Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A0A094YUV8 · A0A094YUV8_9PROT

  • Protein
    3-phosphoshikimate 1-carboxyvinyltransferase
  • Gene
    aroA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

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

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.

Type
IDPosition(s)Description
Binding site323-phosphoshikimate (UniProtKB | ChEBI)
Binding site32phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site333-phosphoshikimate (UniProtKB | ChEBI)
Binding site373-phosphoshikimate (UniProtKB | ChEBI)
Binding site105phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site133phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1783-phosphoshikimate (UniProtKB | ChEBI)
Binding site1803-phosphoshikimate (UniProtKB | ChEBI)
Binding site180phosphoenolpyruvate (UniProtKB | ChEBI)
Active site331Proton acceptor
Binding site3313-phosphoshikimate (UniProtKB | ChEBI)
Binding site3583-phosphoshikimate (UniProtKB | ChEBI)
Binding site362phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site406phosphoenolpyruvate (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
    • ORF names
      AtDm6_1112

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DmCS_006
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae > Acetobacter

Accessions

  • Primary accession
    A0A094YUV8

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain18-439Enolpyruvate transferase

Sequence similarities

Belongs to the EPSP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    450
  • Mass (Da)
    47,237
  • Last updated
    2014-11-26 v1
  • MD5 Checksum
    E9E30142C5C12F3C5CBEC71DEF32A151
MGMTQAPSSSRPLRVTRAPAPLAGTVVVPGDKSISHRALMFSALAEGETRIIGLLEGEDVLRTADAMRALGAHITRDENGRWHVRGRGLGALTEPSDVLDMGNSGTAARLLSGILASHGMMSVMTGDASLRRRPMKRVTDPLAGTGATFLAREGGRLPLAIQGNATPAPLDYRLPVASAQVKSAVLLAGLNAAGETRVEEPVPTRDHTENMLRHFGAQVAVEETPEGGRIIRLQGKPHLIARDVTVPGDPSSAAFVLVAALLVAGSDVVISNVGLNPLRTGLFTTLREMGARLDITNERTEGGEPVGDLHVQASSLQAVDVPAERAPSMIDEYPILAVAAAFATGISRFRGVEELRVKESDRLASTVALLEKNGVRTKVDGDDLIIYGTQGAIPGGGTVETHMDHRLAMSASILGLVAENPVEIDDTAFIDTSFPGYFPLLNSLGAGFAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JOKM01000038
EMBL· GenBank· DDBJ
KGB24404.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help