Modularity of methylotrophy, revisited
Version of Record online: 28 MAR 2011
© 2011 Society for Applied Microbiology and Blackwell Publishing Ltd
Volume 13, Issue 10, pages 2603–2622, October 2011
How to Cite
Chistoserdova, L. (2011), Modularity of methylotrophy, revisited. Environmental Microbiology, 13: 2603–2622. doi: 10.1111/j.1462-2920.2011.02464.x
- Issue online: 10 OCT 2011
- Version of Record online: 28 MAR 2011
- Received 25 November, 2010; accepted 13 February, 2011.
Fig. S1. Phylogeny of Mtd enzymes. The dotted line separates known and presumed MtdB enzymes from other Mtd types. α, β, γ: α-, β- and γ-Proteobacteria.
Fig. S2. Phylogenetic tree showing different classes of XoxF proteins, along with MxaF proteins. All proteins share more than 40% amino acid identity. A distantly related PQQ-linked dehydrogenase (less than 35% amino acid identity) was used as outgroup. All reported mutations (see text) were for group XoxF5.
Fig. S3. Phylogeny of Fae and Fae-like proteins. The dotted line separates known and presumed true Fae from homologues of unknown function.
Table S1. Substrate specificities of Mtd enzymes, compared with FolD.
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