Curated BLAST
Searching in Brucella microti CCM 4915 (GCF_000022745.1)
Found 11 curated entries in PaperBLAST's database that match '2.3.1.174' as complete word(s).
These curated entries have 9 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Brucella microti CCM 4915, or try another query
pcaF BMI_RS13025 BMI_II633 WP_002968962.1: 3-oxoadipyl-CoA thiolase
is similar to: | PaperBLAST |
pcaF / Q0K4S3: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Cupriavidus necator | 74% 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 | 73% 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 | 72% id,
100% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 72% id,
100% cov |
pcaF / Q51956: subunit of β-ketoadipyl CoA thiolase (EC 2.3.1.174; EC 2.3.1.16) from Pseudomonas putida | 68% 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
YdbW / b1397: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli
paaJ / P0C7L2: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli | 67% id,
100% cov |
PCAF_PSEKB / Q8VPF1: Beta-ketoadipyl-CoA thiolase; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 from Pseudomonas knackmussii | 67% id,
99% 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 | 67% id,
100% cov |
Tfu_0875 / Q47RK4: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Thermobifida fusca | 56% id,
100% cov |
More... |
BMI_RS08205 BMI_I1790 WP_004689226.1: 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. | 48% id,
99% cov |
PCAF_PSEKB / Q8VPF1: Beta-ketoadipyl-CoA thiolase; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 from Pseudomonas knackmussii | 47% id,
99% 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 | 46% id,
99% 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,
99% cov |
pcaF / Q51956: subunit of β-ketoadipyl CoA thiolase (EC 2.3.1.174; EC 2.3.1.16) from Pseudomonas putida | 45% id,
100% 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 | 45% id,
99% cov |
Tfu_0875 / Q47RK4: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Thermobifida fusca | 44% 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
YdbW / b1397: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli
paaJ / P0C7L2: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli | 44% id,
100% cov |
pcaF / Q0K4S3: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Cupriavidus necator | 44% id,
99% cov |
More... |
BMI_RS13755 BMI_II788 WP_004687161.1: acetyl-CoA C-acetyltransferase
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
YdbW / b1397: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli
paaJ / P0C7L2: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli | 39% id,
100% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 38% id,
100% cov |
pcaF / Q0K4S3: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Cupriavidus necator | 38% 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 | 38% 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 | 38% id,
100% cov |
pcaF / Q51956: subunit of β-ketoadipyl CoA thiolase (EC 2.3.1.174; EC 2.3.1.16) from Pseudomonas putida | 37% id,
100% cov |
PCAF_PSEKB / Q8VPF1: Beta-ketoadipyl-CoA thiolase; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 from Pseudomonas knackmussii | 37% id,
99% 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 | 37% id,
100% cov |
Tfu_0875 / Q47RK4: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Thermobifida fusca | 36% id,
100% cov |
More... |
BMI_RS12165 BMI_II445 WP_004685006.1: 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 | 39% id,
99% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 39% id,
99% cov |
Tfu_0875 / Q47RK4: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Thermobifida fusca | 38% id,
99% cov |
pcaF / Q51956: subunit of β-ketoadipyl CoA thiolase (EC 2.3.1.174; EC 2.3.1.16) from Pseudomonas putida | 38% id,
99% 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 | 38% id,
99% cov |
PCAF_PSEKB / Q8VPF1: Beta-ketoadipyl-CoA thiolase; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 from Pseudomonas knackmussii | 37% id,
100% cov |
pcaF / Q0K4S3: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Cupriavidus necator | 38% id,
99% 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 | 38% id,
99% 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
YdbW / b1397: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli
paaJ / P0C7L2: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli | 37% id,
99% cov |
More... |
fabF BMI_RS02135 BMI_I463 WP_004689504.1: 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 | 24% id,
72% cov |
paaJ / Q845J8: β-ketoadipyl-CoA thiolase (EC 2.3.1.174; EC 2.3.1.223) from Pseudomonas sp. | 25% id,
48% cov |
PCAF_PSEKB / Q8VPF1: Beta-ketoadipyl-CoA thiolase; 3-oxoadipyl-CoA thiolase; EC 2.3.1.174 from Pseudomonas knackmussii | 35% id,
17% cov |
pcaF / Q0K4S3: 3-oxoadipyl-CoA thiolase (EC 2.3.1.174) from Cupriavidus necator | 40% id,
14% 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 | 37% id,
14% 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
YdbW / b1397: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli
paaJ / P0C7L2: β-ketoadipyl-CoA thiolase (EC 2.3.1.223; EC 2.3.1.174) from Escherichia coli | 46% id,
11% 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 | 38% id,
13% cov |
More... |
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.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory