<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Mingnan Qu</submitter><species>Glycine Max</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0016878000</full_dataset_link><submitter_email>qmn@yzu.edu.cn</submitter_email><submitter_affiliation>College of Agriculture</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>Raw mass spectrometry data for the identification of GmGNAT10 as a key acetyltransferase mediating acetylation modification of Rubisco in soybean</name><description>Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco), the core rate-limiting enzyme of photosynthetic carbon metabolism, is regulated by acetylation, yet its upstream acetyltransferases remain largely uncharacterized. Here, we identified a novel soybean acetyltransferase GmGNAT10, which interacts with Rubisco and other photosynthetic enzymes via IP-MS/MS interactomics. Quantitative acetylomics under fluctuating light revealed dramatic genotypic differences in acetylation levels of key RbcL lysine residues (K23, K175, K236) between wild-type and GmGNAT10 mutants. Our findings expand the mechanistic understanding of chloroplast non-histone acetylation in fine-tuning photosynthetic carbon metabolism.</description><dates><publication>Tue Apr 28 00:00:00 GMT+01:00 2026</publication></dates><accession>PXD077705</accession><cross_references><TAXONOMY>3847</TAXONOMY></cross_references></HashMap>