To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00065

3-hydroxyacyl-CoA dehydrogenase signature


3-hydroxyacyl-CoA dehydrogenase (EC (HCDH) [1] 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 β-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 [2].

The other proteins structurally related to HCDH are:

  • Bacterial 3-hydroxybutyryl-CoA dehydrogenase (EC which reduces 3-hydroxybutanoyl-CoA to acetoacetyl-CoA [3].
  • Eye lens protein lambda-crystallin [4], which is specific to lagomorphes (such as rabbit).

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 center of the sequence. We have chosen to derive a signature pattern from this central region.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

3HCDH, PS00067; 3-hydroxyacyl-CoA dehydrogenase signature  (PATTERN)


1AuthorsBirktoff J.J., Holden H.M., Hamlin R., Xuong N.-H., Banaszak L.J.
SourceProc. Natl. Acad. Sci. U.S.A. 84:8262-8266(1987).

2AuthorsNakahigashi K., Inokuchi H.
TitleNucleotide sequence of the fadA and fadB genes from Escherichia coli.
SourceNucleic Acids Res. 18:4937-4937(1990).
PubMed ID2204034

3AuthorsMullany P., Clayton C.L., Pallen M.J., Slone R., al-Saleh A., Tabaqchali S.
TitleGenes encoding homologues of three consecutive enzymes in the butyrate/butanol-producing pathway of Clostridium acetobutylicum are clustered on the Clostridium difficile chromosome.
SourceFEMS Microbiol. Lett. 124:61-67(1994).
PubMed ID8001771

4AuthorsMulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H., de Jong W.W.
TitleLambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases.
SourceJ. Biol. Chem. 263:15462-15466(1988).
PubMed ID3170592

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)