N1PVJ0 · N1PVJ0_DOTSN

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 site89-92NAD+ (UniProtKB | ChEBI)
Binding site120-122NAD+ (UniProtKB | ChEBI)
Binding site125NAD+ (UniProtKB | ChEBI)
Binding site1367-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site145-146NAD+ (UniProtKB | ChEBI)
Binding site1527-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1587-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site167NAD+ (UniProtKB | ChEBI)
Binding site1687-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site185-188NAD+ (UniProtKB | ChEBI)
Binding site196NAD+ (UniProtKB | ChEBI)
Binding site200Zn2+ (UniProtKB | ChEBI); catalytic
Binding site200-2037-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2547-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site264Proton acceptor; for 3-dehydroquinate synthase activity
Binding site268-2727-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site2757-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site275Zn2+ (UniProtKB | ChEBI); catalytic
Active site279Proton acceptor; for 3-dehydroquinate synthase activity
Binding site2917-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site291Zn2+ (UniProtKB | ChEBI); catalytic
Binding site3597-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site829For EPSP synthase activity
Binding site895-902ATP (UniProtKB | ChEBI)
Active site1207Proton acceptor; for 3-dehydroquinate dehydratase activity
Active site1237Schiff-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
      DOTSEDRAFT_70392

Organism names

Accessions

  • Primary accession
    N1PVJ0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-3873-dehydroquinate synthase
Domain85-3613-dehydroquinate synthase
Domain406-841Enolpyruvate transferase
Region1320-1621Shikimate dehydrogenase
Domain1325-1406Shikimate dehydrogenase substrate binding N-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
    1,621
  • Mass (Da)
    175,158
  • Last updated
    2013-06-26 v1
  • Checksum
    E154F8A6409AA7CA
MTTASGSPTATKVKILGKESIVVDYGLWPNYAVHDLLSNIPSSTYVLICDSNIAKLPYVPAFKKSFEQELAVQGKQARLLMYDQVAPGEESKSRRTKAHIEDYLLSQGCTRDTIILALGGGVMGDLIGFVAATYMRGVKFVQVPTSLLAMVDSSIGGKTAIDVPLGKNLVGAFHQPERIYIDLAFLETLDKRQVCNGMAEVVKTAAIWDVEEFERLEDNANAIMTALEKPIGQGRFKGIENVFKRIVLGSARVKAEVVSTDEKEGGLRNILNFGHSIGHAYEAILTPEILHGECVAVGMVKEAELARYLGLFPPGAVARLQKCIASYGLPTTLHDKLILKQTKKQCPVDELLKKMAVDKKNAGSKKKITLLSSIGQCYEPHATTCEDKDIRIVLSPSIKVKPGVPKSLNVSCKPPGSKSISNRVLLMAALGAGTCRISNLLHSDDTQFMLTAIAKLGGATYSWEDDGRILVLNGNGGALKASYDEIYIGNAGTASRFLTTAVCIAQATKDVSHTVLTGNARMQERPQGPLVDALKANGVDIEYLGKPGSQSLPLKIAAAGGFEGGDIELTAKVSSQYVSSILISAPYAKTPVTLRLVGGKVISQLYIDMTIAMMAAFGVHVTRSKTEPNVYHVPNQKYKNPAAYEVESDASSATYPLALAAITGTTCTVPNIGSASLQGDARFAVDVLRPMGCNVKQTETSTTVTGPPLGELQPIPEVDMEPMTDAFLTASVLAAVAKPGQHGATTRIVGIANQRQKECNRIKAMYDELAKFGVTCRELEDGIEVDGRGIHISPASGTIHTYDDHRVAMSFSVLGAVAPRGTLLEERECVGKTWPGWWDHLHQIFGVELEGVEEYKHINGVLTNGVNGVDRPLLVKGVSGTYQHREVKKSIFIIGMRGAGKTTTGGWASRILGWPLADMDTELEAQEGMSIPEMLKDNDWVGFRQKELKLLKRLITEKPNGHIFAAGGGIVETPQCREILKDWQNEGMVLYVTRDIRAVMDFLQIDKTRPAYVEDMMGVYLRRKPWFEECSNLHYHSQKIDESAAIAGWTSPLDDFTRFLNTMTGRSGALQKIQKKKHSFFVALTSPQIEKVTTILPEVTMGSDAIELRADLLVDEKSTDGLSSPDFLTEQVSLLRSSSTLPLIFTLRSVSQGGRFPDGDSTRAIALYAVALRMGFDFVDLELTSLPDVKEYVLNHRKMCTIIASHHDPKATLSWADGAKDWIPHFDAAQEYGDIVKLVGVAKTDDDNDDLKTFKKWAAKEYAHKPFIAMNMAEIGKMSRVNNGFMTPVSHPALPSKAAPGQLSAAEIRKVLGLVGHIKPKKFCIFGKPVQHSRSPALHNTLFDATGLPHAYGLHETDLVDDEVQKIISSPDFGGASVTIPLKLDIMPLLDEVDPAAKTIGAVNTIVPVENDGGRATLIGHNTDWQGMVLALRNAGAHSAPGQRHAAAMVVGGGGTARAAIYALKEMGHSPIYLVGRNKSKLAALAGNFSTDYNVQLLGSADEVRTIPAEKQPIVAVGTIPGDIEPDPAMKEILTAIFEVGSTASNAAGVTGANANKVLLEMAYKPAVTPLMEIASHGGWRTVPGLEALVGQGVHQFRLWTAITPIFNVARDAVMGKTGQK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KB446537
EMBL· GenBank· DDBJ
EME46370.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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