biostudies-literatureSmith AJwelcome trust-nihNEI NIH HHSnational eye instituteNational Institutes of Health68https://www.ebi.ac.uk/biostudies/studies/S-EPMC8935817biostudies-literatureUnknown20(1)<h4>Background</h4>Functional complexity of the eukaryotic mitochondrial proteome is augmented by independent gene acquisition from bacteria since its endosymbiotic origins. Mammalian homologs of many ancestral mitochondrial proteins have uncharacterized catalytic activities. Recent forward genetic approaches attributed functions to proteins in established metabolic pathways, thereby limiting the possibility of identifying novel biology relevant to human disease. We undertook a bottom-up biochemistry approach to discern evolutionarily conserved mitochondrial proteins with catalytic potential.<h4>Results</h4>Here, we identify a Parkinson-associated DJ-1/PARK7-like protein-glutamine amidotransferase-like class 1 domain-containing 3A (GATD3A), with bacterial evolutionary affinities although nBMC biologyGATD3A, a mitochondrial deglycase with evolutionary origins from gammaproteobacteria, restricts the formation of advanced glycation end products.PMC8935817ZIAEY000450106820/Z/15/ZZIAEY000546Advani JKennedy BDong LBrock DCNellissery JGumerson JAravind LSwaroop ASmith AJfalseGATD3A, a mitochondrial deglycase with evolutionary origins from gammaproteobacteria, restricts the formation of advanced glycation end products.<h4>Background</h4>Functional complexity of the eukaryotic mitochondrial proteome is augmented by independent gene acquisition from bacteria since its endosymbiotic origins. Mammalian homologs of many ancestral mitochondrial proteins have uncharacterized catalytic activities. Recent forward genetic approaches attributed functions to proteins in established metabolic pathways, thereby limiting the possibility of identifying novel biology relevant to human disease. We undertook a bottom-up biochemistry approach to discern evolutionarily conserved mitochondrial proteins with catalytic potential.<h4>Results</h4>Here, we identify a Parkinson-associated DJ-1/PARK7-like protein-glutamine amidotransferase-like class 1 domain-containing 3A (GATD3A), with bacterial evolutionary affinities although n2022-01-01T00:00:00Z2022 Mar2025-04-04T12:56:28.401Z2024-12-03T16:03:33.439ZS-EPMC89358173530702910.1186/s12915-022-01267-6