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fml12304-sup-0001-FigS1-S3.docxWord document40K

Fig. S1. Multiple sequence alignments generated by clustalw analysis of the N-termini of MtrB homologs identified in the genomes of 22 metal-reducing Shewanella strains.

Fig. S2. Multiple sequence alignments generated by clustalw analysis of the N-termini of three CXXC-containing MtrB paralogs identified in the Shewanella oneidensis genome.

Fig. S3. Growth of Shewanella oneidensisMR-1 wild-type (●), ∆mtrB (∆), C42A (□), and C45A (×) mutant strains with either O2 (A), DMSO (B), TMAO (C), fumarate (D), nitrite (E), thiosulfate (F), or nitrate (G) as electron acceptor.

fml12304-sup-0002-TableS1-S3.docxWord document34K

Table S1. Amino acid sequence identity (ID), similarity (Sim), expect-value (e-value), N-terminal CXXC motif (CXXC motif), number of amino acid residues in the N-terminus (N-term length), and number of β-sheets in the C-terminus (No. β-sheets) of the MtrB homologs identified in the genomes of 22 metal-reducing Shewanella strains.

Table S2. Amino acid sequence identity (ID), similarity (Sim), expect-value (e-value),108mm N-terminal CXXC motif (CXXC motif), number of amino acid residues in the N-terminus (N-term length), and number of β-sheets in the C-terminus (No. β-sheets) of the three MtrB paralogs identified in the genome of Shewanella oneidensis MR-1.

Table S3. Phylogenetic affiliation (Class), amino acid sequence identity (ID, %), similarity (Sim, %), expect-value (e-value), N-terminal CXXC motif, (CXXC motif) number of amino acid residues in the N-terminus (N-term length), number of β-sheets in the C-terminus (No. β-sheets), and reported dissimilatory metal reduction or oxidation activity of the host strain (metal redox) for 52 MtrB homologs displaying similarity to Shewanella oneidensisMtrB.

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