A0A3R7VN87 · A0A3R7VN87_9PROT
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids447 (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 | 27 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 27 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 28 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 32 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 101 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 130 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 174 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 176 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 176 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 325 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 325 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 352 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 356 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 402 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Candidatus Pelagibacterales > Candidatus Pelagibacteraceae > Candidatus Pelagibacter
Accessions
- Primary accessionA0A3R7VN87
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 13-437 | Enolpyruvate transferase | ||||
Sequence: KIKSFNKTIEVDSDKSLSIRSFLIGSISNNISIAKNILESEDVKSTITACKKLGVKIERIKPKCYKIYGKGLGGFYAKKNTTLNFGNSGTLARLLTGILSTTPNIQIKVSGDHSLNKRSMKKLINLMTKFGTIFLPKNKYTFPLKLISSKMPIGIKYNAGVSAQLKSAVILAGLNSYGETSIFEQVFSRDHTENILKKNINAIKIKKNKKKIIKVFGKKNLKQININVSGDPSSAAFFATLALLNPNSSIRIKNVGLNPSRTGFYKILKKQKAKLKFVNLKKENNEVSGDILVKNCKLKPLKTPASMYPSTTDEYLLLFLIAALQKGISVFKGISDLANKESSRAYEMKKILNQLGIQCKLIKDEMKIYGKGMIDASDKKINVGNLGDHRVAMCAFLLGVLTNATTNIKNFETVFTSSPSFLKVM |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length447
- Mass (Da)49,563
- Last updated2019-04-10 v1
- Checksum2B51B6E84D06B34E