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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.

December 2004 / Pattern and text revised.

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

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

Consensus pattern: [DNES]-x(2)-[GA]-F-[LIVMFYA]-x-[NT]-R-x(3)-[PA]-[LIVMFY]-[LIVMFYST]-x(5,6)-[LIVMFYCT]-[LIVMFYEAH]-x(2)-[GVE] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00067 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00067 • Scan Swiss-Prot/TrEMBL entries against PS00067 • view ligand binding statistics

Matching PDB structures: 1F0Y 1F12 1F14 1F17 ... [ALL]

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

2	Authors	Nakahigashi K., Inokuchi H.
	Title	Nucleotide sequence of the fadA and fadB genes from Escherichia coli.
	Source	Nucleic Acids Res. 18:4937-4937(1990).
	PubMed ID	2204034

3	Authors	Mullany P., Clayton C.L., Pallen M.J., Slone R., al-Saleh A., Tabaqchali S.
	Title	Genes encoding homologues of three consecutive enzymes in the butyrate/butanol-producing pathway of Clostridium acetobutylicum are clustered on the Clostridium difficile chromosome.
	Source	FEMS Microbiol. Lett. 124:61-67(1994).
	PubMed ID	8001771

4	Authors	Mulders J.W.M., Hendriks W., Blankesteijn W.M., Bloemendal H., de Jong W.W.
	Title	Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases.
	Source	J. Biol. Chem. 263:15462-15466(1988).
	PubMed ID	3170592

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