Q3I1Q0 · Q3I1Q0_NOSCO
- Protein3-phosphoshikimate 1-carboxyvinyltransferase
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids403 (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 | 23 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 23 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 24 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 28 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 96 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 124 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 170 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 171 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 172 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 172 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 198 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 314 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 314 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 341 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 345 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 386 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | 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
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Nostocaceae > Nostoc
Accessions
- Primary accessionQ3I1Q0
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-402 | Enolpyruvate transferase | ||||
Sequence: RPVDATVEIPGSKSLTNRALLVAALAQGDSLLENALFSEDSEYFAKCVEQLGIPITLNPDLAQIRVAGRGGDIPAKQADLFVGLAGTAARFISALVALGNGEYRLDGVPRMRERPMGDLLTVLQTGGATVNFEGNSGFMPYTVYSQGFTGGNFRLKANQTSQQLSALLMIAPYAQQDTNIEVEGTLVSQSYVKMTCRLMADFGVEVIQIGDNQFQIKAGQRYQARHYTVEPDASNASYFFAAAAVTGGRVRVKHLTKQSCQGDILWLNVLEQMGCQIKDSDDYTEVTGPKQLQGIDIDMNDISDLVQTLGAIAPFASSTITIRNVEHIRYKETDRIKAVVTELRRLGVQVEEFPDQLKIEPGPVTPAAIETYHDHRMAMAFAVTGLKVPGIV |
Sequence similarities
Belongs to the EPSP synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)43,790
- Last updated2005-11-08 v1
- Checksum3A548490F6239AF6