Summary: Pyridoxamine 5'-phosphate oxidase
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Pyridoxamine 5'-phosphate oxidase Provide feedback
No Pfam abstract.
Internal database links
| Similarity to PfamA using HHSearch: | DUF385 DUF447 FMN_bind_2 Pyridox_oxase_2 Pyridox_ox_2 Pyrid_oxidase_2 |
External database links
| HOMSTRAD: | Pyridox_oxidase |
| PANDIT: | PF01243 |
| PROSITE: | PDOC00815 |
| Pseudofam: | PF01243 |
| SCOP: | 1ci0 |
| SYSTERS: | Pyridox_oxidase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR011576
Pyridoxamine 5'-phosphate oxidase (PNPOx; EC) is a FMN flavoprotein that catalyses the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This reaction serves as the terminal step in the de novo biosynthesis of PLP in Escherichia coli and as a part of the salvage pathway of this coenzyme in both E. coli and mammalian cells [PUBMED:12686112, PUBMED:12824491]. The binding sites for FMN and for substrate have been highly conserved throughout evolution.
This entry represents the FMN-binding domain present in pyridoxamine 5'-phosphate oxidases, as well as in a number of proteins that have not been demonstrated to have enzymatic activity. The FMN-binding domain has a structure consisting of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. PNPOx has a different dimerisation mode than that found in flavin reductases, which also carry an FMN-binding domain with a similar topology.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | pyridoxamine-phosphate oxidase activity (GO:0004733) |
| FMN binding (GO:0010181) | |
| Biological process | oxidation-reduction process (GO:0055114) |
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 FMN-binding (CL0336), which contains the following 8 members:
DUF385 DUF447 Flavin_Reduct FMN_bind_2 Pyrid_oxidase_2 Pyridox_ox_2 Pyridox_oxase_2 Pyridox_oxidaseAlignments
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...
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 (141) |
Full (8674) |
Representative proteomes | NCBI (8805) |
Meta (4127) |
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| RP15 (870) |
RP35 (1911) |
RP55 (2492) |
RP75 (2886) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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 (141) |
Full (8674) |
Representative proteomes | NCBI (8805) |
Meta (4127) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (870) |
RP35 (1911) |
RP55 (2492) |
RP75 (2886) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
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...
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
| Seed source: | Prosite |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Finn RD |
| Number in seed: | 141 |
| Number in full: | 8674 |
| Average length of the domain: | 89.20 aa |
| Average identity of full alignment: | 19 % |
| Average coverage of the sequence by the domain: | 47.13 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 89 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
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 Pyridox_oxidase domain has been found. There are 83 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence