A0A6F8TUH6 · A0A6F8TUH6_9BACI
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids432 (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 | 24 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 24 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 25 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 29 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 96 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 124 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 169 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 171 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 171 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 316 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 316 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 343 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 347 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 389 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionA0A6F8TUH6
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-423 | Enolpyruvate transferase | ||||
Sequence: PKRGLKGKLEVPGDKSISHRSIMFGSIAEGKTVIHNFLMGEDCLSTISCFRKLGVDIDVSEDEVVVHGKGWDHLKEPKDILDVGNSGTTTRLIMGILAGRPFHSVLIGDDSIAKRPMNRVTIPLRQFGTNIDGRSEGNYTPLSVRGGNLKAIRYSLPVASAQVKSAILLAGLQAEGTTEIVEPEKTRNHTEKMIVEFGGSVEREGDTIKVKGGQVFKGTDIYVPGDISSAAFFMVAAAIVPGSSVRLKNVGLNETRIGIIEVMKKMGAAIEVIEHTKSGEPIGDIVVQSSELTGIEIGGELIPSLIDEIPVIALLASQANGKTVIKDAEELKVKETNRIDAVVKELGKLGADIEGTDDGMIIHGKTELHGGEVHSWGDHRIGMTLAVASLLTDSDVYLDGSEAVKISYPQFFDH |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length432
- Mass (Da)46,447
- Last updated2020-08-12 v1
- ChecksumED1D75B3B883E5E6