Searching in Pseudomonas fluorescens GW456-L13 (pseudo13_GW456_L13)
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 4 relevant proteins in Pseudomonas fluorescens GW456-L13, or try another query
PfGW456L13_1214: Alcohol dehydrogenase (EC 1.1.1.1) is similar to: | PaperBLAST |
rhaZ / Q8ZKS2: L-lactaldehyde reductase (EC 1.1.1.77) from Salmonella typhimurium | 39% id, 99% cov |
FUCO_ECOLI / P0A9S1: Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli | 39% id, 97% cov |
BT3767: L-lactaldehyde reductase FucO (EC 1.1.1.77) from Bacteroides thetaiotaomicron | 38% id, 97% cov |
PfGW456L13_3512: Alcohol dehydrogenase (EC 1.1.1.1); Acetaldehyde dehydrogenase (EC 1.2.1.10) is similar to: | PaperBLAST |
BT3767: L-lactaldehyde reductase FucO (EC 1.1.1.77) from Bacteroides thetaiotaomicron | 37% id, 97% cov |
FUCO_ECOLI / P0A9S1: Lactaldehyde reductase; Propanediol oxidoreductase; EC 1.1.1.77 from Escherichia coli | 36% id, 99% cov |
rhaZ / Q8ZKS2: L-lactaldehyde reductase (EC 1.1.1.77) from Salmonella typhimurium | 36% id, 98% cov |
PfGW456L13_2712: Alcohol dehydrogenase (EC 1.1.1.1) is similar to: | PaperBLAST |
rhaZ / Q8ZKS2: L-lactaldehyde reductase (EC 1.1.1.77) from Salmonella typhimurium | 34% id, 97% 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 | 30% id, 97% cov |
PfGW456L13_3171: Short-chain dehydrogenase/reductase SDR 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, 32% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory