AC   MF_00169;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00169; -; 1; level=0
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Names: AroQ
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ID   AROQ
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type II DHQase;
GN   Name=aroQ;
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CC   -!- FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC         Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:32364; EC=4.2.1.10;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       3/7.
CC   -!- SUBUNIT: Homododecamer.
CC   -!- SIMILARITY: Belongs to the type-II 3-dehydroquinase family.
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DR   Pfam; PF01220; DHquinase_II; 1; trigger=no
DR   NCBIfam; TIGR01088; AroQ; 1; trigger=no
DR   PROSITE; PS01029; DEHYDROQUINASE_II; 1; trigger=no
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KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   Lyase
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GO   GO:0003855; F:3-dehydroquinate dehydratase activity
GO   GO:0009073; P:aromatic amino acid family biosynthetic process
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FT   From: AROQ_STRCO (P15474)
FT   BINDING         108..109
FT                   /ligand="substrate"
FT   Condition: [LIVM]-[ST]
FT   ACT_SITE        29
FT                   /note="Proton acceptor"
FT   Condition: Y
FT   ACT_SITE        107
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         80
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         86
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         93
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         118
FT                   /ligand="substrate"
FT   Condition: R
FT   SITE            24
FT                   /note="Transition state stabilizer"
FT   Condition: R
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Size: 143-170;
Related: None;
Template: P15474; Q48255; P9WPX7; P46380; P54517; P43877;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in AGRFC, BRADU, COREF, PSEAE, PSEPK, RALN1
Plasmid: in RALN1
Comments: There are two type of DHQases, B.subtilis seems to have both
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# Revision 1.37 2023/11/28
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