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69  structures 11879  species 4  interactions 33564  sequences 92  architectures

Family: FAD-oxidase_C (PF02913)

Summary: FAD linked oxidases, C-terminal domain

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This is the Wikipedia entry entitled "FAD-oxidase". More...

FAD-oxidase Edit Wikipedia article

FAD linked oxidases, C-terminal domain
PDB 1wve EBI.jpg
p-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit
Symbol FAD-oxidase_C
Pfam PF02913
Pfam clan CL0277
InterPro IPR004113
SCOP 1ahu

In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes.[1]


  1. ^ Mattevi, A.; Fraaije, M. W.; Coda, A.; Van Berkel, W. J. H. (1997). "Crystallization and preliminary x-ray analysis of the flavoenzyme vanillyl-alcohol oxidase fromPenicillium Simplicissimum". Proteins: Structure, Function, and Genetics 27 (4): 601–603. doi:10.1002/(SICI)1097-0134(199704)27:4<601::AID-PROT12>3.0.CO;2-O. PMID 9141139.  edit

This article incorporates text from the public domain Pfam and InterPro IPR004113

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

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.

FAD linked oxidases, C-terminal domain Provide feedback

This domain has a ferredoxin-like fold.

Literature references

  1. Mattevi A, Fraaije MW, Coda A, van Berkel WJ; , Proteins 1997;27:601-603.: Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum. PUBMED:9141139 EPMC:9141139

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR004113

Some oxygen-dependent oxidoreductases are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes (see INTERPRO).

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 FAD-oxidase_C (CL0277), which has the following description:

This clan consists of a duplicated subdomain in a variety of FAD-liked oxidase/dehydrogenase enzymes.

The clan contains the following 6 members:

ALO BBE Chol_subst-bind Cytokin-bind FAD-oxidase_C Lact-deh-memb


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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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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.

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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.

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

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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...


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: Structural domain
Previous IDs: none
Type: Domain
Author: Griffiths-Jones SR
Number in seed: 51
Number in full: 33564
Average length of the domain: 235.60 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 40.71 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.2 13.9
Trusted cut-off 21.2 14.0
Noise cut-off 21.1 13.8
Model length: 250
Family (HMM) version: 15
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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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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There are 4 interactions for this family. More...

FAD_binding_4 FAD_binding_4 FAD-oxidase_C Cytochrome_CBB3


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 FAD-oxidase_C domain has been found. There are 69 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 seqence.

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