Table 1.
Percent identities between representative PbfB, PbfC, and PbfD enzymes and the most similar enzymes of known function
| PuuB | MabO | ThiO | SolA | SarDH | DadA | SoxA | |
|---|---|---|---|---|---|---|---|
| PbfB V. vulnificus | 31.2% | 28.6% | 25.7% | 23.1% | 24.7% | 22.4% | 22.8% |
| PbfC Azospirillum sp. B510 | 25.8% | 30.2% | 27.6% | 24.5% | 26.5% | 22.2% | 27.7% |
| PbfD1 A. baumannii | 23.4% | 24.5% | 25.2% | 23.9% | 20.6% | 22.9% | 25.0% |
| PbfD2 M. fucicola | 25.7% | 23.1% | 24.9% | 27.2% | 24.9% | 23.8% | 22.5% |
The enzymes of known function are: PuuB, γ-glutamyl putrescine oxidase from E. coli35; MabO, 4-methylamino butyrate oxidase from Arthrobacter nicotinovorans36; ThiO, glycine oxidase from Bacillus licheniformis37; SolA, N-methyl-L-tryptophan oxidase from E. coli38; SarDH, sarcosine dehydrogenase from Rattus norvegicus39; DadA, D-amino acid dehydrogenase from Helicobacter pylori40; SoxA, sarcosine oxidase from Bacillus sp. B-0618.41 The GenBank accession IDs for these enzymes are found in Table S2 and the reactions they catalyze are shown in Figure S4. Percent identities were evaluated by the pairwise global alignment of the portions of the sequences denoting the PF01266 domain, carried out with Needle (https://www.ebi.ac.uk/Tools/psa/emboss_needle/) with a Blosum30 substitution matrix. Percent identities rarely exceed 30%, indicative of only distant homologies between the oxidoreductases described in this study and the other functionally characterized PF01266 enzymes. A more refined analysis of the evolutionary relationships between the enzymes in this table is provided in Figure S5. Related to Table S2, Figures S4 and S5.