A0A3B9P0Y3 · A0A3B9P0Y3_9PROT

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 site253-phosphoshikimate (UniProtKB | ChEBI)
Binding site25phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site263-phosphoshikimate (UniProtKB | ChEBI)
Binding site303-phosphoshikimate (UniProtKB | ChEBI)
Binding site97phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site125phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1713-phosphoshikimate (UniProtKB | ChEBI)
Binding site1723-phosphoshikimate (UniProtKB | ChEBI)
Binding site1733-phosphoshikimate (UniProtKB | ChEBI)
Binding site173phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site1993-phosphoshikimate (UniProtKB | ChEBI)
Active site316Proton acceptor
Binding site3163-phosphoshikimate (UniProtKB | ChEBI)
Binding site3433-phosphoshikimate (UniProtKB | ChEBI)
Binding site347phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site389phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site414phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site437-445ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function3-phosphoshikimate 1-carboxyvinyltransferase activity
Molecular FunctionATP binding
Molecular FunctionCMP kinase activity
Molecular FunctiondCMP kinase activity
Biological Processamino acid biosynthetic process
Biological Processaromatic amino acid family biosynthetic process
Biological Processchorismate biosynthetic process
Biological Processphosphorylation
Biological Processpyrimidine nucleotide metabolic process

Keywords

Enzyme and pathway databases

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
    Cytidylate kinase
  • EC number
  • Short names
    CK
  • Alternative names
    • Cytidine monophosphate kinase
      (CMP kinase
      )

Gene names

    • Name
      cmk
    • Synonyms
      aroA
    • ORF names
      DCK83_11095

Organism names

  • Taxonomic identifier
  • Strain
    • UBA12482
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Nitrosomonadales > Gallionellaceae

Accessions

  • Primary accession
    A0A3B9P0Y3

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain16-421Enolpyruvate transferase
Domain433-641Cytidylate kinase

Sequence similarities

Belongs to the EPSP synthase family.
Belongs to the cytidylate kinase family. Type 1 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    647
  • Mass (Da)
    69,134
  • Last updated
    2019-01-16 v1
  • Checksum
    093FC8FE82EA0EE8
MTQHESLELPPLMSAHGSVRLPGSKSISNRVLLLAALAQGTTTVRDLLHSDDTERMLDALRTLGVQVESLGDNAYRVTGCGGNFPVKQAKLFLGNAGTAFRPLTAALALSGGSYELSGVPRMHERPIGDLVDALRQLGADIKYLGNEGFPPLQISPAKLAGDTAQVRGDVSSQFLTGLLMALPLLDRTVKVEVVGELISKPYIEITLAMMARFGVVVQRDGWRSFTVDAGSRYVSPKEIFVEGDASSASYFLAAGAIGGGPLRVEGVGKTSVQGDVRFAEALQKMGAVITMGDNWIEAKASGRLKAIDLDCNHIPDAAMTLAVAALFADGTTTLRNIASWRVKETDRIAAMATELRKVGATVEEGADFIRVTPPAQVKHAAIDTYDDHRMAMCFSLAAFGGAGVRINDPKCVAKTFPDYFDMFKQVTQTVPVIAIDGPSASGKGTVAQRVATALGMHYLDSGALYRLLGLAAQKRGIALEAEDRLAELAGQVDIRFEGADIWLDGAKVGDELRTEEAGSAASKIAALPKVRAALLDKQRAFRQAPGLVADGRDMASVVFPDSVLKIFLTASAEARAERRYKQLKEKGMSANIAALLQDIKARDERDTQRSVAPLQQAQGASLLDTTPLNIEQAVQEVLSRYRAITSK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DMCN01000098
EMBL· GenBank· DDBJ
HAF45450.1
EMBL· GenBank· DDBJ
Genomic DNA

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