A0AAE4ZIA4 · A0AAE4ZIA4_RHOHA
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids449 (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 | 32 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 32 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 33 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 37 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 104 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 132 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 175 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 176 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 177 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 177 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 204 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 323 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 323 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 350 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 354 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 395 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 420 | 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
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Prescottella
Accessions
- Primary accessionA0AAE4ZIA4
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 18-427 | Enolpyruvate transferase | ||||
Sequence: AEAPVDASVTLPGSKSITNRALILAALASGPSTITGALRSRDTDLMIQGLRALGVAITATPDAATGTTLHVVPGPMTGAAVDCGLAGTVMRFLPPAAALAEGTVAVDGDEQARTRPLGTILDALRGLGADIDGDALPFTVHGHGGLRGGTVTIDASGSSQFVSGLLLSAARFDEGVTVRHQGGSLPSMPHIDMTVEMLREAGVTVHTPGESGDADTWKVLPGKIDPVDWVVEPDLSNATPFLAAAAVTGGTVRVPLWPSRTTQPGDAIRGILAEMGADVRLEEGVLSVTGPETLRGIDIDLHDIGELTPTVAALAALADGPSVLRGIAHLRGHETDRLAALATEIGKLGGAVTETADGLRIEPRPLHGAQWHSYADHRMATAGAILGLVVDGVDIEDVGTTAKTLPGFEN |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)46,196
- Last updated2024-05-29 v1
- ChecksumB1AF1E70DB3501BA