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This study elucidates the role of ATP\u2010citrate lyase (ACLY), an essential enzyme in acetyl\u2010CoA production that uniquely localizes to the nucleus in oocytes and early embryos. Maternal\u00a0<jats:italic>Acly<\/jats:italic>\u00a0deletion in oocytes preserves fertility due to the compensatory upregulation of Acetyl\u2010CoA Synthetase 2 (ACSS2), whereas zygotic\u00a0<jats:italic>Acly<\/jats:italic>\u00a0knockout causes developmental arrest at the pre\u2010blastocyst stage without ACSS2 induction. Mechanistically, nuclear ACLY recruits and interacts with histone acetyltransferases, specifically E1A binding protein p300 (P300) and histone acetyltransferase 1 (HAT1), supplying acetyl\u2010CoA for histone acetylation to activate transcription, which is essential for embryogenesis. Clinically, enhanced ACLY nuclear localization correlates with superior quality of human embryos. Functionally, AKT\u2010mediated phosphorylation (Thr447\/Ser451\/Ser455) drives the nuclear translocation of ACLY and facilitates its interaction with HAT1 and P300. Inhibition of ACLY or its phosphorylation disrupts the promoting effects of AKT activators, such as insulin\u2010like growth factor\u20101 (IGF\u20101), on blastocyst formation. 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