Multiple sequence alignment of P(N/M)P oxidases and putative P(N/M)P oxidases.

<p>(A) Protein alignment of putative P(N/M)P oxidases from <i>S</i>. <i>cerevisiae YLR456W</i> (AAS56557), <i>YPR172W</i> (NP_015498) and characterized P(N/M)P oxidases: RATN, <i>Rattus norvegicus</i> (O88794); HUMN, <i>Homo sapiens</i> (AK001397); CAEN, <i>Caenorhabditis elegans</i> (AAA21167); SCHC, <i>Schizophyllum commune</i> (AAC28862); SACC, <i>Saccharomyces cerevisiae</i> (P38075); SCHI, <i>Schizosaccharomyces pombe</i> (CAB60247); ECOL, <i>Echerichia coli</i> (P28225); MYCT, <i>Mycobacterium tuberculosis</i> (O06207); MYCL, <i>Mycobacterium leprae</i> (O33065); DEIN, <i>Deinococcus radiodurans</i> (AAF10072); NEIS, <i>Neisseria meningitidis</i> (CAB84799); HAEL, <i>Haemophilus influenzae</i> (P44909); SYNS, <i>Synechocystis sp</i>. (P74211); ZYMM, <i>Zymomonas mobilis</i> (AAD53919). Protein Alignment was generated by Clustal-W2. Red asterisks indicate residues that are 100% conserved among P(N/M)P oxidases and directly involved in the binding of FMN. (B) Phylogenetic tree representation of the alignment shown in A. This is a neighbor-joining tree without distance corrections. (C) Sequence logo of 50 P(N/M)P oxidases homologous to <i>PDX3</i> showing the most conserved residues in P(N/M)P oxidases, charged residues are shown in blue, polar residues in green and non-polar in black. The motif EFWxxxxxRxHxR is delimited by the orange bracket on panel A.