UniProt functional annotation for Q186A6



	UniProt functional annotation for Q186A6

UniProt code: Q186A6.

Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile).

Taxonomy: Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae; Clostridioides.

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 epsylon-amino group of Lys-170 at the active site. {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925}.

Catalytic activity: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP- Rule:MF_00214, ECO:0000269|PubMed:21087925};

Biophysicochemical properties: Kinetic parameters: KM=36 uM for 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:21087925}; Note=Kcat is 125 sec(-1) for dehydratase activity with 3- dehydroquinate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269|PubMed:21087925};

Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}.

Subunit: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:21087925, ECO:0000269|Ref.3}.

Similarity: Belongs to the type-I 3-dehydroquinase family. {ECO:0000255|HAMAP-Rule:MF_00214}.

Annotations taken from UniProtKB at the EBI.


Organism:		Clostridioides difficile (strain 630) (Peptoclostridium difficile).
Taxonomy:		Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae; Clostridioides.



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 epsylon-amino group of Lys-170 at the active site. {ECO:0000255\|HAMAP-Rule:MF_00214, ECO:0000269\|PubMed:21087925}.


Catalytic activity:		Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255\|HAMAP- Rule:MF_00214, ECO:0000269\|PubMed:21087925};
Biophysicochemical properties:		Kinetic parameters: KM=36 uM for 3-dehydroquinate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269\|PubMed:21087925}; Note=Kcat is 125 sec(-1) for dehydratase activity with 3- dehydroquinate (at pH 7.5 and 37 degrees Celsius). {ECO:0000269\|PubMed:21087925};
Pathway:		Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255\|HAMAP-Rule:MF_00214}.
Subunit:		Homodimer or homotetramer. {ECO:0000255\|HAMAP-Rule:MF_00214, ECO:0000269\|PubMed:21087925, ECO:0000269\|Ref.3}.
Similarity:		Belongs to the type-I 3-dehydroquinase family. {ECO:0000255\|HAMAP-Rule:MF_00214}.