A0A932YPR1 · A0A932YPR1_9BACT

Function

function

Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

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 site233-phosphoshikimate (UniProtKB | ChEBI)
Binding site23phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site243-phosphoshikimate (UniProtKB | ChEBI)
Binding site283-phosphoshikimate (UniProtKB | ChEBI)
Binding site94phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site122phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1683-phosphoshikimate (UniProtKB | ChEBI)
Binding site1693-phosphoshikimate (UniProtKB | ChEBI)
Binding site1703-phosphoshikimate (UniProtKB | ChEBI)
Binding site170phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1953-phosphoshikimate (UniProtKB | ChEBI)
Active site310Proton acceptor
Binding site3103-phosphoshikimate (UniProtKB | ChEBI)
Binding site3373-phosphoshikimate (UniProtKB | ChEBI)
Binding site341phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site382phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site407phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site439-444ATP (UniProtKB | ChEBI)
Binding site443Mg2+ (UniProtKB | ChEBI)
Binding site461substrate
Binding site485substrate
Binding site507substrate
Binding site545ATP (UniProtKB | ChEBI)
Binding site565substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionshikimate kinase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • 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

Gene names

    • Name
      aroA
    • Synonyms
      aroK
    • ORF names
      HY417_04350

Organism names

Accessions

  • Primary accession
    A0A932YPR1

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain11-416Enolpyruvate transferase

Sequence similarities

Belongs to the EPSP synthase family.
Belongs to the shikimate kinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    601
  • Mass (Da)
    66,805
  • Last updated
    2023-02-22 v1
  • Checksum
    A54C5921C99044F4
MRRIRITPSSRPVRAIVSVPGSKSYTNRALMLAALTGDTVRVRNPLVADDTHAMIACLRELGFSCVFKGDVLEMRGNLKNVETREHHLNTFLSGMTARFMLALACIVPGVKIIQGRGRLNERPIGHLVDSLRQLGAKIEYINKKGYPPVRVRSSKLRPGTVRMQGTISSQFLSALLMIAPLVGKVEIEVEGEQISRPYIDMTIEAIRAFGVQIRHEGYSRFIVPARQRYFAKRYDIEGDVSSASYFAAIAALTHSTITLKNVNPKSRQADIRFFKILEEMGNRITRSKSSVTIRGSGVRPVSVDMRDCPDQAQTLAVLAAFAEGVTKITGIQSLRVKETERIAALQQELKKMGIRTESTHDSLTIHGGSPRRARIDTYGDHRMAMAFAVAGTKLAGIEINEPDVVSKTFPRFWETLGSIGVGIELSYERPNIVLIGMRGGGKSTVARHLSERLGLRTADLDAIVEKQEGMSIPEIVERYGWEYFRDRESEVVQKVGRLKDTVISTGGGVINRPENIAALKQRGILVFLNAPVERLLSRLEGDTSRPRLTSSSTALSEMKAVLAERKRLYETVADEIIDDTTLTLEEKVEEVVRRLQKRGIV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACQKE010000091
EMBL· GenBank· DDBJ
MBI4094170.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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