Q9S400 · AROA_STRPN

Function

function

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.

Catalytic activity

Activity regulation

Competitively inhibited by glyphosate. Activated by ammonium, rubidium or potassium ions.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
22 μMPEP725with 100 mM ammonium
31 μMS3P725with 100 mM ammonium
91 μMPEP725with 10 mM ammonium
100 μMPEP725with 1 mM ammonium
118 μMS3P725with 10 mM ammonium
145 μMS3P725with 1 mM ammonium

Pathway

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 site20phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site213-phosphoshikimate (UniProtKB | ChEBI)
Binding site253-phosphoshikimate (UniProtKB | ChEBI)
Binding site92phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site120phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1663-phosphoshikimate (UniProtKB | ChEBI)
Binding site1673-phosphoshikimate (UniProtKB | ChEBI)
Binding site1683-phosphoshikimate (UniProtKB | ChEBI)
Binding site168phosphoenolpyruvate (UniProtKB | ChEBI)
Active site312Proton acceptor
Binding site3123-phosphoshikimate (UniProtKB | ChEBI)
Binding site3393-phosphoshikimate (UniProtKB | ChEBI)
Binding site343phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site385phosphoenolpyruvate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3-phosphoshikimate 1-carboxyvinyltransferase
  • EC number
  • Alternative names
    • 5-enolpyruvylshikimate-3-phosphate synthase
      (EPSP synthase
      ; EPSPS
      )

Gene names

    • Name
      aroA
    • Ordered locus names
      SP_1371

Organism names

Accessions

  • Primary accession
    Q9S400

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Chemistry

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000883041-4273-phosphoshikimate 1-carboxyvinyltransferase

Proteomic databases

Interaction

Subunit

Homotetramer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9S400eno Q97QS22EBI-2207276, EBI-2207206
BINARY Q9S400gatC Q97SE52EBI-2207276, EBI-2207053
BINARY Q9S400groES Q97NV32EBI-2207276, EBI-2206949

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the EPSP synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    45,766
  • Last updated
    2001-09-26 v2
  • Checksum
    45CE6F4D0D1C7B70
MKLKTNIRHLHGSIRVPGDKSISHRSIIFGSLAEGETKVYDILRGEDVLSTMQVFRDLGVEIEDKDGVITIQGVGMAGLKAPQNALNMGNSGTSIRLISGVLAGADFEVEMFGDDSLSKRPMDRVTLPLKKMGVSISGQTERDLPPLRLKGTKNLRPIHYELPIASAQVKSALMFAALQAKGESVIIEKEYTRNHTEDMLKQFGGHLSVDGKKITVQGPQKLTGQKVVVPGDISSAAFWLVAGLIAPNSRLVLQNVGINETRTGIIDVIRAMGGKLEITEIDPVAKSATLIVESSDLKGTEIGGALIPRLIDELPIIALLATQAQGVTVIKDAEELKVKETDRIQVVADALNSMGADITPTADGMIIKGKSALHGARVNTFGDHRIGMMTAIAALLVADGEVELDRAEAINTSYPSFFDDLESLIHG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict13in Ref. 1; AAD45819
Sequence conflict71in Ref. 1; AAD45819
Sequence conflict201in Ref. 1; AAD45819
Sequence conflict303in Ref. 1; AAD45819

Mass Spectrometry

Molecular mass is 45,825 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF169483
EMBL· GenBank· DDBJ
AAD45819.1
EMBL· GenBank· DDBJ
Genomic DNA
AE005672
EMBL· GenBank· DDBJ
AAK75469.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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