PROSITE documentation PDOC00815
Pyridoxamine 5'-phosphate oxidase signature


Pyridoxamine 5'-phosphate oxidase (EC is a FMN flavoprotein 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 sequences of the enzyme from bacterial (genes pdxH or fprA) [1] and fungal (gene PDX3) [2] sources show that this protein has been highly conserved throughout evolution.

PdxH is evolutionary related [3] to one of the enzymes in the phenazine biosynthesis protein pathway, phzD (also known as phzG).

As a signature pattern, we selected a highly conserved region located in the C-terminal part of these enzymes.

Last update:

April 2006 / Pattern revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

PYRIDOX_OXIDASE, PS01064; Pyridoxamine 5'-phosphate oxidase signature  (PATTERN)


1AuthorsLam H.-M. Winkler M.E.
TitleCharacterization of the complex pdxH-tyrS operon of Escherichia coli K-12 and pleiotropic phenotypes caused by pdxH insertion mutations.
SourceJ. Bacteriol. 174:6033-6045(1992).
PubMed ID1356963

2AuthorsLoubbardi A. Marcireau C. Karst F. Guilloton M.
TitleSterol uptake induced by an impairment of pyridoxal phosphate synthesis in Saccharomyces cerevisiae: cloning and sequencing of the PDX3 gene encoding pyridoxine (pyridoxamine) phosphate oxidase.
SourceJ. Bacteriol. 177:1817-1823(1995).
PubMed ID7896706

3AuthorsPierson L.S. III Gaffney T. Lam S. Gong F.
TitleMolecular analysis of genes encoding phenazine biosynthesis in the biological control bacterium. Pseudomonas aureofaciens 30-84.
SourceFEMS Microbiol. Lett. 134:299-307(1995).
PubMed ID8586283

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)