A0A7C4PLQ9 · A0A7C4PLQ9_9CHLR
- ProteinMultifunctional fusion protein
- GenearoB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids557 (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 | 49-54 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GSGKST | ||||||
Binding site | 53 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 71 | substrate | ||||
Sequence: D | ||||||
Binding site | 95 | substrate | ||||
Sequence: R | ||||||
Binding site | 117 | substrate | ||||
Sequence: G | ||||||
Binding site | 156 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 176 | substrate | ||||
Sequence: R | ||||||
Binding site | 310-314 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GVVGD | ||||||
Binding site | 334-335 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 347 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 356 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 374-377 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TLST | ||||||
Binding site | 389 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 448 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 464 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-dehydroquinate synthase activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
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 > Chloroflexota > Anaerolineae > Anaerolineales > Anaerolineaceae > Anaerolinea
Accessions
- Primary accessionA0A7C4PLQ9
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-159 | AAA+ ATPase | ||||
Sequence: SETLYFIYGPPGSGKSTLARRLAGLLDLPFMDLDEQIQASAGMPIPAIFDREGERGFRQRERVALEAALQSGRGVVALGGGALLDPTSRSLVESAGRVLCLRAERETLFERLGQEVGTRPLL |
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
- Length557
- Mass (Da)59,539
- Last updated2020-12-02 v1
- Checksum3BE6C12EF5E4DE63