title: Prokaryotic origins for the mitochondrial alternative oxidase and plastid terminal oxidase nuclear genes.
abstract: The mitochondrial alternative oxidase is a diiron carboxylate quinol oxidase (Dox) found in plants and some fungi and protists, but not animals. The plastid terminal oxidase is distantly related to alternative oxidase and is most likely also a Dox protein. Database searches revealed that the alpha-proteobacterium Novosphingobium aromaticivorans and the cyanobacteria Nostoc sp. PCC7120, Synechococcus sp. WH8102 and Prochlorococcus marinus subsp. pastoris CCMP1378 each possess a Dox homolog. Each prokaryotic protein conforms to the current structural models of the Dox active site and phylogenetic analyses suggest that the eukaryotic Dox genes arose from an ancestral prokaryotic gene.
authors.affiliation: Plant Molecular Biology Group and School of Plant Biology, University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia. pfinnega@agric.uwa.edu.au
authors.forename: Patrick M
authors.initials: PM
authors.lastname: Finnegan
authors.forename: Ann L
authors.initials: AL
authors.lastname: Umbach
authors.forename: Jackie A
authors.initials: JA
authors.lastname: Wilce
mesh_terms: D020561:Alphaproteobacteria / Q000201:enzymology / Q000235:genetics; D000595:Amino Acid Sequence; D001665:Binding Sites; D000458:Cyanobacteria / Q000201:enzymology / Q000235:genetics; D008928:Mitochondria / Q000201:enzymology*; D024101:Mitochondrial Proteins; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000235:genetics*; D010802:Phylogeny; D010940:Plant Proteins; D018087:Plastids / Q000201:enzymology*; D011387:Prokaryotic Cells / Q000201:enzymology* / Q000502:physiology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000099188:Alternative Oxidase
chemical_list: D024101:Mitochondrial Proteins; D010088:Oxidoreductases; D010940:Plant Proteins; D000099188:Alternative Oxidase