Q0S2X1 · AROA_RHOJR
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids438 (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 | 28 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 28 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 29 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 33 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 97 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 125 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 168 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 169 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 170 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 170 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 316 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 316 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 343 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 347 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 388 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 413 | 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 > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionQ0S2X1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000325378 | 1-438 | 3-phosphoshikimate 1-carboxyvinyltransferase | |||
Sequence: METVSLSLWNAPRAEAPVVATVALPGSKSITNRALILAALADGPSTLTGALRSRDTDLMIEALRTLGISIETVGADTTLRVTPGPLQGGAVDCGLAGTVMRFLPPVAALASGTVHFDGDEQARTRPLDTILDALRGLGADIDGASLPFTVRGAGSLRGGRVTIDASGSSQFVSGLLLSAAAFDEGVTVHHDGKTVPSMPHIDMTVEMLRESGVEVTTPATGGEADTWRVSPGVVRAVDRAIEPDLSNATAFLAAAAVTGGEVTVPLWPSRTTQPGDAIREILLAMGADVRLDGANLTVRGPQQLTGIDIDLHDVGELTPTVAALAALADGPSHLRGIAHLRGHETDRLAALAHEINSLGGNVTETEDGLTIVPAGLHGGTWRSYADHRMATAGAIVGLRVDGIRIEDVGTTAKTLPGFENLWATMLSAAAGTERKASF |
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length438
- Mass (Da)45,110
- Last updated2006-09-05 v1
- Checksum01626E54D413E88B
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000431 EMBL· GenBank· DDBJ | ABG98115.1 EMBL· GenBank· DDBJ | Genomic DNA |