PROSITE logo

PROSITE documentation PDOC00065 [for PROSITE entry PS00067]
3-hydroxyacyl-CoA dehydrogenase signature


Description

3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) (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 1.1.1.157) 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)


References

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 copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

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