A0A0F4ZJ30 · A0A0F4ZJ30_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.
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 site44-46NAD+ (UniProtKB | ChEBI)
Binding site81-84NAD+ (UniProtKB | ChEBI)
Binding site112-114NAD+ (UniProtKB | ChEBI)
Binding site117NAD+ (UniProtKB | ChEBI)
Binding site1287-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site137-138NAD+ (UniProtKB | ChEBI)
Binding site1447-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site159NAD+ (UniProtKB | ChEBI)
Binding site1607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site177-180NAD+ (UniProtKB | ChEBI)
Binding site188NAD+ (UniProtKB | ChEBI)
Binding site192Zn2+ (UniProtKB | ChEBI); catalytic
Binding site192-1957-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 site820For EPSP synthase activity
Binding site877-884ATP (UniProtKB | ChEBI)
Active site1184Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1212Schiff-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
      TD95_003439

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CR-DP1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Microascales > Ceratocystidaceae > Thielaviopsis

Accessions

  • Primary accession
    A0A0F4ZJ30

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3843-dehydroquinate synthase
Domain75-3583-dehydroquinate synthase
Domain402-832Enolpyruvate transferase
Region1294-1606Shikimate dehydrogenase
Domain1299-1379Shikimate dehydrogenase substrate binding N-terminal
Domain1569-1599SDH 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
    1,606
  • Mass (Da)
    172,276
  • Last updated
    2015-06-24 v1
  • Checksum
    D82A572AC7D83F23
MADPTRIPILGKENIIINSGLWLDFVPQELLTHLTSSTYVLITDTNLYDTYVPPFKAVFEKLAAATPDAPRLLTYSIPPGEVSKSRETKAEIEDWMLEQQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPTGKNLVGSFWQPQRVFIDLLFLETLPEREFINGMAEVIKTAAIWDEAEFSALEQNAPAILAAVKTKPSAGASNTRLASIQPILKRIVMGSARIKAHVVSSDEKESGLRNLLNFGHSIGHAIEALLTPQLLHGEAVAIGMVKEAELSRYLGVLSPGAVARLSKCIASYDLPISVHDKRVAKRTAGKKCPVDVLLSKMAVDKKNVGKAKKIVLLKAIGKTLEEKATTVDDNAIRVVLSPAIVESPGISKNLNVTVTPPGSKSISNRALVLAALGTGSCRIKNLLHSDDVEFMLAALSKLGGATYSWEEAGEVLVINGKGGKLNACDEPLYLGNAGTASRFLTTVVALCQPVGETVSTVLTGNARMQQRPIGPLVDALRSNGLAIKYLGPNLSLPLQIDAAGGFEGGVIELAATISSQYVSSILMAAPYAKEPVTLKLVGGKPISQLYIDMTIAMMKAFGVTVERSATEENTYHIPKGVYSNPAEYVIESDASSATYPLAVAAITGTTCTVPNIGFSSLQGDARFAMEVLKPMGCTVEQTATSTTVTGPAIGSLKAIPHVDMEPMTDAFLTASVLAAVAAGTTTITGIANQRVKECDRIAAMRTQLAKFGVTCVELDDGIQVQGRPLAELQTPETSVYCYDDHRVAMSFSVLALVAPKPVLILERECTGKTWPGWWDTLSSKFGGSLDGADVLPDHGSSASGGEKAKDATDVPAAAARSVFLIGMRGAGKSTTGKWAASLLGMKFVDLDRELERRVGKTIPDMIHGSEGWEGFRKAELELLSEVTKEPVHSTGFVFSCGGGIVESPEARKMLTGYHTSGGRVILVHRNIDRVISYLNADQTRPSFGQDIRAVYLRRKPWYRECSTHAYMSPHFEDSAISHSSPPADFRAFVSAVFDQEHHLERVRHAKQSFFVSLTFPDLFAVKDLIPQIVVGADAVELRVDLLENLSREEVACQVSLLRSLAPLPVVFTLRTVSQGGKFPDNDHAKALELYQTAIRIGVEYLDLEMTLPTEMLVSLTESKGQSRIIASHHDPLGSLSWKNGGWIPWYNKALQYGDVIKLVGMASKLEDNFDLANFKARMLAAHDTPIIALNMGPHGKLSRVLNGFLTPVSHEALPFKAAPGQLSAAEIRRALALLGEIDTKQFYLFGKPISASQSPALHNTLFQATGLPHTYSRFETDDAAAVTDLIRAPHFGGASVTIPLKLDVIPLLDEVSAAATALGAVNTIIPVTRTVTRSNGQTETQTRLLGDNTDWRGIVHTLKIAGIEKLVGDADAQAESSTPRPAAVVGSGGTSRAAIYALKSLGFSPIYVVARNAKSLDELAATFGGDCDLRFLSSVAEVEQLSSSSSSAVAAIVSTIPADRPIDANMREVLIALLHSAFDPEQSRILLDMAYKPLQTPLMQMAADSKGKWKTINGLEVLVSQGWFQFQLWTGITPLFSDARAAVLGPDAAQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LAEV01000655
EMBL· GenBank· DDBJ
KKA29878.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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