Extended Data Fig. 1: In-depth bioinformatics analysis of cytoplasmic multidomain FDHs.
From: A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases
a. Phylogenetic tree generated of the N-terminal domain of 442 FDH catalytic subunit sequences (Cata SU) using a maximum likelihood approach. Inter-sequence identity was reduced to a maximum of 90% between any two sequences. Sequences forming a clade have been collapsed. The presence of specific redox centers was deduced from the identification of conserved motifs in the primary amino acid sequence and the partner subunit(s) from the genomic organization. The arrow indicates the position at scale between the N-terminal and the C-terminal domain. Characterized representatives are indicated: Bacillus subtilis (1), Methylobacterium extorquens AM1 (2), Rhodobacter capsulatus (3) and Gottschalkia acidurici (4). b. Phylogenetic tree of the C-terminal domain of 442 FDH sequences using a maximum likelihood approach. Each branch tip represents a single sequence. ForC sequences are colored red. Both trees were built with IQ-TREE using the WAG + I + G4 model. Supports at nodes are ultrafast bootstrap values above 95% and are indicated by a black circle. iTOL 6.8.1 was used to generate the figures.
