CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family Fatty oxidation complex, alpha subunit

Enzyme Information

4.2.1.17
Enoyl-CoA hydratase.
based on mapping to UniProt P28793
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O.
-!- Acts in the reverse direction. -!- With cis-compounds, yields (3R)-3-hydroxyacyl-CoA (cf. EC 4.2.1.74).
1.1.1.35
3-hydroxyacyl-CoA dehydrogenase.
based on mapping to UniProt P28793
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH.
-!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3- hydroxyacylhydrolipoate. -!- Some enzymes act, more slowly, with NADP(+). -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211).
5.1.2.3
3-hydroxybutyryl-CoA epimerase.
based on mapping to UniProt P28793
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.
5.3.3.8
Delta(3)-Delta(2)-enoyl-CoA isomerase.
based on mapping to UniProt P28793
(1) A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA. (2) A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.
-!- The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. -!- Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C(3), which cannot be processed further by the regular enzymes of the beta- oxidation system. -!- This enzyme isomerizes the bond to a trans bond at position C(2), which can be processed further. -!- The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. -!- The enzyme can also catalyze the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.

UniProtKB Entries (1)

P28790
FADA_PSEFR
Pseudomonas fragi
3-ketoacyl-CoA thiolase

PDB Structure

PDB 1WDL
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex
Ishikawa, M., Tsuchiya, D., Oyama, T., Tsunaka, Y., Morikawa, K.
Embo J.