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Annotation rule MF_01578
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General rule information [?]

Accession MF_01578
Dates 23-FEB-2007 (Created)
19-NOV-2019 (Last updated, Version 17)
Name Shikimate_DH_YdiB
Scope
Bacteria; Enterobacterales
Templates P0A6D5 (YDIB_ECOLI); Q8ZPR4 (YDIB_SALTY): [Recover all]

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
ydiB

Comments [?]

Function The 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 RHEA:22364: L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH
EC 1.1.1.282
RHEA:18425: L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH
EC 1.1.1.282
RHEA:17737: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
EC 1.1.1.282
RHEA:17741: NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH
EC 1.1.1.282
Pathway Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Subunit Homodimer.
Similarity Belongs 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;
PF08501; Shikimate_dh_N; 1;

Features [?]

From: YDIB_ECOLI (P0A6D5)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     132     135       NAD     A-G-G-A  
NP_BIND     155     158       NAD     N-R-[RK]-D  
NP_BIND     232     235       NAD     C-x(2)-N  
BINDING     71     71       Substrate     K  
BINDING     107     107       Substrate     D  
BINDING     205     205       NAD; via amide nitrogen     K  
BINDING     255     255       NAD; via carbonyl oxygen     G  

Additional information [?]

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