AC   MF_00222;
DC   Protein; auto
TR   HAMAP; MF_00222; -; 1; level=0
XX
Names: Shikimate_DH_AroE
XX
ID   AROE
DE   RecName: Full=Shikimate dehydrogenase (NADP(+));
DE            Short=SDH;
DE            EC=1.1.1.25;
GN   Name=aroE;
XX
CC   -!- FUNCTION: Involved in the biosynthesis of the chorismate, which leads
CC       to the biosynthesis of aromatic amino acids. Catalyzes the reversible
CC       NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate
CC       (SA).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       4/7.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
XX
DR   Pfam; PF01488; Shikimate_DH; 1; trigger=no
DR   Pfam; PF08501; Shikimate_dh_N; 1; trigger=no
DR   NCBIfam; TIGR00507; AroE; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   NADP
KW   Oxidoreductase
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GO   GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity
GO   GO:0009073; P:aromatic amino acid family biosynthetic process
XX
FT   From: AROE_AQUAE (O67049)
FT   BINDING         130..134
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: G-[AGNSVY]-G-G-[AISV]
FT   BINDING         153..158
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: N-R-T-x(2)-[KR]
FT   BINDING         19..21
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: [ST]-x-[ST]
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT   Condition: K
FT   BINDING         82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [DE]
FT   BINDING         66
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: [TS]
FT   BINDING         91
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: N
FT   BINDING         106
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: D
FT   BINDING         214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: [IVMLCATFG]
FT   BINDING         216
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: Y
FT   BINDING         235
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: G
FT   BINDING         242
FT                   /ligand="shikimate"
FT                   /ligand_id="ChEBI:CHEBI:36208"
FT   Condition: Q
XX
Size: 253-295;
Related: MF_01578!; MF_03143!;
Template: P15770; O67049; P43876; P56119; Q8Y9N5; Q5HNV1; Q5SJF8; Q9KVT3; Q58484; P44774; Q9X5C9;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: MF_00214 (aroD)
 Cter: None
Duplicate: None
Plasmid: None
Comments: Aroe in CORGL and CORGB catalyzes the NAD(+)-dependent oxidation of both
 quinate and shikimate with a higher catalytic efficiency for quinate rather than
 shikimate, and seems to play a key role in the quinate-degradation pathway
 (PubMed=18566515).
XX
# Revision 1.41 2023/06/01
//