A0A932YPR1 · A0A932YPR1_9BACT
- ProteinMultifunctional fusion protein
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids601 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
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.
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
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 | 94 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 122 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 168 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 169 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 170 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 170 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 195 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 310 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 310 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 337 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 341 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 382 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 407 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 439-444 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GGGKST | ||||||
Binding site | 443 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 461 | substrate | ||||
Sequence: D | ||||||
Binding site | 485 | substrate | ||||
Sequence: R | ||||||
Binding site | 507 | substrate | ||||
Sequence: G | ||||||
Binding site | 545 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 565 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | shikimate kinase 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
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
- Recommended nameShikimate kinase
- EC number
- Short namesSK
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Candidatus Kaiserbacteria
Accessions
- Primary accessionA0A932YPR1
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-416 | Enolpyruvate transferase | ||||
Sequence: RPVRAIVSVPGSKSYTNRALMLAALTGDTVRVRNPLVADDTHAMIACLRELGFSCVFKGDVLEMRGNLKNVETREHHLNTFLSGMTARFMLALACIVPGVKIIQGRGRLNERPIGHLVDSLRQLGAKIEYINKKGYPPVRVRSSKLRPGTVRMQGTISSQFLSALLMIAPLVGKVEIEVEGEQISRPYIDMTIEAIRAFGVQIRHEGYSRFIVPARQRYFAKRYDIEGDVSSASYFAAIAALTHSTITLKNVNPKSRQADIRFFKILEEMGNRITRSKSSVTIRGSGVRPVSVDMRDCPDQAQTLAVLAAFAEGVTKITGIQSLRVKETERIAALQQELKKMGIRTESTHDSLTIHGGSPRRARIDTYGDHRMAMAFAVAGTKLAGIEINEPDVVSKTFPRFWETL |
Sequence similarities
Belongs to the EPSP synthase family.
Belongs to the shikimate kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length601
- Mass (Da)66,805
- Last updated2023-02-22 v1
- ChecksumA54C5921C99044F4