Modularity of methylotrophy, revisited
Article first published 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 published online: 10 OCT 2011
- Article first published 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.
|EMI_2464_sm_FigS1-3-TableS1.pdf||1747K||Supporting info item|
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.