Nitrotoxin metabolism in bacteria may have emerged from a diverse oxidoreductase reservoir

Authors

Barman, P., Sinha, S., Chakraborty, R.

Abstract

Bacterial transformation of 3 nitropropionic acid (3NPA) is typically viewed through canonical nitronate monooxygenases (NMOs), yet sequence annotation poorly resolves function across this flavoprotein family. Here we show that the environmental YrpB/NMO associated oxidoreductase space is dominated by YrpB related proteins: across 13 metagenomes, 83.1% of 390 conserved domain supported candidates were YrpB-associated. Cultivation along an Eisenia fetida feed gut cast continuum recovered 31 phylogenetically diverse 3NPA responsive bacteria, revealing that this phenotype is distributed across multiple lineages. Using the previously genome-sequenced Serratia sp. EWG9 as a tractable exemplar, we demonstrate sustained 3NPA supported growth, 44% parent compound depletion and a broad early transcriptional reorganization. Its focal oxidoreductase OXR01 occupies overlapping YrpB/NMO sequence space and shows stable predicted 3NPA accommodation without strong transcriptional induction. These findings reposition canonical NMOs as one component of a broader, ecologically distributed oxidoreductase reservoir for bacterial nitrotoxin responsiveness.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 18 Sep 2026.

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