Summary: Pyridoxine 5'-phosphate oxidase C-terminal dimerisation region
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Pyridoxine 5'-phosphate oxidase C-terminal dimerisation region Provide feedback
Pyridoxine 5'-phosphate oxidase (PNPOx) catalyses the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidises either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. This domain represents one of the two dimerisation regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In P21159 S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule .
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
Safo MK, Mathews I, Musayev FN, di Salvo ML, Thiel DJ, Abraham DJ, Schirch V; , Structure. 2000;8:751-762.: X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution. PUBMED:10903950 EPMC:10903950
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This tab holds annotation information from the InterPro database.
InterPro entry IPR019576
Pyridoxamine 5'-phosphate oxidase (EC) is an enzyme that is involved in the de novo synthesis of pyridoxine (vitamin B6) and pyridoxal phosphate. It oxidizes pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P. The enzyme requires the presence of flavin mononucleotide (FMN) as a cofactor, although there is some evidence that coenzyme F420 may perform this role in some species [PUBMED:20675471].
The sequences of the enzyme from bacterial (genes pdxH or fprA) [PUBMED:1356963] and fungal (gene PDX3) [PUBMED:7896706] sources show that this protein has been highly conserved throughout evolution. PdxH is evolutionary related [PUBMED:8586283] to one of the enzymes in the phenazine biosynthesis protein pathway, phzD (also known as phzG).
This entry represents one of the two dimerisation regions of the protein, located at the edge of the dimer interface, at the C terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In SWISSPROT, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule [PUBMED:10903950].
|Molecular function||oxidoreductase activity, acting on the CH-NH2 group of donors (GO:0016638)|
|Biological process||oxidation-reduction process (GO:0055114)|
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Curation and family details
|Seed source:||Pfam-B_685 (release 22.0), PROSITE_PS01064|
|Author:||Finn R, Coggill P|
|Number in seed:||593|
|Number in full:||10268|
|Average length of the domain:||41.00 aa|
|Average identity of full alignment:||56 %|
|Average coverage of the sequence by the domain:||18.69 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|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 PNPOx_C domain has been found. There are 30 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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