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  Domain Name: PNPOx_C
Pyridoxine 5'-phosphate oxidase C-terminal dimerisation region. Pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes 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 Myxococcus xanthus pdxH, 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.
No pairwise interactions found for the domain PNPOx_C

Total Mutations Found: 1
Total Disease Mutations Found: 1
This domain occurred 1 times on human genes (1 proteins).



  PYRIDOXAMINE 5-PRIME-PHOSPHATE OXIDASE DEFICIENCY


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Range on the Protein:  

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No Conserved Features/Sites Found for PNPOx_C







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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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