Archaeal genomes used in the study "Unique minimal and hybrid hydrogenases are active from anaerobic archaea".

Unique minimal and hybrid hydrogenases are active from anaerobic archaeaChris Greening1,9 * #, Princess R. Cabotaje2 #, Luis E. Valentin Alvarado3 #, Pok Man Leung1 #, Henrik Land2, Thiago Rodrigues-Oliveira4, Rafael I. Ponce-Toledo4, Moritz Senger2, Max A. Klamke2, Michael Milton1, Rachael Lappan1, Susan Mullen3, Jacob West-Roberts3, Jie Mao1,5, Jiangning Song5, Marie Schoelmerich3, Courtney W. Stairs6, Christa Schleper4, Rhys Grinter1 *, Anja Spang7,8 *, Jillian F. Banfield1,3 *, Gustav Berggren2 *SummaryMicrobial hydrogen (H2) cycling underpins the diversity and functionality of diverse anoxic ecosystems. Among the three evolutionarily distinct hydrogenase superfamilies responsible, [FeFe]-hydrogenases were thought to be restricted to bacteria and eukaryotes. Here we show that anaerobic archaea encode diverse, active, and ancient lineages of [FeFe]-hydrogenases through combining analysis of existing and new genomes with extensive biochemical experiments. [FeFe]-hydrogenases are encoded by genomes of nine archaeal phyla and expressed by H2-producing Asgard archaeon cultures. We report a novel ultra-minimal hydrogenase in DPANN archaea that binds the catalytic H-cluster and produces H2. Moreover, we identified and characterised remarkable hybrid complexes formed through the fusion of [FeFe]- and [NiFe]-hydrogenases in ten other archaeal orders. Phylogenetic analysis and structural modelling suggest a deep evolutionary history of hybrid hydrogenases. These findings reveal new metabolic adaptations of archaea, streamlined H2 catalysts for biotechnological development, and a surprisingly intertwined evolutionary history between the two major H2-metabolizing enzymes.