-1628Shikimate dehydrogenase
Domain1341-1422Shikimate dehydrogenase substrate binding N-terminal
Domain1465-1524Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase

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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,628
  • Mass (Da)
    176,803
  • Last updated
    2017-08-30 v1
  • Checksum
    27C5C426D7350145
MSHPSPHIDKVSILGQETICLGFHIFDYLVRDTLSNFKASTYVIVTDTHLQKLYLDRFQCTFNKIAKELAHDAPLPRLLTYVIPPGENSKSRAVKAEIEDYFLAQGCTRDTLVFAMGGGVIGDLVGFVAATFMRGIPFVQIPTTLLAMVDSSIGGKTAIDTPQAKNSIGAFWQPKRIFIDLAVLETLPEREFVNGMAEVIKTAAIWNESDFVLLENGAEAIRDAVLKPVRNVEFQGATLETRTPAQQLLLKVVMASVAVKSYVVTHDERETGMRGLLNFGHSIGHAIEGLVTPKLLHGECVAIGMIKEAEIARHCGYLSQVAVGRLSRCIQAYGLPITMEDKFVKNHIGNQYCTVDELMQVLRVDKKNMGSQKRIVMLSGIGKTLEQKPTNISDDIIRKVLAGSTIVHPRPINVPPVTLSPPGSKSISNRALVLAALGKGTCRLTGLLHSDDTQVMLTALTKLGAATFEWENNGDTLVVHGNGGKMHIPDSELYMGNAGTAARFLTTVSVLVPPSTIPGQKTILTGNSRMKQRPIAPLIDALTTNGSELKYLETKGCLPLEVTPFSHGLAGGEIQLAASISSQYVSSILLCAPYATKEPVTLVLTGGQVISQPYIDMTIAMMKSFGITVEALPNNTYRIPQGTYVNPAEYLVEADASSATYPLAIAAITGTTCTVPNIGSTSLQGDAGFAVNVLRPMGCTVVQTETSTTVTGPPIGTLRPLPHIDMETMTDAFLTASVLAAVTQPATSGGNNVTKISGIANQRVKECNRIAAMMHELGKFGVVTSEFDDGIIVHGHDIASLSPPKDGVKCYDDHRVAMSFSVLANVIPGGTIIREKKCVEKTWPTWWDDLENKLGGRTSDIDLGPPSEHHDYEVKSSPSPSPSASSNKKNIVRNARNNATIVVIGMRGAGKTSMGRFAAKALKRPFEDVDQYFEKTLSTTIPEFIKEHGWAAFREKEAKMLVELLVKHPSGYVISCGGGIVETASSREAFKNYAAEGGIVLHLVRNINEIEAYLNRDTSRPMYGESMRDVWARREGWYRECCNYEFVVAGQQLKGIEAEDAKEWALVESNFERFLKVILTNKSSKHANRAQVVATPTFFLSLTFSDISPALPHLSKLTLGSDAIELRVDLLRAPEKSGISFRDHVAQQVSLLRRHSDLPILFTVRSVSQGGLWPDSDVHGMISLLNDGLGWGVEYLDIEIGLPRNEIDEVLAGRGNTLIVASWHDVKGTVAWSSDAMENQYMLAKSISPDVIKLIGAANSMKGNFECSEFAARHTAKTDDLPLISMNMGAQGQLSRILNNYLTPVTHKLLPVKAAPGQLSAHEILIARHIAGLLPAKQFYLFGTPISQSLSPLMHNTSFQSLGLPYTYGLHETATVDESVVAKMRSADFGGASVTIPHKIEIMSKLDEITDEAKAIGAVNTIVPIVDRQGKTILVGDNTDWLGIYYQIVRNLSSTTTIHPQNMSGLVIGAGGTSRAALYALYRLGVQEISIFNRTMVKAQAVADSFKNLFTVKILSANELLKNDDGAGTGFDLIISTVPGTIDSSAMFDDSIFGSISEKDKKGVAVELAYTPRFTRFLKLAAQAGWATVEGGQVLVEQGGWQALKWVGRKWDLESVLTQMDLVQAGRE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias876-891Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MCFF01000044
EMBL· GenBank· DDBJ
ORZ06789.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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