ArticleBMC bioinformatics2013
LUD, a new protein domain associated with lactate utilization.
Article in BMC bioinformatics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Identification of biofilm-associated genes inBiofilm · 2026Article
- The L-lactate dehydrogenase LldD contributes to oxidative stress resistance, survival from neutrophils, and host colonization inInfection and immunity · 2026Article
- D- and L-lactate consumers are taxonomically, biochemically, and energetically different.ISME communications · 2026Article
- A single-nucleotide variant conditions the ability vs. inability ofApplied and environmental microbiology · 2025Article
- Carbon upshift inmBio · 2025Article
- Aerobic adaptation and metabolic dynamics ofmSystems · 2024Article
- Comparative genomics ofFrontiers in microbiology · 2024Article
- Comparative genomic analysis reveals differential genomic characteristics and featured genes between rapid- and slow-growingFrontiers in microbiology · 2023Article
- Unraveling Anaerobic Metabolisms in a Hypersaline Sediment.Frontiers in microbiology · 2022Article
- Key Enzymes for Anaerobic Lactate Metabolism in Geobacter sulfurreducens.Applied and environmental microbiology · 2021Article
- Metabolic activity analyses demonstrate that Lokiarchaeon exhibits homoacetogenesis in sulfidic marine sediments.Nature microbiology · 2020Article
- Sulfate-Reducing Bacteria That Produce Exopolymers Thrive in the Calcifying Zone of a Hypersaline Cyanobacterial Mat.Frontiers in microbiology · 2019Article
- Changes in protein abundance are observed in bacterial isolates from a natural host.Frontiers in cellular and infection microbiology · 2015Article
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Authors and funding
13 authors.
Funding
Abstract
backgroundA novel highly conserved protein domain, DUF162 [Pfam: PF02589], can be mapped to two proteins: LutB and LutC. Both proteins are encoded by a highly conserved LutABC operon, which has been implicated in lactate utilization in bacteria. Based on our analysis of its sequence, structure, and recent experimental evidence reported by other groups, we hereby redefine DUF162 as the LUD domain family.
resultsJCSG solved the first crystal structure [PDB:2G40] from the LUD domain family: LutC protein, encoded by ORF DR_1909, of Deinococcus radiodurans. LutC shares features with domains in the functionally diverse ISOCOT superfamily. We have observed that the LUD domain has an increased abundance in the human gut microbiome.
conclusionsWe propose a model for the substrate and cofactor binding and regulation in LUD domain. The significance of LUD-containing proteins in the human gut microbiome, and the implication of lactate metabolism in the radiation-resistance of Deinococcus radiodurans are discussed.
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