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A0A3N4KK94 · A0A3N4KK94_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 site91-94NAD+ (UniProtKB | ChEBI)
Binding site122-124NAD+ (UniProtKB | ChEBI)
Binding site127NAD+ (UniProtKB | ChEBI)
Binding site1387-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site147-148NAD+ (UniProtKB | ChEBI)
Binding site1547-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site169NAD+ (UniProtKB | ChEBI)
Binding site1707-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site187-190NAD+ (UniProtKB | ChEBI)
Binding site198NAD+ (UniProtKB | ChEBI)
Binding site202Zn2+ (UniProtKB | ChEBI); catalytic
Binding site202-2057-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2617-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site271Proton acceptor; for 3-dehydroquinate synthase activity
Binding site275-2797-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2827-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site282Zn2+ (UniProtKB | ChEBI); catalytic
Active site286Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2987-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site298Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3677-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site833For EPSP synthase activity
Binding site879-886ATP (UniProtKB | ChEBI)
Active site1188Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1216Schiff-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
      P167DRAFT_525254

Organism names

  • Taxonomic identifier
  • Strain
    • CCBAS932
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Pezizomycetes > Pezizales > Morchellaceae > Morchella

Accessions

  • Primary accession
    A0A3N4KK94

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3953-dehydroquinate synthase
Domain85-3693-dehydroquinate synthase
Domain419-845Enolpyruvate transferase
Region872-1064Shikimate kinase
Region1297-1591Shikimate dehydrogenase
Domain1302-1384Shikimate dehydrogenase substrate binding N-terminal
Domain1428-1484Quinate/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
    1,591
  • Mass (Da)
    174,982
  • Last updated
    2019-02-13 v1
  • MD5 Checksum
    67830362A167A04EB6A7C1312B705D96
MVTAETNGTSVPMEIATVSILGKDTIKVGYDLIHEITSDILQNLKSTTYVLITDINIGRIYLPRIEEAFEQDSQKYSPNARLLTYTIPPGEASKTRVTKAEIEDWMLSKECTRDTVIIALGGGVIGDMIGYVAATFMRGVRFIQVPTTLLSMVDSSIGGKTAIDSPHGKNLIGAFWQPERIYIDLQFLETLPEREFINGMAEVIKTAAIWDEEEFTKLEKSSDVILQAVRSKITAIQEGPSRLSSVKQLLKEVVLGSVRTKAHVVSADEREGGLRNLLNFGHTIGHAIEAILFPQMLHGECVAIGMIKEAELSRHLGHLKPSAVARISKCLTAYGLPTSLDDKRVKKLTAGKHCEVEEMIRIMGVDKKNDGRKKKVVLLTAIGKTLERKASVVLDDAIRVIMAPSVIVDSQKSVIPELSITPPGSKSISNRALVLAALGTGTCRIKNLLHSDDTEHMLTALYKLGGMQFSWEDDGDTLVVNGNGGKLTACGDELYLGNAGTAARFLSTVATLVSPSTENDSIVLTGNARMKQRPIGPLVNALRSNGNTVDYLEDEGCLPLRVPSTSGFAGGKIELAATVSSQYVSSILMCAPYARQPVTLSLVGGKPISQLYIEMTTAMMASFGIQVTKSETEEYTYHIPQGTYKNPSEYVVESDASSATYPLAIAAITGTTVTIPNIGKKSLQGDARFAVDILRPMGCEVVQTDYSTTVRGPAKGQLKPIPQVDMEPMTDAFLTASVLAAVAVGSERTNITGIANQRVKECNRIAAMVHELAKFGVTAGELEDGIWIEGKDYSTLQSPVDGVHCYDDHRMAMSFSVLSLIAPEPVIVLEKECTAKTWPGWWDVLASSFKVALNGTEIIDHSEPSIIKKGNNASIIIIGMRGAGKTTMGNIATRIMQRPLLDLDVVMEEEQGRVIPDIVKTDGWEGFRQIEFDLLKRKMAEHPTEHIIACGGGIIETPEARELLIRYHQTGGIVIHIHRNIENVIDFLNVDKTRPAFSEDLHNVWLRRRPWYDECSNFQYYSPVVSAEHLDIAQADFARFLHVIIGKANYHEKFLRRERTFFVSLTYPDISQAIDIVGPVTIGADALEIRVDLLEDPNGEYGVPTIKFVSEQLALLRSKTQLPAIFAIRTVSQGGRFPDDAPEKALEFFLTAIRMGLEYIDLEMSWPLLVIEKVTASKNHTKIIASHHDVQGHLRWKNASWVSIFNTALKFGDVIKLIGVANKLQDNFDLQNFREWASSRATRLIALNAGEKGKLSRILNMFLTPVTHPALPFKAAPGQLTVSEIHRGLWLMGEIERKQFYLFGKPIQHSRSPALHNHLFKDMGLPHHYQIFENDTVNDEATRAILYADDFGGASVTIPHKLNIMPLLDEITPEAEMIGAVNTVLPVLVKTRGETKRKLVGYNFDWVGIKTSLFQGGVRDTYDDPGSALVIGAGGTSRAAVYALHNMRYNTIYIINRSVANLQPIIDAFPAEYNIIAVKTLEEAQAISVKPVTAVSTVPADKPIDAATKAILTELLKVNPTDSQKERVLAEMAYKPRHTEVMELAEEAGWKTVPGLEALTGQGVKQFEVFTGGIIPDYEQARQAVLGDEKY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ML119139
EMBL· GenBank· DDBJ
RPB10977.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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