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254  structures 3538  species 7  interactions 31652  sequences 148  architectures

Clan: Acyl-CoA_dh (CL0087)


Acyl-CoA dehydrogenase, C-terminal domain-like Add an annotation

The Acyl-CoA dehydrogenase FAD binding domain forms an mostly alpha helical domain, comprised of four helices arranged in up-and-down bundle. In Acyl-CoA oxidase II this domain appears to have been duplicated.

This clan contains 4 families and the total number of domains in the clan is 31652. The clan was built by RD Finn.

Literature references

  1. Dym O, Eisenberg D; , Protein Sci 2001;10:1712-1728.: Sequence-structure analysis of FAD-containing proteins. PUBMED:11514662 EPMC:11514662


This clan contains the following 4 member families:

ACOX Acyl-CoA_dh_1 Acyl-CoA_dh_2 HpaB

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
Acyl-CoA_dh_1 (PF00441) 26994 (85.3%) View
Acyl-CoA_dh_2 (PF08028) 2598 (8.2%) View
ACOX (PF01756) 1066 (3.4%) View
HpaB (PF03241) 994 (3.1%) View
Total: 4 Total: 31652 Clan alignment

Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.

Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

Tree controls


This tree shows the occurrence of the domains in this clan across different species. More...



There are 7 interactions for this clan. More...

Interacting families
Acyl-CoA_dh_1 Acyl-CoA_dh_1
Acyl-CoA_dh_2 Acyl-CoA_dh_2
HpaB HpaB


For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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