Searching in Escherichia coli BW25113 (Keio)
Found 10 curated entries in PaperBLAST's database that match '2.3.1.223' as complete word(s).
These curated entries have 8 distinct sequences.
Running ublast with E ≤ 0.01
Found 7 relevant proteins in Escherichia coli BW25113, or try another query
b1397: acetyl-CoA acetyltransferase (NCBI) is similar to: | PaperBLAST |
PAAJ_ECOLI / P0C7L2: 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase; EC 2.3.1.174; EC 2.3.1.223 from Escherichia coli | 100% id, 100% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 71% id, 100% cov |
H281DRAFT_05723: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Paraburkholderia bryophila | 69% id, 100% cov |
b1391: predicted multicomponent oxygenase/reductase subunit for phenylacetic acid degradation (RefSeq) is similar to: | PaperBLAST |
Q845J3: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223) from Pseudomonas sp. | 53% id, 90% cov |
b2224: acetyl-CoA acetyltransferase (NCBI) is similar to: | PaperBLAST |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 48% id, 100% cov |
H281DRAFT_05723: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Paraburkholderia bryophila | 47% id, 100% cov |
BPHYT_RS17345: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Burkholderia phytofirmans | 47% id, 100% cov |
b2844: putative acyltransferase (VIMSS) is similar to: | PaperBLAST |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 47% id, 100% cov |
H281DRAFT_05723: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Paraburkholderia bryophila | 46% id, 100% cov |
BPHYT_RS17345: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Burkholderia phytofirmans | 45% id, 100% cov |
b3845: acetyl-CoA acetyltransferase (NCBI) is similar to: | PaperBLAST |
HSERO_RS20660: bifunctional thiolase PaaJ: 3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Herbaspirillum seropedicae | 45% id, 100% cov |
H281DRAFT_05723: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Paraburkholderia bryophila | 44% id, 100% cov |
BPHYT_RS17345: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Burkholderia phytofirmans | 43% id, 100% cov |
b2342: acetyl-CoA acetyltransferase (NCBI) is similar to: | PaperBLAST |
PAAJ_ECOLI / P0C7L2: 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase; EC 2.3.1.174; EC 2.3.1.223 from Escherichia coli | 33% id, 98% cov |
HSERO_RS20660: bifunctional thiolase PaaJ: 3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Herbaspirillum seropedicae | 33% id, 98% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 33% id, 98% cov |
b1095: 3-oxoacyl-(acyl carrier protein) synthase (NCBI) is similar to: | PaperBLAST |
H281DRAFT_05723: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Paraburkholderia bryophila | 36% id, 17% cov |
BPHYT_RS17345: bifunctional thiolase PaaJ: 3-oxo-5,6-didehydrosuberyl-CoA thiolase (EC 2.3.1.223); 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Burkholderia phytofirmans | 36% id, 17% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 36% id, 15% 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 7 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory