P24670 · AROD_SALTI
- Protein3-dehydroquinate dehydratase
- GenearoD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids252 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsilon-amino group of Lys-170 at the active site.
Catalytic activity
- 3-dehydroquinate = 3-dehydroshikimate + H2O
Activity regulation
Inhibited by (2R)-2-methyl-3-dehydroquinic acid.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
24 μM | 3-dehydroquinate | 7.2 | 25 |
kcat is 1.1 sec-1 for dehydratase activity with 3-dehydroquinate (at pH 7.2 and 25 degrees Celsius).
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 46-48 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: EWR | ||||||
Binding site | 82 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 143 | Proton donor/acceptor | ||||
Sequence: H | ||||||
Active site | 170 | Schiff-base intermediate with substrate | ||||
Sequence: K | ||||||
Binding site | 213 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 232 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 236 | 3-dehydroquinate (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3-dehydroquinate dehydratase activity | |
Biological Process | 3,4-dihydroxybenzoate biosynthetic process | |
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
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3-dehydroquinate dehydratase
- EC number
- Short names3-dehydroquinase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP24670
Proteomes
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000138805 | 1-252 | 3-dehydroquinate dehydratase | |||
Sequence: MKTVTVKNLIIGEGMPKIIVSLMGRDINSVKAEALAYREATFDILEWRVDHFMDIASTQSVLTAARVIRDAMPDIPLLFTFRSAKEGGEQTITTQHYLTLNRAAIDSGLVDMIDLELFTGDADVKATVDYAHAHNVYVVMSNHDFHQTPSAEEMVLRLRKMQALGADIPKIAVMPQSKHDVLTLLTATLEMQQHYADRPVITMSMAKEGVISRLAGEVFGSAATFGAVKQASAPGQIAVNDLRSVLMILHNA |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length252
- Mass (Da)27,649
- Last updated2001-12-05 v2
- ChecksumF9D4D4C86D18F17B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 156 | in Ref. 1; CAA38418 | ||||
Sequence: L → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54546 EMBL· GenBank· DDBJ | CAA38418.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL513382 EMBL· GenBank· DDBJ | CAD02002.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014613 EMBL· GenBank· DDBJ | AAO68886.1 EMBL· GenBank· DDBJ | Genomic DNA |