A0A0A1H7F6 · A0A0A1H7F6_9BURK
- ProteinMultifunctional fusion protein
- GenearoA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids698 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 20 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 20 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 21 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 25 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 91 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 119 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 167 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 168 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 169 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 169 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 200 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 324 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 324 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 351 | 3-phosphoshikimate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 355 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 422 | phosphoenolpyruvate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 483-491 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GPTASGKGA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | CMP kinase activity | |
Molecular Function | dCMP kinase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | pyrimidine nucleotide metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
- Recommended nameCytidylate kinase
- EC number
- Short namesCK
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales
Accessions
- Primary accessionA0A0A1H7F6
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-431 | Enolpyruvate transferase | ||||
Sequence: EPIARAAGEVRLPGSKSISNRALLLAALAQGATELSGVLDADDTRVMIAALRTLGVAVEVDGDRVRVAGCGGDFPNREADLFLGNAGTAMRPLAAVLAFAGGRYRLDGVARMRERPIGDLVDAVNGMGARVRYAGTPGYPPLQVEPADRGKLVPRVRVRGAVSSQFVTGLLLAAPGYARATAWRSLTIEIDGNLISQPYVAMTIAMMRQFGADVRAPLPGTYVVGPDAYCAPTGRYAVEGDASGASYFLALGAIAGGPVRVRGVGRDSLQGDVAFTTVLEKMGARVAIGDDWIETAGGGTGVDGRFVLQPVDWDCSEIPDAAMTVAVLALFARGTTRLRGIGSWRVKETDRIHAMATELTKLGAEVEFGDDWIAVTAPEQVREAWIDTYDDHRMAMCLSLAAAAGVPVHVRDPGCVAKTYPDYFDRL | ||||||
Domain | 479-693 | Cytidylate kinase | ||||
Sequence: IAIDGPTASGKGAVAQRVAQELGFACLDSGALYRIVGLLALEQGVGLDDGPALAAVADALTAAEDPAMRLRFADGRITLGARDITEAIRREEVGRAASRIATAGELRTALLALQRAQRRPPGLVADGRDMGTVVFPDASLKVFLIADVRVRAERRYKQLIEKGYPGTLETLLQDLEERDARDRTRDHAPLVAAEGAKILDSTAMTIDAVVAQVLG |
Sequence similarities
Belongs to the EPSP synthase family.
Belongs to the cytidylate kinase family. Type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length698
- Mass (Da)73,567
- Last updated2015-02-04 v1
- ChecksumF2F02F239BC542D1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP014683 EMBL· GenBank· DDBJ | BAP89189.1 EMBL· GenBank· DDBJ | Genomic DNA |