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563  structures 7388  species 0  interactions 109544  sequences 596  architectures

Clan: Acyl-CoA_dh (CL0087)

Summary

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 109544. 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

Members

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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Alignments

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) 94233 (86.0%) View
Acyl-CoA_dh_2 (PF08028) 7294 (6.7%) View
ACOX (PF01756) 6130 (5.6%) View
HpaB (PF03241) 1887 (1.7%) View
Total: 4 Total: 109544 Clan alignment
 

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Family relationships

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

Species distribution

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

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Structures

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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