A0AAQ0NM45 · A0AAQ0NM45_9PSED

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 site363-phosphoshikimate (UniProtKB | ChEBI)
Binding site36phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site373-phosphoshikimate (UniProtKB | ChEBI)
Binding site413-phosphoshikimate (UniProtKB | ChEBI)
Binding site107phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site135phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1803-phosphoshikimate (UniProtKB | ChEBI)
Binding site1813-phosphoshikimate (UniProtKB | ChEBI)
Binding site1823-phosphoshikimate (UniProtKB | ChEBI)
Binding site182phosphoenolpyruvate (UniProtKB | ChEBI)
Active site307Proton acceptor
Binding site3073-phosphoshikimate (UniProtKB | ChEBI)
Binding site3303-phosphoshikimate (UniProtKB | ChEBI)
Binding site3343-phosphoshikimate (UniProtKB | ChEBI)
Binding site338phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site385phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site410phosphoenolpyruvate (UniProtKB | ChEBI)

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
      ALP55_100520

Organism names

  • Taxonomic identifier
  • Strain
    • ICMP 9091
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas > Pseudomonas coronafaciens

Accessions

  • Primary accession
    A0AAQ0NM45

Proteomes

Subcellular Location

Cytoplasm

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain25-273Enolpyruvate transferase
Domain301-419Enolpyruvate transferase

Sequence similarities

Belongs to the EPSP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    44,719
  • Last updated
    2024-10-02 v1
  • MD5 Checksum
    7F9A5C0D5CC27DDD3DF9868BC2AE97B7
MVFPLTFRDIMRPQATLTVLPVERPLVGRVSPPGSKSITNRALLLAGLAQGTSRLTGALKSDDTRVMSEALRLMGVQVDEPDESTFVVTSNGHWNAPQQALFLGNAGTATRFLTAALANFEGDFVVDGDEYMRKRPIGPLVDALQRMGVDVSAPSGCPPVAISGKGGLAAGRIEIDGNLSSQYVSALLMAGACGKGAIEVALTGSEIGARGYVDLTLAAMQAFGAEVQAIGDSAWKVSATGYRATDFHIEPDASAATYLWAAQALTQGSIDLGVASDAFTQPDALASQIIDLFPNMPAVIDGSQMQDAIPTLAVLAAFNRQPVRFVGIANLRVKECDRISALSQGLCAIAPGLAVEEGDDLLVNANPALAGTTVDALIDTHADHRIAMCFALAGLKIKGIHIQDPDCVGKTYPGYWDALASLGVSIQL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
RBTA01000066
EMBL· GenBank· DDBJ
RMT07913.1
EMBL· GenBank· DDBJ
Genomic DNA

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