InterPro : IPR006108

Name  3-hydroxyacyl-CoA dehydrogenase, C-terminal Short Name  3HC_DH_C
Type  Domain Description  3-hydroxyacyl-CoA dehydrogenase () (HCDH) []is an enzyme involved in fatty acid metabolism, it catalyzes the reduction of 3-hydroxyacyl-CoA to 3-oxoacyl-CoA. Most eukaryotic cells have 2 fatty-acid beta-oxidation systems, one located in mitochondria and the other in peroxisomes. In peroxisomes 3-hydroxyacyl-CoA dehydrogenase forms, with enoyl-CoA hydratase (ECH) and 3,2-trans-enoyl-CoA isomerase (ECI) a multifunctional enzyme where the N-terminal domain bears the hydratase/isomerase activities and the C-terminal domain the dehydrogenase activity. There are two mitochondrial enzymes: one which is monofunctional and the other which is, like its peroxisomal counterpart, multifunctional.In Escherichia coli(gene fadB) and Pseudomonas fragi(gene faoA) HCDH is part of a multifunctional enzyme which also contains an ECH/ECI domain as well as a 3-hydroxybutyryl-CoA epimerase domain [].There are two major region of similarities in the sequences of proteins of the HCDH family, the first one located in the N-terminal, corresponds to the NAD-binding site, the second one is located in the centre of the sequence. This represents the C-terminal domain which is also found in lambda crystallin. Some proteins include two copies of this domain.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

1 Contains

Id Name Short Name Type
IPR006180 3-hydroxyacyl-CoA dehydrogenase, conserved site 3-OHacyl-CoA_DH_CS Conserved_site

5 Found In

Id Name Short Name Type
IPR012803 Fatty acid oxidation complex, alpha subunit, mitochondrial Fa_ox_alpha_mit Family
IPR012799 Fatty oxidation complex, alpha subunit FadB FadB Family
IPR022694 3-hydroxyacyl-CoA dehydrogenase 3-OHacyl-CoA_DH Family
IPR012802 Fatty oxidation complex, alpha subunit FadJ FadJ Family
IPR011967 3-hydroxyacyl-CoA dehydrogenase PaaC 3-OHacyl-CoA_DH_PaaC Family

1 Parent Features

Id Name Short Name Type
IPR013328 Dehydrogenase, multihelical DH_multihelical Domain

2 Publications

First Author Title Year Journal Volume Pages
Nakahigashi K Nucleotide sequence of the fadA and fadB genes from Escherichia coli. 1990 Nucleic Acids Res 18 4937
Birktoft JJ Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution. 1987 Proc Natl Acad Sci U S A 84 8262-6

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)