A0A7M2JGR7 · A0A7M2JGR7_PSEFL
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids736 (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 | 322 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 322 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 323 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 327 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 395 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 423 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 468 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 470 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 470 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Active site | 616 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 616 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 643 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 647 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 688 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Molecular Function | NAD+ binding | |
Molecular Function | prephenate dehydrogenase (NAD+) activity | |
Molecular Function | prephenate dehydrogenase (NADP+) activity | |
Biological Process | chorismate biosynthetic process | |
Biological Process | tyrosine 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 > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionA0A7M2JGR7
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-291 | Prephenate/arogenate dehydrogenase | ||||
Sequence: GRLVVVGLGLIGGSFAKGLRESGLCGEVVGVDLDPQSRKLAVELGVVDRCEADLALACQGADVIQLAVPILAMEKLLALLAGMDLGQAILTDVGSAKGNVVRAAQQAFGGMPSRFVPGHPIAGSEQSGVEASNAQLFRRHKVILTPLEQTDPAALAVVDRLWRELGADVEHMQVERHDEVLAATSHLPHLLAFGLVDSLAKRNENLEIFRYAAGGFRDFTRIAGSDPVMWHDIFLANREAVLRTLDTFRSDLDALRDAVDAGDGHQLLGVFTRARVAREHFSKILARRA |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length736
- Mass (Da)77,942
- Last updated2021-06-02 v1
- Checksum819FC7D18D41BF51