CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Putative quinone oxidoreductase YhdH

Enzyme Information

With a quinone or similar compound as acceptor.
based on mapping to UniProt P26646
Acrylyl-CoA reductase (NADPH).
based on mapping to UniProt P26646
Propanoyl-CoA + NADP(+) = acrylyl-CoA + NADPH.
-!- Catalyzes a step in the 3-hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2) fixation pathway found in some thermoacidophilic archaea. -!- The reaction is catalyzed in the opposite direction to that shown. -!- The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA. -!- Different from EC, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16.
S-(hydroxymethyl)glutathione dehydrogenase.
based on mapping to UniProt P26646
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.
-!- The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC -!- Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC -!- Also specifically reduces S-nitrosylglutathione. -!- Formerly EC

UniProtKB Entries (1)

Escherichia coli K-12
Probable acrylyl-CoA reductase AcuI

PDB Structure

PDB 1O89
External Links
Primary Citation
Structure of the Escherichia Coli Yhdh, a Putative Quinone Oxidoreductase
Sulzenbacher, G., Roig-Zamboni, V., Pagot, F., Grisel, S., Salamoni, A., Valencia, C., Campanacci, V., Vincentelli, R., Tegoni, M., Eklund, H., Cambillau, C.
Acta Crystallogr.,Sect.D