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34  structures 2117  species 0  interactions 5535  sequences 104  architectures

Family: ACOX (PF01756)

Summary: Acyl-CoA oxidase

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Acyl-CoA oxidase Provide feedback

This is a family of Acyl-CoA oxidases EC:1.3.3.6. Acyl-coA oxidase converts acyl-CoA into trans-2- enoyl-CoA [1].

Literature references

  1. Hayashi H, De Bellis L, Yamaguchi K, Kato A, Hayashi M, Nishimura M; , J Biol Chem 1998;273:8301-8307.: Molecular characterization of a glyoxysomal long chain acyl-CoA oxidase that is synthesized as a precursor of higher molecular mass in pumpkin. PUBMED:9525937 EPMC:9525937


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002655

Acyl-CoA oxidase (ACO) acts on CoA derivatives of fatty acids with chain lengths from 8 to 18. It catalyses the first and rate-determining step of the peroxisomal beta-oxidation of fatty acids [ PUBMED:11872165 ].

Acyl-CoA oxidase is a homodimer and the polypeptide chain of the subunit is folded into the N-terminal alpha-domain, beta-domain, and C-terminal alpha-domain [ PUBMED:11872165 ]. Functional differences between the peroxisomal acyl-CoA oxidases and the mitochondrial acyl-CoA dehydrogenases are attributed to structural differences in the FAD environments [ PUBMED:15581893 ].

Experimental data indicate that, in the pumpkin, the expression pattern of ACOX is very similar to that of the glyoxysomal enzyme 3-ketoacyl-CoA thiolase [ PUBMED:9525937 ]. In humans, defects in ACOX1 are the cause of pseudoneonatal adrenoleukodystrophy, also known as peroxisomal acyl-CoA oxidase deficiency. Pseudo-NALD is a peroxisomal single-enzyme disorder. Clinical features include mental retardation, leukodystrophy, seizures, mild hepatomegaly and hearing deficit. Pseudo-NALD is characterised by increased plasma levels of very-long chain fatty acids due to a decrease in, or absence of, peroxisome acyl-CoA oxidase activity, despite the peroxisomes being intact and functioning.

This entry represents the Acyl-CoA oxidase C-terminal.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Acyl-CoA_dh (CL0087), which has the following description:

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.

The clan contains the following 4 members:

ACOX Acyl-CoA_dh_1 Acyl-CoA_dh_2 HpaB

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(243)
Full
(5535)
Representative proteomes UniProt
(11321)
RP15
(1028)
RP35
(2599)
RP55
(4711)
RP75
(6781)
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(243)
Full
(5535)
Representative proteomes UniProt
(11321)
RP15
(1028)
RP35
(2599)
RP55
(4711)
RP75
(6781)
Alignment:
Format:
Order:
Sequence:
Gaps:
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Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(243)
Full
(5535)
Representative proteomes UniProt
(11321)
RP15
(1028)
RP35
(2599)
RP55
(4711)
RP75
(6781)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_598 (release 4.2)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bashton M , Bateman A
Number in seed: 243
Number in full: 5535
Average length of the domain: 161.70 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 24.89 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.1 22.1
Trusted cut-off 22.1 22.1
Noise cut-off 22.0 22.0
Model length: 181
Family (HMM) version: 21
Download: download the raw HMM for this family

Species distribution

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Selections

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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. 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 PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ACOX domain has been found. There are 34 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A0R0HNI5 View 3D Structure Click here
A0A1D6EBD9 View 3D Structure Click here
A0A1D6N7A4 View 3D Structure Click here
A0A1D6NXM9 View 3D Structure Click here
A0A1D6PR01 View 3D Structure Click here
A0A1D6QKY9 View 3D Structure Click here
A0A1D8PQ67 View 3D Structure Click here
A0A2R8QDD9 View 3D Structure Click here
A4I325 View 3D Structure Click here
B4F8X3 View 3D Structure Click here
B7Z028 View 3D Structure Click here
D4A257 View 3D Structure Click here
F1QXK3 View 3D Structure Click here
F1R071 View 3D Structure Click here
I1J9T7 View 3D Structure Click here
I1K4K8 View 3D Structure Click here
I1KEV4 View 3D Structure Click here
I1LS94 View 3D Structure Click here
O15254 View 3D Structure Click here
O62137 View 3D Structure Click here
O62138 View 3D Structure Click here
O62139 View 3D Structure Click here
O62140 View 3D Structure Click here
O65201 View 3D Structure Click here
O65202 View 3D Structure Click here
P07872 View 3D Structure Click here
P0CZ23 View 3D Structure Click here
P0CZ24 View 3D Structure Click here
P13711 View 3D Structure Click here
P34355 View 3D Structure Click here
P97562 View 3D Structure Click here
Q15067 View 3D Structure Click here
Q20992 View 3D Structure Click here
Q2R1G8 View 3D Structure Click here
Q4CND8 View 3D Structure Click here
Q4DTT8 View 3D Structure Click here
Q54GQ6 View 3D Structure Click here
Q54II1 View 3D Structure Click here
Q54LF1 View 3D Structure Click here
Q54RB0 View 3D Structure Click here
Q55BH8 View 3D Structure Click here
Q55CT6 View 3D Structure Click here
Q5AJD6 View 3D Structure Click here
Q5AJD9 View 3D Structure Click here
Q63448 View 3D Structure Click here
Q69XR7 View 3D Structure Click here
Q7KML2 View 3D Structure Click here
Q8H631 View 3D Structure Click here
Q8MMS1 View 3D Structure Click here
Q93839 View 3D Structure Click here
Q945U3 View 3D Structure Click here
Q99424 View 3D Structure Click here
Q9DBS4 View 3D Structure Click here
Q9EPL9 View 3D Structure Click here
Q9LMI7 View 3D Structure Click here
Q9NUZ1 View 3D Structure Click here
Q9QXD1 View 3D Structure Click here
Q9R0H0 View 3D Structure Click here
Q9VIX4 View 3D Structure Click here
Q9W2G8 View 3D Structure Click here
Q9W2G9 View 3D Structure Click here
Q9W3U0 View 3D Structure Click here
Q9ZQP2 View 3D Structure Click here