A0A1S2N303 · A0A1S2N303_9MICC
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids437 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphateThis reaction proceeds in the forward direction.
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 | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 26 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 27 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 31 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 97 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 125 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 172 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 173 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 174 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 174 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 201 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 322 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 322 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 349 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 353 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 394 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 419 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micrococcales > Micrococcaceae > Rothia
Accessions
- Primary accessionA0A1S2N303
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-425 | Enolpyruvate transferase | ||||
Sequence: RPVHAVVAVPGSKSLTNRHLLLAAVADAPMRIRGALDSRDSRLMIEALRALGARIRTQGRDLLITPVPEEPSDEPAVIDAGLAGTVMRFIPPLAAALGRGIVLDGDAAARRRPMGPVLEAVRQLGARVHEDGEAGALPVRIEPGAGEAAPELRIDASGSSQFLSGVLLAAALLPQGLTVRHVGAELPSVPHVRMTVQVLAEYGIDVAHPDPATWVVPAGRPRAHDAVIEPDLSNAGPFLAAAVVTGGEVQIPDWPQRTTQGGDTWRELLPRFGASVHRTPDGGLRVTGPEGGAGALTAPGEIDLRAAGEIAPTVAAIAALCPGTTRLSGIAHLRGHETDRLAALAAELTRLGARTEETDDGLVITGPAHRAARMRTYEDHRIATAAAVLGLIVPGVLVEDIGTTGKTLPDFP |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)45,681
- Last updated2017-04-12 v1
- ChecksumE2482C7864BD0F4F