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A0A6J3MBD0 · A0A6J3MBD0_9PEZI

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.

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 site92-95NAD+ (UniProtKB | ChEBI)
Binding site123-125NAD+ (UniProtKB | ChEBI)
Binding site128NAD+ (UniProtKB | ChEBI)
Binding site1397-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site148-149NAD+ (UniProtKB | ChEBI)
Binding site1557-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1617-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site170NAD+ (UniProtKB | ChEBI)
Binding site1717-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site188-191NAD+ (UniProtKB | ChEBI)
Binding site199NAD+ (UniProtKB | ChEBI)
Binding site203Zn2+ (UniProtKB | ChEBI); catalytic
Binding site203-2067-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2577-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site267Proton acceptor; for 3-dehydroquinate synthase activity
Binding site271-2757-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2787-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site278Zn2+ (UniProtKB | ChEBI); catalytic
Active site282Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2947-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site294Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site832For EPSP synthase activity
Binding site887-894ATP (UniProtKB | ChEBI)
Active site1199Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1229Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
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
      K489DRAFT_377871

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 342.82
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetidae > Mycosphaerellales > Dissoconiaceae > Dissoconium

Accessions

  • Primary accession
    A0A6J3MBD0

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane117-138Helical

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3903-dehydroquinate synthase
Domain88-3643-dehydroquinate synthase
Domain411-844Enolpyruvate transferase
Region1312-1608Shikimate dehydrogenase
Domain1317-1397Shikimate dehydrogenase substrate binding N-terminal
Domain1574-1604SDH 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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,608
  • Mass (Da)
    173,851
  • Last updated
    2020-10-07 v1
  • MD5 Checksum
    86ED29DB2E30578B181C44F059248AD2
MQSTNGSHGAIKVPILGKESIIVDYGLWRNYVVRDLLANIVSSTYVLICDSNLAKFDYVPFFKQQFEAERERLGKSAQQARLLIYDRIRPGERSKSRKTKNDIEDWLLLRGCTRDTVILALGGGVIGDLIGFVAATYMRGVRFCQIPTSLLAMVDSSIGGKTAIDTPLGKNLIGSFWQPERIYIDLAFLETLNKRQVCNGMAEVVKTAAIWDESEFERLEANAEAIMEALSKPPGAGRFKGIEDIFKRIVLGSARVKAEVVSADEREGGLRNLLNFGHSIGHAYEALWTPEVLHGECVAVGMVKEAELARHLGMLPPGAVARLTKCIASYGLPVSVDDKLITSLTSTQCPVDELLRRMAVDKKNAGSTKKIVMLAAIGRCYEPKATAIVDKYIRIVLCPAIQVKPGVAPSLRATCKPPGSKSISNRVLLLAALGQGTCKISNLLHSDDTQFMLSALGQLGGASYSWEDEGRVLVVKGNGGALKASTTEVYIGNAGTASRFLTTAVSLAQASPAASHTVLTGNARMQERPQGPLVDALRSNGVDIEYVGKPGSQSLPLRIAAAGGFEGGVIELTAKVSSQYVSSILMCAPYAKNPVTLRLVGGKVISQPYIDMTLAMMADFGVTVTRDGSEPNVYHVPKQNYANPSVYEVESDASSATYPLAIAAITGTTCTIPNIGSASLQGDARFAVDVLEPMGCTITQTKTSTTVTGPPVGELKPLPQIDMEPMTDAFLTASVLAAVAKPNEKGATTRITGIANQRQKECNRIKAMHDELAKFGVVCRELEDGIEIDGRGVQLGAASIGIDCYDDHRVAMSFGVLGVVAPKQTLILERECTGKTWPGWWDQMHQTFGVDLEGIEVDNVPASGNTVAGGRHTARNAISNKSIFIIGMRGAGKTTAGRWASGTLGWPFIDMDDELEASEGMKIPEMLKDNDWEGFRRREVNLLKRLMKEKPTGHIFATGGGIVETPEARQLLKDWHKDGTVLHISRDIESVMEFLQIDKTRPAYVEDMMGVYLRRRPWFEECSNLHFHSQTIDLNTVPSAWTNPLDTFARFLDTAFGRSEVLEGIRAKQHSFFLSLTSPTIEKILPLLKEITVGVDAIELRADLLVDGSSAIGLPTPEHLTQQITLLRASTSLPLIFTLRTVSQGGRFPDQDKDGAKQLYAVALKMGFEFIDVELTSDTELKKFILDRRRASAIIASHHDPKGELSWQDSGAEWVPHYDAAREYGDIVKLIGVARSTIDNDDLKNFKRWAAEERSDVPVIAMNMGEFGKMSRVTNGFMTPVSHPSLPFTAAPGQISAADIRKVLSLVGEISPKTFCLFGKPIQSSRSPALHNALFQATGLPHSYILRESDNASQEVDFIRSPNFGGASVTIPLKLDFMDLIDSVDDAAKTIGAVNTIVPSRGLGGKTVLIGYNTDWQGMVLSLRNAGAQTTLSGTPESALVVGGGGTARAALFALKSMGYSPLFLVGRNPSKLTSLGASFPSNYDIRILSSEADVKGLVPYQLPSVSIGTIPGDAPIDPIMEKVLGAVFHGSTSQQSDAVTAPRKRILLEMAYKPAVTPLVTLAASAGWAIVPGLEALVGQGVYQFKLWTGITPLYEFSRQAVMGSKV

Keywords

Sequence databases

Similar Proteins

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