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<i>Magnaporthe oryzae</i> is the causal agent of rice blast outbreaks. L-ascorbic acid (ASC) is a famous antioxidant found in nature. However, while ASC is rare or absent in fungi, a five-carbon analog, D-erythroascorbic acid (EASC), seems to appear to be a substitute for ASC. Although the antioxidant function of ASC has been widely described, the specific properties and physiological functions of EASC remain poorly understood. In this study, we identified a D-arabinono-1,4-lactone oxidase (ALO) domain-containing protein, MoAlo1, and found that MoAlo1 was localized to mitochondria. Disruption of <i>MoALO1</i> (Δ<i>Moalo1</i>) exhibited defects in vegetative growth as well as conidiogenesis. The Δ<i>Moalo1</i> mutant was found to be more sensitive to exogenous H₂O₂. Additionally, the pathogenicity of conidia in the Δ<i>Moalo1</i> null mutant was reduced deeply in rice, and defective penetration of appressorium-like structures (ALS) formed by the hyphal tips was also observed in the Δ<i>Moalo1</i> null mutant. When exogenous EASC was added to the conidial suspension, the defective pathogenicity of the Δ<i>Moalo1</i> mutant was restored. Collectively, MoAlo1 is essential for growth, conidiogenesis, and pathogenicity in <i>M. oryzae.</i>