A0A9P5ZTV6 · A0A9P5ZTV6_PLEER

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 site45-47NAD+ (UniProtKB | ChEBI)
Binding site85-88NAD+ (UniProtKB | ChEBI)
Binding site116-118NAD+ (UniProtKB | ChEBI)
Binding site121NAD+ (UniProtKB | ChEBI)
Binding site1327-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site141-142NAD+ (UniProtKB | ChEBI)
Binding site1487-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1547-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site163NAD+ (UniProtKB | ChEBI)
Binding site1647-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site181-184NAD+ (UniProtKB | ChEBI)
Binding site192NAD+ (UniProtKB | ChEBI)
Binding site196Zn2+ (UniProtKB | ChEBI); catalytic
Binding site196-1997-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site266Proton acceptor; for 3-dehydroquinate synthase activity
Binding site270-2747-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2777-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site277Zn2+ (UniProtKB | ChEBI); catalytic
Active site281Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2937-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site293Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3627-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site832For EPSP synthase activity
Binding site881-888ATP (UniProtKB | ChEBI)
Active site1203Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1231Schiff-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

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

    • ORF names
      BDN71DRAFT_1449947

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 90797
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Pleurotineae > Pleurotaceae > Pleurotus

Accessions

  • Primary accession
    A0A9P5ZTV6

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3903-dehydroquinate synthase
Domain80-3643-dehydroquinate synthase
Domain416-844Enolpyruvate transferase
Region1314-1600Shikimate dehydrogenase
Domain1319-1400Shikimate dehydrogenase substrate binding N-terminal
Domain1435-1485Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
Domain1563-1588SDH 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
    1,600
  • Mass (Da)
    172,705
  • Last updated
    2023-09-13 v1
  • Checksum
    773F8F6707A8303F
MAATDVFKVSILGKESIHCGFHLFPHIAATVLSTLPSSTYVLVTDTNVANFHLSTFEEEFMASIGRLENVLTRPRFLSHVILPGETSKSREGKANIEDFLLLNKCTRDTVILALGGGVIGDLVGFVAATFMRGVRFVQIPTTLLAMVDSSVGGKTAIDTPQGKNLIGAFWQPEYIFIDAAFLETLPAREFSNGMAEVVKTAAIWDESEFASLESRYGEIFAAIQTPSRDYSGRTKATRSPAQDILLSVIVGSISVKAHIVTIDERETGLRNLVNFGHTIGHAIEAVLTPTILHGECVSVGMVLEAEVSRQLGVLSQVGVGRLSRCLKSYNLPIALSDLRIANLPASKFLTVDKLLDIMRVDKKNSGPEKKVVILSKIGATYEQKATVVRDDVIAKTLSEAARVVPGIPSKDPVKMATPGSKSISNRALVLAALGQGTCRLKNLLHSDDTAVMMAALMELKGASFSWEDGGETLVVQGGDGSLSVPTKGKELYLGNAGTAARFLTTVCTLVQSTSSSDGTATVITGNARMKQRPIGPLVNALKANGAQIEYLESQGCLPLSIAPNGLKGSRIQLAASVSSQYVSSILLCAPYAAEAVTLELTGGQVISQPYIDMTVAMMKTFGVDVVRRRDPETNALLDIYDIPKATYISPPVYAIESDASSATYPLAIAAITGTTCTIENIGSASLQGDARFAKEVLERMGCSVTQTETETTVTGPPIGSLQAIEEVDMEVMTDAFLTATALAAVAKGKTRILGIANQRVKECNRIRAMIDQLAKFGVETNELDDGLEIIGRPIAELKEGVSVHCYDDHRVAMAFSVLGSVIKGTILEEKRCVEKTWPNWWDDLENKIGLKVEGVELPPSNATSSVGALSPESAASVVVVGMRGSGKTFIGELAASALSWTFVDADAYFEEKHQTGVREFVHKNGWPAFREAETSLLKELLTADEKSTRHVISLGGGIVDTEGARQLLKDYATKGPVVHVIREIDEVVKYLGAEVSRPAYGEPITDVFRRREPWYKECSNYEFVNWVTSGSSASDEVTTRKTTRAEVERFFKHITGERPNLAHNLVPGNRSYFLSLTYPDVTPALPHIEELTTGVDAIELRVDLLRSPKDFDVVGKYIPPATYVADQIALLRRSTTLPIVFTVRTASQGGSFPDNADDEAFELLNLGLRMGVEYIDVETSWPAKRIQGLVSRKGFSQIIASWHDWSGKVQWSSGAVKEKYDAAKAFGDIVKIVGKANRLEDNFELFTFVKRVSSVPGAKPIIAINMGVEGQMTRILNTSFSPVSHPLLPNKAAPGQLSFPQIQQALHLLGQLPSRRFFLFGTPIAHSMSPTLHNTAFSLLGLPYIYELLETKAVGEEIKAALASHDFGGASVTIPFKLDIVPLLDELSPAAQAIGAVNTVIAKPTESSKILYGDNTDWIGIRTSVVNIVGEGNIYSALVIGAGGTARAALYALTSLGAKKIYLFNRTQSKAQELEAAFSNSAIEVIGELGSWSSDPPNVIVSTVPASATTIEALNNSLQIPVSIFNYRSGPAVVVDMAYKPAETPLLQLAKRLAGDNWTTVPGVEVLLEQGYQQFKLWTGRACPRKAVSSKVWEKYNTSV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MU154582
EMBL· GenBank· DDBJ
KAF9493700.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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