Summary: Pyridoxamine 5'-phosphate oxidase
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Pyridoxamine 5'-phosphate oxidase Provide feedback
Pyridoxamine 5'-phosphate oxidase catalyses the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP), the terminal step in the de novo biosynthesis of PLP in Escherichia coli and part of the salvage pathway of this coenzyme in both E. coli and mammalian cells. This region is the flavoprotein FMN-binding domain.
di Salvo ML, Safo MK, Musayev FN, Bossa F, Schirch V; , Biochim Biophys Acta. 2003;1647:76-82.: Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase. PUBMED:12686112 EPMC:12686112
Internal database links
|Similarity to PfamA using HHSearch:||Pyridox_oxidase|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR024624
Pyridoxamine 5'-phosphate oxidase catalyses the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP), the terminal step in the de novo biosynthesis of PLP in Escherichia coli and part of the salvage pathway of this coenzyme in both E. coli and mammalian cells.
This entry represents the FMN-binding domain of pyridoxamine 5'-phosphate oxidases that belong to the Alr4036 family.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||FMN binding (GO:0010181)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
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This includes those related to the ferredoxin reductase-like FAD-binding domain and those that are Pyridoxine 5'-phosphate oxidase (PNP)-like.
The clan contains the following 8 members:DUF385 DUF447 Flavin_Reduct FMN_bind_2 Pyrid_oxidase_2 Pyridox_ox_2 Pyridox_oxase_2 Pyridox_oxidase
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_2486 (release 24.0)|
|Author:||Wood V, Coggill P|
|Number in seed:||60|
|Number in full:||319|
|Average length of the domain:||100.10 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||42.69 %|
|HMM build commands:||
build method: hmmbuild --amino -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||2|
|Download:||download the raw HMM for this family|
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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_oxase_2 domain has been found. There are 4 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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