Searching in Acidovorax sp. GW101-3H11 (acidovorax_3H11)
Found 7 curated entries in PaperBLAST's database that match '1.1.1.77' as complete word(s).
These curated entries have 5 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Acidovorax sp. GW101-3H11, or try another query
| Ac3H11_2497: Alcohol dehydrogenase (EC 1.1.1.1) is similar to: | PaperBLAST |
rhaZ / Q8ZKS2: L-lactaldehyde reductase (EC 1.1.1.77) from Salmonella typhimurium | 35% id, 92% cov |
BT3767: L-lactaldehyde reductase FucO (EC 1.1.1.77) from Bacteroides thetaiotaomicron | 33% id, 95% cov |
FUCO_ECOLI / P0A9S1: Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli | 32% id, 96% cov |
| Ac3H11_4515: NADH-dependent butanol dehydrogenase A (EC 1.1.1.-) is similar to: | PaperBLAST |
rhaZ / Q8ZKS2: L-lactaldehyde reductase (EC 1.1.1.77) from Salmonella typhimurium | 28% id, 92% cov |
BT3767: L-lactaldehyde reductase FucO (EC 1.1.1.77) from Bacteroides thetaiotaomicron | 25% id, 95% cov |
FUCO_ECOLI / P0A9S1: Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli | 24% id, 94% cov |
| Ac3H11_1071: Dihydroflavonol-4-reductase (EC 1.1.1.219) is similar to: | PaperBLAST |
YLL056C / Q12177: NADH-dependent aldehyde reductase (EC 1.1.1.77; EC 1.1.1.244; EC 1.1.1.1) from Saccharomyces cerevisiae | 22% id, 83% cov |
| Ac3H11_3518: Rrf2-linked NADH-flavin reductase is similar to: | PaperBLAST |
YLL056C / Q12177: NADH-dependent aldehyde reductase (EC 1.1.1.77; EC 1.1.1.244; EC 1.1.1.1) from Saccharomyces cerevisiae | 28% id, 36% cov |
| Ac3H11_1578: 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) is similar to: | PaperBLAST |
YLL056C / Q12177: NADH-dependent aldehyde reductase (EC 1.1.1.77; EC 1.1.1.244; EC 1.1.1.1) from Saccharomyces cerevisiae | 36% id, 23% 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 5 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory