ダウンロード数: 135
このアイテムのファイル:
ファイル | 記述 | サイズ | フォーマット | |
---|---|---|---|---|
fmicb.2018.03353.pdf | 3.84 MB | Adobe PDF | 見る/開く |
タイトル: | Structural and phylogenetic diversity of anaerobic carbon-monoxide dehydrogenases |
著者: | Inoue, Masao Nakamoto, Issei Omae, Kimiho Oguro, Tatsuki Ogata, Hiroyuki https://orcid.org/0000-0001-6594-377X (unconfirmed) Yoshida, Takashi https://orcid.org/0000-0002-5257-0617 (unconfirmed) Sako, Yoshihiko |
著者名の別形: | 井上, 真男 大前, 公保 緒方, 博之 吉田, 天士 左子, 芳彦 |
キーワード: | carbon-monoxide dehydrogenase genomic context structural prediction functional prediction molecular evolution horizontal gene transfer |
発行日: | 17-Jan-2019 |
出版者: | Frontiers Media SA |
誌名: | Frontiers in Microbiology |
巻: | 9 |
論文番号: | 3353 |
抄録: | Anaerobic Ni-containing carbon-monoxide dehydrogenases (Ni-CODHs) catalyze the reversible conversion between carbon monoxide and carbon dioxide as multi-enzyme complexes responsible for carbon fixation and energy conservation in anaerobic microbes. However, few biochemically characterized model enzymes exist, with most Ni-CODHs remaining functionally unknown. Here, we performed phylogenetic and structure-based Ni-CODH classification using an expanded dataset comprised of 1942 non-redundant Ni-CODHs from 1375 Ni-CODH-encoding genomes across 36 phyla. Ni-CODHs were divided into seven clades, including a novel clade. Further classification into 24 structural groups based on sequence analysis combined with structural prediction revealed diverse structural motifs for metal cluster formation and catalysis, including novel structural motifs potentially capable of forming metal clusters or binding metal ions, indicating Ni-CODH diversity and plasticity. Phylogenetic analysis illustrated that the metal clusters responsible for intermolecular electron transfer were drastically altered during evolution. Additionally, we identified novel putative Ni-CODH-associated proteins from genomic contexts other than the Wood–Ljungdahl pathway and energy converting hydrogenase system proteins. Network analysis among the structural groups of Ni-CODHs, their associated proteins and taxonomies revealed previously unrecognized gene clusters for Ni-CODHs, including uncharacterized structural groups with putative metal transporters, oxidoreductases, or transcription factors. These results suggested diversification of Ni-CODH structures adapting to their associated proteins across microbial genomes. |
著作権等: | © 2019 Inoue, Nakamoto, Omae, Oguro, Ogata, Yoshida and Sako. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
URI: | http://hdl.handle.net/2433/241359 |
DOI(出版社版): | 10.3389/fmicb.2018.03353 |
PubMed ID: | 30705673 |
出現コレクション: | 学術雑誌掲載論文等 |
このリポジトリに保管されているアイテムはすべて著作権により保護されています。