One of the defining characters of insects is their mechanism of respiration: tracheae, an elaborate system of chitinized ectodermal tubules, delivering oxygen directly to tissues. While hemoglobins have been characterized in a few insects, the supposed adequacy of tracheae has led to the long-held assumption that insects do not require respiratory proteins. A comprehensive analysis of 845 Hexapod transcriptomes revealed the expression of hemoglobins in 32 orders of hexapods, including all 29 recognized orders of insects. Discovery of 1333 putative hemoglobins was achieved with target-gene BLAST searches of the NCBI TSA database, followed by verification via identification of functional residues, secondary- and tertiary-structure predictions, and localization predictions. While the majority of these hemoglobins are intracellular, extracellular hemoglobins were recovered in 38 species. Gene trees were constructed using multiple-sequence alignments and phylogenetic analyses. These results indicate duplication events within Insecta and a monophyletic grouping of hemoglobins outside other globin clades, for which we propose the term insectahemoglobins. Insectahemoglobins appear structurally convergent with and are phylogenetically adjacent to the clade of chordate myoglobins, cytoglobins, and hemoglobins. The co-option and derivation of insectahemoglobins from early neuroglobins may explain the widespread nature of hemoglobins in various kingdoms and phyla. It is hoped that these results can guide future work, including genome comparisons to transcriptome results, cell and tissue localization, experimental investigations of gene expression, and gas binding properties, to further illuminate the complex respiratory adaptations in insects.