Searching in Stenotrophomonas chelatiphaga DSM 21508 (GCF_001431535.1)
Found 3 curated entries in PaperBLAST's database that match '1.1.99.40' as complete word(s).
These curated entries have 2 distinct sequences.
Running ublast with E ≤ 0.01
Found 2 relevant proteins in Stenotrophomonas chelatiphaga DSM 21508, or try another query
ABB28_RS12370 ABB28_12405 WP_057508924.1: FAD-binding oxidoreductase is similar to: | PaperBLAST |
DLD2_YEAST / P46681: D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2; D-2HG--pyruvate transhydrogenase DLD2; Actin-interacting protein 2; D-lactate dehydrogenase [cytochrome] 2, mitochondrial; D-lactate ferricytochrome C oxidoreductase; D-LCR; EC 1.1.99.40; EC 1.1.2.4 from Saccharomyces cerevisiae | 36% id, 84% cov |
DLD3_YEAST / P39976: D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3; D-2HG--pyruvate transhydrogenase DLD3; (R)-2-hydroxyglutarate--pyruvate transhydrogenase; D-lactate dehydrogenase [cytochrome] 3; D-lactate ferricytochrome C oxidoreductase; D-LCR; EC 1.1.99.40; EC 1.1.2.4 from Saccharomyces cerevisiae | 33% id, 89% cov |
ABB28_RS06140 ABB28_06175 WP_057507800.1: FAD-linked oxidase C-terminal domain-containing protein is similar to: | PaperBLAST |
DLD3_YEAST / P39976: D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3; D-2HG--pyruvate transhydrogenase DLD3; (R)-2-hydroxyglutarate--pyruvate transhydrogenase; D-lactate dehydrogenase [cytochrome] 3; D-lactate ferricytochrome C oxidoreductase; D-LCR; EC 1.1.99.40; EC 1.1.2.4 from Saccharomyces cerevisiae | 27% id, 94% cov |
DLD2_YEAST / P46681: D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2; D-2HG--pyruvate transhydrogenase DLD2; Actin-interacting protein 2; D-lactate dehydrogenase [cytochrome] 2, mitochondrial; D-lactate ferricytochrome C oxidoreductase; D-LCR; EC 1.1.99.40; EC 1.1.2.4 from Saccharomyces cerevisiae | 28% id, 85% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 2 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory