Searching in Pseudomonas fluorescens FW300-N2E2 (pseudo6_N2E2)
Found 5 curated entries in PaperBLAST's database that match '5.3.3.18' as complete word(s).
These curated entries have 3 distinct sequences.
Running ublast with E ≤ 0.01
Found 17 relevant proteins in Pseudomonas fluorescens FW300-N2E2, or try another query
Pf6N2E2_1934: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 43% id, 96% cov |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 35% id, 97% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 34% id, 100% cov |
Pf6N2E2_1840: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 38% id, 100% cov |
Pf6N2E2_1834: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 37% id, 100% cov |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 36% id, 97% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 35% id, 97% cov |
Pf6N2E2_1147: Enoyl-CoA hydratase [valine degradation] (EC 4.2.1.17) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 37% id, 100% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 35% id, 100% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 35% id, 99% cov |
Pf6N2E2_5493: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 33% id, 95% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 35% id, 90% cov |
Pf6N2E2_1922: Enoyl-CoA hydratase (EC 4.2.1.17) / Delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase (EC 5.3.3.8) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) / 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 34% id, 89% cov |
Pf6N2E2_1835: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 38% id, 76% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 35% id, 77% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 35% id, 77% cov |
Pf6N2E2_1269: Enoyl-CoA hydratase [valine degradation] (EC 4.2.1.17) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 28% id, 98% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 27% id, 99% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 27% id, 98% cov |
Pf6N2E2_2290: Enoyl-CoA hydratase (EC 4.2.1.17) / Delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase (EC 5.3.3.8) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) / 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 30% id, 91% cov |
Pf6N2E2_1850: Enoyl-CoA hydratase [isoleucine degradation] (EC 4.2.1.17) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) / 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 32% id, 81% cov |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 29% id, 70% cov |
Pf6N2E2_742: 4-hydroxycinnamoyl CoA hydratase/lyase (Enoyl-CoA hydratase/lyase) (EC 4.2.1.17) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 27% id, 95% cov |
Pf6N2E2_1149: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 26% id, 98% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 32% id, 78% cov |
Pf6N2E2_6000: Enoyl-CoA hydratase [isoleucine degradation] (EC 4.2.1.17) / 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) / 3-hydroxybutyryl-CoA epimerase (EC 5.1.2.3) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 33% id, 67% cov |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 29% id, 74% cov |
Pf6N2E2_1046: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 25% id, 90% cov |
Pf6N2E2_1013: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli | 27% id, 81% cov |
Pf6N2E2_2773: Enoyl-CoA hydratase (EC 4.2.1.17) is similar to: | PaperBLAST |
H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila | 24% id, 87% cov |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 28% id, 72% cov |
Pf6N2E2_2078: hoxX-like protein is similar to: | PaperBLAST |
Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus | 28% id, 62% 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 17 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory