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        <parTitl xml:lang="en">Plasmid sequences corresponding to the study "Origin and evolution of key enzymes in the anammox pathway revisited".</parTitl>
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        <parTitl xml:lang="en">Plasmid sequences corresponding to the study "Origin and evolution of key enzymes in the anammox pathway revisited".</parTitl>
        <IDNo agency="SND">doi-10-17044-scilifelab-30103798-0</IDNo>
        <IDNo agency="DOI">https://doi.org/10.17044/SCILIFELAB.30103798</IDNo>
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        <AuthEnty xml:lang="en" affiliation="Science for Life Laboratory">Jimenez-Gonzalez, Alejandro</AuthEnty>
        <AuthEnty xml:lang="en" affiliation="Science for Life Laboratory">Hägglund, Emil</AuthEnty>
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      <abstract xml:lang="en" contentType="abstract">pHA-1 plasmid sequences with synthetic gene constructs in which the N-terminal sequences of the hydrazine dehydrogenase (HDH) and the gamma-subunit of the hydrazine synthase (HZS) from “Ca. Kuenenia stuttgartiensis” strain MBR1 were fused to the phoA gene lacking its own native signal sequence. For comparison, the signal sequences of two periplasmic proteins in “Ca. Kuenenia stuttgartiensis” strain MBR1, a flagellar P-ring protein, and an outer membrane lipoprotein-sorting protein, were also fused to the phoA gene. As positive controls, we used plasmids containing the phoA gene with its native signal sequence as well as a fusion of the lepB and the phoA genes. As negative controls, we used a plasmid that contained the phoA gene without a signal sequence.</abstract>
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