Beauveria　bassiana　is　a　popular　and　eco-friendly　biopesticide.　During　its　pathogen-pest　interaction,　both　N-acetylglucosamine　(GlcNAc)　catabolism　and　anabolism　are　crucial　for　nutrient　supply　and　cell-wall　construction.　The　initiation　of　GlcNAc　metabolism　relies　on　the　catalysis　of　GlcNAc　kinase,　which　has　been　extensively　studied　in　the　human　pathogen　Candida　albicans.　However,　the　physiological　function　of　GlcNAc　kinase　remains　poorly　understood　in　entomopathogenic　fungi.　In　the　present　study,　a　GlcNAc　kinase　homolog　was　identified　and　designated　as　BbHxk1　in　B.　bassiana.　Deletion　of　BbHxk1　resulted　in　viable　but　reduced　vegetative　growth　on　various　carbon　sources.　Delta　BbHxk1　mutants　displayed　severe　defects　in　cell　wall　integrity,　making　them　more　susceptible　to　cell　wall　stress　cues.　Furthermore,　the　absence　of　BbHxk1　resulted　in　an　increase　in　conidial　yield　and　blastospore　production,　and　a　faster　rate　of　germination　and　filamentation,　potentially　attributed　to　higher　intracellular　ATP　levels.　BbHxk1　deficiency　led　to　a　reduction　in　the　activities　of　cuticle-degrading　enzymes,　which　might　contribute　to　the　attenuated　pathogenicity　specifically　through　cuticle　penetration　rather　than　hemocoel　infection　towards　Galleria　mellonella　larvae.　Being　different　from　C.　albicans　Hxk1,　which　facultatively　acts　as　a　catalyzing　enzyme　and　transcriptional　regulator,　BbHxk1　primarily　acts　as　a　catalyzing　enzyme　and　metabolic　regulator.　The　altered　metabolomic　profiling　correlated　with　the　phenotypic　defects　in　Delta　BbHxk1　mutants,　further　implicating　a　potential　metabolism-dependent　mechanism　of　BbHxk1　in　mediating　physiologies　of　B.　bassiana.　These　findings　not　only　unveil　a　novel　role　for　GlcNAc　kinase　in　B.　bassiana,　but　also　provide　a　solid　theoretical　basis　to　guide　metabolic　reprogramming　in　order　to　maintain　or　even　enhance　the　efficiency　of　fungi　for　practical　applications.