PltM

Enzyme Information
reference: 10.1038/s41467-019-09215-9
host: E. coli BL21(DE3)
test: Crystallization , mutagenesis and in vitro assays (200 mM of either NaF (Assay 1a), NaCl (Assay 1b), NaBr (Assay 1c), or NaI (Assay 1d), 200 μL reaction with 300 mM NaF, substrate (0.5 mM), FAD (0.2 mM), NADPH (5 mM), PltM (5.5 μM), and SsuE (5.0 μM), 30 mM sodium phosphate pH 7.4)
phmm-model: FDH_all_conventional.hmm

Gene Data
phmm effect mutation gene_name reference
- inactive in vitro K87A PltM DOI: 10.1038/s41467-019-09215-9
- decreased efficiency for monochlorination and dichlorination L111Y PltM DOI: 10.1038/s41467-019-09215-9
- decreased efficiency compared to WT and only monochlorinated compounds S404Y PltM DOI: 10.1038/s41467-019-09215-9
33 substrate binding site P48 PltM DOI: 10.1038/s41467-019-09215-9
34 substrate binding site E49 PltM DOI: 10.1038/s41467-019-09215-9
57 substrate binding site K87 PltM DOI: 10.1038/s41467-019-09215-9
60 substrate binding site F90 PltM DOI: 10.1038/s41467-019-09215-9
364 substrate binding site W400 PltM DOI: 10.1038/s41467-019-09215-9
82 substrate binding site L111 PltM DOI: 10.1038/s41467-019-09215-9
466 substrate binding site K501 PltM DOI: 10.1038/s41467-019-09215-9
365 substrate binding site L401 PltM DOI: 10.1038/s41467-019-09215-9
367 substrate binding site N405 PltM DOI: 10.1038/s41467-019-09215-9
366 substrate binding site S404 PltM DOI: 10.1038/s41467-019-09215-9
296 FAD binding S331 PltM DOI: 10.1038/s41467-019-09215-9
154 FAD binding Q175 PltM DOI: 10.1038/s41467-019-09215-9
286 FAD binding Q321 PltM DOI: 10.1038/s41467-019-09215-9
153 FAD binding A173 PltM DOI: 10.1038/s41467-019-09215-9
24 FAD binding R39 PltM DOI: 10.1038/s41467-019-09215-9
290 flexible loop; changes conformation upon FAD binding F325 PltM DOI: 10.1038/s41467-019-09215-9
286 flexible loop; changes conformation upon FAD binding Q321 PltM DOI: 10.1038/s41467-019-09215-9
154 flexible loop; changes conformation upon FAD binding Q175 PltM DOI: 10.1038/s41467-019-09215-9
152 FAD binding; flexible loop; changes conformation upon FAD binding A174 PltM DOI: 10.1038/s41467-019-09215-9