AC   MF_00214;
DC   Protein; auto
TR   HAMAP; MF_00214; -; 1; level=0
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Names: AroD
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ID   AROD
DE   RecName: Full=3-dehydroquinate dehydratase;
DE            Short=3-dehydroquinase;
DE            EC=4.2.1.10;
DE   AltName: Full=Type I dehydroquinase;
DE            Short=DHQ1;
DE   AltName: Full=Type I DHQase;
GN   Name=aroD;
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CC   -!- FUNCTION: Involved in the third step of the chorismate pathway, which
CC       leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-
CC       dehydration of 3-dehydroquinate (DHQ) and introduces the first double
CC       bond of the aromatic ring to yield 3-dehydroshikimate.
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: Homodimer.
CC   -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family.
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DR   Pfam; PF01487; DHquinase_I; 1; trigger=no
DR   NCBIfam; TIGR01093; AroD; 1; trigger=no
DR   PROSITE; PS01028; DEHYDROQUINASE_I; 1; trigger=no
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KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   Lyase
KW   Schiff base
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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: AROD_SALTY (P58687)
FT   BINDING         46..48
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: E-x-R
FT   ACT_SITE        143
FT                   /note="Proton donor/acceptor"
FT   Condition: H
FT   ACT_SITE        170
FT                   /note="Schiff-base intermediate with substrate"
FT   Condition: K
FT   BINDING         21
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: S
FT   BINDING         82
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: R
FT   BINDING         213
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: R
FT   BINDING         232
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: [ST]
FT   BINDING         236
FT                   /ligand="3-dehydroquinate"
FT                   /ligand_id="ChEBI:CHEBI:32364"
FT   Optional; Condition: Q
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Size: 196-272;
Related: MF_03143!;
Template: P05194; P24670; P58687; Q186A6; Q6GII7; O30011;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: MF_00222 (aroE); <Chorismate mutase>
Duplicate: None
Plasmid: None
Comments: There are two type of DHQases, B.subtilis seems to have both.
 AroD can be confused with of DHQases involved in catabolism (quiB) or in
 other pathways (example ebsD).
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# Revision 1.41 2023/06/01
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