Searching in Shewanella sp. ANA-3 (ANA3)
Found 3 curated entries in PaperBLAST's database that match 'propionyl-CoA synthetase' as complete word(s).
These curated entries have 2 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Shewanella sp. ANA-3, or try another query
| Shewana3_1675: AMP-dependent synthetase and ligase (RefSeq) is similar to: | PaperBLAST |
YahU / b0335: propionyl-CoA synthetase (EC 6.2.1.17) from Escherichia coli | 45% id, 99% cov |
PRPE_SALTY / P55912: Propionate--CoA ligase; Propionyl-CoA synthetase; EC 6.2.1.17 from Salmonella typhimurium | 44% id, 99% cov |
| Shewana3_2523: acetyl-CoA synthetase (RefSeq) is similar to: | PaperBLAST |
YahU / b0335: propionyl-CoA synthetase (EC 6.2.1.17) from Escherichia coli | 38% id, 99% cov |
PRPE_SALTY / P55912: Propionate--CoA ligase; Propionyl-CoA synthetase; EC 6.2.1.17 from Salmonella typhimurium | 37% id, 99% cov |
| Shewana3_2475: AMP-binding domain protein (RefSeq) is similar to: | PaperBLAST |
PRPE_SALTY / P55912: Propionate--CoA ligase; Propionyl-CoA synthetase; EC 6.2.1.17 from Salmonella typhimurium | 24% id, 84% cov |
YahU / b0335: propionyl-CoA synthetase (EC 6.2.1.17) from Escherichia coli | 35% id, 11% cov |
| Shewana3_2713: peptide synthase (RefSeq) is similar to: | PaperBLAST |
YahU / b0335: propionyl-CoA synthetase (EC 6.2.1.17) from Escherichia coli | 24% id, 79% cov |
PRPE_SALTY / P55912: Propionate--CoA ligase; Propionyl-CoA synthetase; EC 6.2.1.17 from Salmonella typhimurium | 24% id, 73% cov |
| Shewana3_2386: long-chain-fatty-acid--CoA ligase (RefSeq) is similar to: | PaperBLAST |
PRPE_SALTY / P55912: Propionate--CoA ligase; Propionyl-CoA synthetase; EC 6.2.1.17 from Salmonella typhimurium | 23% id, 55% cov |
YahU / b0335: propionyl-CoA synthetase (EC 6.2.1.17) from Escherichia coli | 26% id, 44% 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 4 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory