Philasterides dicentrarchi is a marine benthic microaerophilic scuticociliate and an opportunistic endoparasite that can infect and cause high mortalities in cultured turbot (Scophthalmus maximus). in addition to a cytochrome pathway (cp), the ciliate can use a cyanide-insensitive respiratory pathway, which indicates the existence of an alternative oxidase (AoX) in the mitochondrion. Although AoX activity has been described in P. dicentrarchi, based on functional assay results, genetic evidence of the presence of AoX in the ciliate has not previously been reported. in this study, we conducted genomic and transcriptomic analysis of the ciliate and identified the AOX gene and its corresponding mRNA. The AOX gene (size 1,106 bp) contains four exons and three introns that generate an open reading frame of 915 bp and a protein with a predicted molecular weight of 35.6 kDa. The amino acid (aa) sequence of the AoX includes an import signal peptide targeting the mitochondria and the protein is associated with the inner membrane of the mitochondria. Bioinformatic analysis predicted that the peptide is a homodimeric glycoprotein, although monomeric forms may also appear under native conditions, with eXXH motifs associated with the diiron active centers. the aa sequences of the AOX of different P. dicentrarchi isolates are highly conserved and phylogenetically closely related to AOXs of other ciliate species, especially scuticociliates. AOX expression increased significantly during infection in the host and after the addition of CP inhibitors. This confirms the important physiological roles of AoX in respiration under conditions of low levels of o 2 and in protecting against oxidative stress generated during infection in the host. Alternative oxidase (AOX), also known as ubiquinol-oxidoreductase, is included within the diiron carboxylate superfamily. The enzyme is characterized by cyanide resistance and is associated with maintenance of metabolic homeostasis via mitochondrial electron transport in plants subjected to various stress conditions 1,2. In plants, AOX is considered a ubiquitous enzyme; however, in algae 3 , fungi 4-9 , protozoa 10-13 and several invertebrate species 14 it is quite sporadic. AOX is involved in the mitochondrial respiratory chain and provides an alternative pathway for the direct transfer of electrons from ubiquinone to oxygen, thus forming water 15. It facilitates mitochondrial respiratory activity and therefore the functioning of the Krebs cycle after inhibition of the cytochrome route due to the presence of nitric oxide, cyanide (both inhibitors of the complex IV) or antimycin A (complex III inhibitor) 1,12,16. However, AOX reduces the energy efficiency of respiration as only 1/3 of the ATP is produced