Small ruminant morbillivirus (SRMV), formerly named Peste-des-petits ruminanats virus (PPRV), belongs to the genus Morbillivirus genus in the family Paramyxoviridae and leads to a highly contagious disease in small ruminants, especially goats and sheep. Lysine succinylation is a newly identified and conserved modification and plays important roles in host cells response to pathogen infection. Herein, we present the comprehensive analysis of the succinylome of SRMV-infected Vero cell using quantitative proteomics. Overall, we identified 875 succinylated proteins with 2840 succinylation sites. Comparative analysis revealed that 139 down-regulated succinylated proteins with 228 succinylation sites and 38 up-regulated succinylated proteins with 44 succinylation sites were significant succinylated in response to SRMV infection, seven lysine succinylation motifs were identified. Bioinformatics analysis showed that the succinalated proteins mainly participated in in cellular respiration and biosynthetic process. Protein-protein interaction networks of the identified proteins provided further evidence that a variety of ATP synthase subunits and carbon metabolism were modulated by succinylation, the overlapped proteins between succinylation and acetylation are involved in glyoxylate and dicarboxylate metabolism. In summary, this is the first study of the succinylome in SRMV infection, lysine acetylation may have a more important effect than succinylation in PPRV infection. It provides a novel view on investigating the infection mechanism of SRMV.