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Nitrate reductase NarGHI is a known virulence factor for this pathogen. This enzyme complex serves as the terminal electron acceptor in anaerobic respiration in other pathogens, such as the phylogenetically related\n                    <jats:italic>Mycobacterium tuberculosis<\/jats:italic>\n                    . A recent study demonstrated that\n                    <jats:italic>R. equi<\/jats:italic>\n                    survives under anaerobic conditions. In this work, we endeavored to uncover the electron transport chain complexes of\n                    <jats:italic>R. equi<\/jats:italic>\n                    . By in silico comparison to known complexes in the Transporter Classification Database, 67 putative respiratory chain proteins were identified in\n                    <jats:italic>R. equi<\/jats:italic>\n                    103S. Their distribution was evaluated in the genomes of 37 clinical (animal and human infections) and 297 non-clinical (environmental)\n                    <jats:italic>Rhodococcus<\/jats:italic>\n                    isolates from the NCBI RefSeq database. NarGHI subunits were found in 100% of clinical and 35% of non-clinical genomes. Loci encoding four potential electron donor complexes (a membrane-bound formate dehydrogenase, a succinate dehydrogenase, and two Ni-Fe hydrogenases) were present in &gt;\u200980% of clinical and &lt;\u200950% of non-clinical isolates. Loci encoding a nitric oxide reductase, a potential terminal electron acceptor, were identified in 40.5% of clinical and 2% of non-clinical isolates. The results show that the respiratory chain in\n                    <jats:italic>R. equi<\/jats:italic>\n                    is highly complex, and point to potential metabolic adaptations of this species to hypoxic conditions.\n                  <\/jats:p>","DOI":"10.1007\/s11274-026-05110-w","type":"journal-article","created":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T08:13:34Z","timestamp":1783152814000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Adaptations in electron transport chain complexes of clinical Rhodococcus equi revealed through comparative genomics"],"prefix":"10.1007","volume":"42","author":[{"given":"Jo\u00e3o Pedro Vasques","family":"da Concei\u00e7\u00e3o","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0692-4939","authenticated-orcid":false,"given":"Fabio Faria","family":"da Mota","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,7,4]]},"reference":[{"key":"5110_CR1","doi-asserted-by":"publisher","first-page":"493","DOI":"10.1038\/s41586-024-07487-w","volume":"630","author":"J Abramson","year":"2024","unstructured":"Abramson J, Adler J, Dunger J, Evans R, Green T, Pritzel A, Ronneberger O, Willmore L, Ballard AJ, Bambrick J et al (2024) Accurate structure prediction of biomolecular interactions with AlphaFold 3. 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