A0A2D3D6C6 · A0A2D3D6C6_9BIFI
- ProteinMultifunctional fusion protein
- GenearoB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids552 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic activity
- 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Cofactor
Protein has several cofactor binding sites:
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Binds 1 divalent metal cation per subunit. Can use either Co2+ or Zn2+.
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 24-29 | ATP (UniProtKB | ChEBI) | |||
Binding site | 28 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 46 | substrate | |||
Binding site | 70 | substrate | |||
Binding site | 92 | substrate | |||
Binding site | 134 | ATP (UniProtKB | ChEBI) | |||
Binding site | 152 | substrate | |||
Binding site | 253-258 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 287-291 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 311-312 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 324 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 333 | NAD+ (UniProtKB | ChEBI) | |||
Binding site | 366 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 438 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 454 | Zn2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-dehydroquinate synthase 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 | |
Biological Process | phosphorylation |
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 name3-dehydroquinate synthase
- EC number
- Short namesDHQS
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Bifidobacteriales > Bifidobacteriaceae > Bifidobacterium
Accessions
- Primary accessionA0A2D3D6C6
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 249-514 | 3-dehydroquinate synthase | |||
Sequence similarities
Belongs to the shikimate kinase family.
Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length552
- Mass (Da)60,267
- Last updated2018-01-31 v1
- MD5 Checksum27F688BB6CC48123388D420F926BFD54
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP018044 EMBL· GenBank· DDBJ | ATU20658.1 EMBL· GenBank· DDBJ | Genomic DNA |