E5ADS1 · E5ADS1_LEPMJ

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.

TypeIDPosition(s)Description
Binding site50-52NAD+ (UniProtKB | ChEBI)
Binding site87-90NAD+ (UniProtKB | ChEBI)
Binding site118-120NAD+ (UniProtKB | ChEBI)
Binding site123NAD+ (UniProtKB | ChEBI)
Binding site1347-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site143-144NAD+ (UniProtKB | ChEBI)
Binding site1507-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site1567-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site165NAD+ (UniProtKB | ChEBI)
Binding site1667-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Binding site183-186NAD+ (UniProtKB | ChEBI)
Binding site194NAD+ (UniProtKB | ChEBI)
Binding site198Zn2+ (UniProtKB | ChEBI); catalytic
Binding site198-2017-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 site3607-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI)
Active site832For 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
      LEMA_P001470.1

Organism names

Accessions

  • Primary accession
    E5ADS1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-3883-dehydroquinate synthase
Domain81-3623-dehydroquinate synthase
Domain407-844Enolpyruvate transferase
Region872-1064Shikimate kinase
Region1065-12853-dehydroquinase
Region1298-1591Shikimate dehydrogenase
Domain1303-1383Shikimate dehydrogenase substrate binding N-terminal
Domain1557-1587SDH 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
    1,591
  • Mass (Da)
    171,501
  • Last updated
    2011-02-08 v1
  • Checksum
    46C864AF82A1BABF
MATEGTSVEPTKVKILGKDSIVVDYGLWQGYIAQDLLSNIPSSTYVLITDTNIGPLYTPTFERAFSTAASTLSTTPRLLTYQIPPGETSKSRSTKAAVEDWLLSQGCVRDTVIIALGGGVIGDMIGYVAATYMRGIKFVNVPTTLLAMVDSSIGGKTAIDVPAGKNLVGAFWQPERIYIDLQFLESLPKREVINGMAEVVKTAAIWNEEEFTALEGNANTILAAIDQKPVHGRRNFDGIASILKRIVLGSVRVKAEVVSADEREGGLRNLLNFGHSIGHAYEAILTPQILHGECVAIGMVKEAELARYLGVLDPSAVARLTKCIASYGLPTSLADKTVRRRSANKHCPVDELIKIMAVDKKNAGAVKKIVLLSGIGRTYEKKASSVADRDIKIALSPSIAVHPGVPSDLDVTCTPPGSKSISNRVLVLAALGTGPCRITNLLHSDDTQVMLDALAKMQGASFAWEDDGKVLVVTGNGGNLKATSSELYLGNAGTAARFLTSVTALCRPVESITSTIVTGNARMKERPIAPLVKSLRTMGVEIEYVEKEGGLPLRIQACSGFGSDSFTGDIELTANVSSQYVSSILLSAPYSKKPVTLRLVGGKVISQPYIDMTIAMMASFGVQVERSASDPNTYHIPNKPYTNPSTYEVESDASSATYPLAIAAITGTTCTVPNIGSGSLQGDARFAIEVLRPMGCKVEQSKTSTTVTGPPRGELKAVKEIDMEPMTDAFLTASVLAAVASSDGTSTTTRIYGIANQRVKECNRIQAMEDELAKFGVTCRQFDDGIEVDGKGYDLATPQVGIHCYDDHRVAMSFAVLSLVAPAPVLILEKDCTGKTWPGYWDSLNQIFKVSLEGVELSTHSHGSKAASKSADRSIFIIGMRGAGKTTAGGWAARTLGRPLIDLDTALEEHVGMTIPEFISTRGWDGFRDEELQLLKRTVKEKPTGYVFACGGGIVESPEAREVLVDWHKQGGIVLLVSRDITKVVEFLQIDKSRPAYVEDIMPVWLRRKPFYDQCSNYRFHSQALESVGLASTQAQFARFLNTITGKNSVLKALKKKKHSFFVCLSAPELQSCIQTLPEIVVGADAVELRVDLLVDPNGQEGLPTPEYVIEQLTILRTVTTTPIIFTIRTKAQGGKFPDTAYDEARALYLTALRLGCEFVDLEMTMSEDILREVSEGRGYTEIIASHHDPKSELNWSNGSWMKYYNRALQYGTVIKLVGVAQSIKDNFALAEFKSWADTAHPVPLIAINMGEHGKLSRILNGFLTPVSHPLLPSATAPGQLSAADIRLGLSLMGEIPTKKFFIFGSPVSQSPSPRLHNRLFRETGLPHVYSRFETTDASSVRDIIRAPDFGGASVTIPLKQDVRTLLDGVGPEVEAIGALNTIVPETSIDETTGQEVTRLIGLNTDYLGMILVLKNAGALSQSGSALVIGGGGTSRGAIYALREMGYAPIYLLGRNLSKITALKDDFPAEYNVQIISSPEQVESLESMPAVAIGTIPADQPIDPAIRETLCALFAKAKKGEADVGSNGRILLEMAYKPPVTALIQLAQDAGWTTVNGLEVLVGQGVHQFEYWTGIKPLYAVAREAVMESSG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FP929139
EMBL· GenBank· DDBJ
CBY01360.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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