A0A154BVI5 · A0A154BVI5_ANASB
- ProteinMultifunctional fusion protein
- GenearoE
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids433 (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.
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Catalytic activity
- shikimate + ATP = 3-phosphoshikimate + ADP + H+
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 14-16 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: SIS | ||||||
Binding site | 61 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Active site | 65 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 77 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 86 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 101 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 206 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 208 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 229 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 236 | shikimate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 278-283 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSGKST | ||||||
Binding site | 282 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 300 | substrate | ||||
Sequence: D | ||||||
Binding site | 324 | substrate | ||||
Sequence: R | ||||||
Binding site | 346 | substrate | ||||
Sequence: G | ||||||
Binding site | 382 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 399 | substrate | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | NADP binding | |
Molecular Function | shikimate 3-dehydrogenase (NADP+) activity | |
Molecular Function | shikimate kinase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | shikimate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameShikimate kinase
- EC number
- Short namesSK
- Recommended nameShikimate dehydrogenase (NADP(+))
- EC number
- Short namesSDH
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Negativicutes > Selenomonadales > Sporomusaceae > Anaerosporomusa
Accessions
- Primary accessionA0A154BVI5
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-88 | Shikimate dehydrogenase substrate binding N-terminal | ||||
Sequence: LLGETLSHSISPEIHGFLFRQLNIEASYSLFPVPPDKLADALYGLILLGSGGVNVTIPYKMKIIPLLDELTDEARALGAVNTV |
Sequence similarities
Belongs to the shikimate dehydrogenase family.
Belongs to the shikimate kinase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length433
- Mass (Da)47,969
- Last updated2016-06-08 v1
- Checksum5BBE06EF08CB5F54
Keywords
- Technical term