AC   MF_01578;
DC   Protein; auto
TR   HAMAP; MF_01578; -; 1; level=0
XX
Names: Shikimate_DH_YdiB
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ID   YDIB
DE   RecName: Full=Quinate/shikimate dehydrogenase;
DE            EC=1.1.1.282;
DE   AltName: Full=NAD-dependent shikimate 5-dehydrogenase;
GN   Name=ydiB;
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CC   -!- FUNCTION: The actual biological function of YdiB remains unclear, nor
CC       is it known whether 3-dehydroshikimate or quinate represents the
CC       natural substrate. Catalyzes the reversible NAD-dependent reduction of
CC       both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate
CC       (SA) and quinate, respectively. It can use both NAD or NADP for
CC       catalysis, however it has higher catalytic efficiency with NAD.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH;
CC         Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.282;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.282;
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;
CC         EC=1.1.1.282;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC         ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.282;
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.
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DR   Pfam; PF01488; Shikimate_DH; 1; trigger=no
DR   Pfam; PF08501; Shikimate_dh_N; 1; trigger=no
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KW   Amino-acid biosynthesis
KW   Aromatic amino acid biosynthesis
KW   NAD
KW   NADP
KW   Oxidoreductase
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GO   GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity
GO   GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity
GO   GO:0009073; P:aromatic amino acid family biosynthetic process
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FT   From: YDIB_ECOLI (P0A6D5)
FT   BINDING         132..135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: A-G-G-A
FT   BINDING         155..158
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: N-R-[RK]-D
FT   BINDING         232..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: C-x(2)-N
FT   BINDING         71
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         107
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         205
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: K
FT   BINDING         255
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: G
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Size: 288-297;
Related: MF_00222;
Template: P0A6D5; Q8ZPR4;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Divergent N-terminus in SHIDS and SHIF8; sequences not included
 in alignment and not taken into account in size range
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# Revision 1.19 2022/11/19
//