Searching in Rhodobacter viridis JA737 (GCF_003217355.1)
Found 10 curated entries in PaperBLAST's database that match '2.3.1.223' as complete word(s).
These curated entries have 7 distinct sequences.
Running ublast with E ≤ 0.01
Found 7 relevant proteins in Rhodobacter viridis JA737, or try another query
C8J30_RS05090 C8J30_102367 WP_110804635.1: acetyl-CoA C-acyltransferase family protein is similar to: | PaperBLAST |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 50% id, 100% cov |
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 | 48% 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 |
C8J30_RS12155 C8J30_10967 WP_110806117.1: acetyl-CoA C-acetyltransferase 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 | 44% id, 99% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 43% 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 | 42% id, 100% cov |
C8J30_RS14960 C8J30_11447 WP_110806646.1: acetyl-CoA C-acyltransferase 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 | 41% id, 100% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 40% 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 | 40% id, 100% cov |
C8J30_RS06880 C8J30_103295 WP_110804969.1: acetyl-CoA C-acetyltransferase is similar to: | PaperBLAST |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 40% id, 100% cov |
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 | 40% 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 | 40% id, 100% cov |
fabF C8J30_RS03100 C8J30_101626 WP_110804222.1: beta-ketoacyl-ACP synthase II 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 | 21% id, 68% cov |
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 | 41% id, 12% cov |
C8J30_RS01885 C8J30_101388 WP_110804019.1: beta-ketoacyl-[acyl-carrier-protein] synthase family protein 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 | 26% id, 34% 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 | 36% id, 14% cov |
C8J30_RS14245 C8J30_11287 WP_110806510.1: IS3 family transposase is similar to: | PaperBLAST |
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 | 32% id, 12% 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