HAMAP logo

HAMAP rule MF_01578

Send feedback

General rule information [?]

Accession MF_01578
Dates 23-FEB-2007 (Created)
19-NOV-2022 (Last updated, Version 19)
Name Shikimate_DH_YdiB
Scope(s) Bacteria
Enterobacterales
Template(s) P0A6D5 (YDIB_ECOLI); Q8ZPR4 (YDIB_SALTY); [ Recover all ]
Triggered by HAMAP; MF_01578 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier YDIB
Protein name RecName: Full=Quinate/shikimate dehydrogenase;
                 EC=1.1.1.282;
AltName: Full=NAD-dependent shikimate 5-dehydrogenase;
Gene name Name=ydiB;

Comments [?]

FUNCTIONThe actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD.
CATALYTIC ACTIVITY Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.282;
CATALYTIC ACTIVITY Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH; Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.282;
CATALYTIC ACTIVITY Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.282;
CATALYTIC ACTIVITY Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH; Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.282;
PATHWAYMetabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
SUBUNITHomodimer.
SIMILARITYBelongs to the shikimate dehydrogenase family.

Keywords [?]


Gene Ontology [?]

GO:0030266; Molecular function:quinate 3-dehydrogenase (NAD+) activity
GO:0004764; Molecular function:shikimate 3-dehydrogenase (NADP+) activity
GO:0009073; Biological process:aromatic amino acid family biosynthetic process

Cross-references [?]

Pfam PF01488; Shikimate_DH; 1;
Pfam PF08501; Shikimate_dh_N; 1;

Features [?]

From: YDIB_ECOLI (P0A6D5)
Key From To Description Tag Condition FTGroup
BINDING 132 135 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
A-G-G-A
BINDING 155 158 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
N-R-[RK]-D
BINDING 232 235 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
C-x(2)-N
BINDING 71 71 /ligand="substrate" K
BINDING 107 107 /ligand="substrate" D
BINDING 205 205 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
K
BINDING 255 255 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"
G

Additional information [?]

Size range 288-297 amino acids
Related rules MF_00222
Fusion Nter: None Cter: None
Comments Divergent N-terminus in SHIDS and SHIF8; sequences not included in alignment and not taken into account in size range



View rule in raw text format (no links)