A0A8B6X6F9 · A0A8B6X6F9_9BURK
- ProteinChorismate synthase
- GenearoC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids358 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
Catalytic activity
- 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Cofactor
Note: Reduced FMN (FMNH2).
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 48 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 54 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 125-127 | FMN (UniProtKB | ChEBI) | ||||
Sequence: RSS | ||||||
Binding site | 238-239 | FMN (UniProtKB | ChEBI) | ||||
Sequence: NA | ||||||
Binding site | 278 | FMN (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 293-297 | FMN (UniProtKB | ChEBI) | ||||
Sequence: KPTSS | ||||||
Binding site | 319 | FMN (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | chorismate synthase 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
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChorismate synthase
- EC number
- Short namesCS
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Derxia
Accessions
- Primary accessionA0A8B6X6F9
Proteomes
Interaction
Subunit
Homotetramer.
Structure
Sequence
- Sequence statusComplete
- Length358
- Mass (Da)38,035
- Last updated2022-01-19 v1
- ChecksumA882865599D9CA1E
Keywords
- Technical term