ArticleProtein science : a publication of the Protein Society2022
Redefining the coenzyme A transferase superfamily with a large set of manually annotated proteins.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
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- Modulation of succinyl-CoA:3-ketoacid CoA transferase activity by a single amino acid residue in acetate:succinate CoA transferase from Trypanosoma brucei, the causative agent of African sleeping sickness.Protein science : a publication of the Protein Society · 2026Article
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- Insights into the nutritional value of honeybee drone larvae (Apis mellifera) through proteomic profiling.Scientific reports · 2024Article
- Enhancement of lactate fraction in poly(lactate-co-3-hydroxybutyrate) biosynthesized by metabolically engineered E. coli.Bioresources and bioprocessing · 2024Article
- The vast landscape of carbohydrate fermentation in prokaryotes.FEMS microbiology reviews · 2024Review
- The phenotype and genotype of fermentative prokaryotes.Science advances · 2023Article
- Analysis of Essential Isoprene Metabolic Pathway Proteins inApplied and environmental microbiology · 2023Article
- Structural Basis for a Cork-Up Mechanism of the Intra-Molecular Mesaconyl-CoA Transferase.Biochemistry · 2023Article
- Biosynthesis of Nodulisporic Acids: A Multifunctional Monooxygenase Delivers a Complex and Highly Branched Array.Angewandte Chemie (International ed. in English) · 2022Article
- Redefining the coenzyme A transferase superfamily with a large set of manually annotated proteins.Protein science : a publication of the Protein Society · 2022Article
- Succinyl-CoA:acetate CoA-transferase functioning in the oxidative tricarboxylic acid cycle inFrontiers in microbiology · 2022Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coenzyme A (CoA) transferases are a superfamily of proteins central to the metabolism of acetyl-CoA and other CoA thioesters. They are diverse group, catalyzing over a 100 biochemical reactions and spanning all three domains of life. A deeply rooted idea, proposed two decades ago, is these enzymes fall into three families (I, II, and III). Here we find they fall into different families, which we achieve by analyzing all CoA transferases characterized to date. We manually annotated 94 CoA transferases with functional information (including rates of catalysis for 208 reactions) from 97 publications. This represents all enzymes we could find in the primary literature, and it is double the number annotated in four protein databases (BRENDA, KEGG, MetaCyc, UniProt). We found family I transferases are not closely related to each other in terms of sequence, structure, and reactions catalyzed. This family is not even monophyletic. These problems are solved by regrouping the three families into six, including one family with many non-CoA transferases. The problem (and solution) became apparent only by analyzing our large set of manually annotated proteins. It would have been missed if we had used the small number of proteins annotated in UniProt and other databases. Our work is important to understanding the biology of CoA transferases. It also warns investigators doing phylogenetic analyses of proteins to go beyond information in databases.
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