Searching in Paraburkholderia bryophila 376MFSha3.1 (Burk376)
Found 8 curated entries in PaperBLAST's database that match '4.1.1.77' as complete word(s).
These curated entries have 7 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Paraburkholderia bryophila 376MFSha3.1, or try another query
H281DRAFT_01664: 2-oxo-3-hexenedioate decarboxylase is similar to: | PaperBLAST |
AMNE_PSESP / Q9KWS3: 4-oxalocrotonate decarboxylase; EC 4.1.1.77 from Pseudomonas sp. | 56% id, 96% cov |
nbaG / Q83V28: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Pseudomonas fluorescens | 51% id, 88% cov |
B0VXM8: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Geobacillus stearothermophilus | 45% id, 95% cov |
H281DRAFT_03253: 2-oxohept-3-enedioate hydratase is similar to: | PaperBLAST |
praD / C4TP06: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Paenibacillus sp. | 39% id, 99% cov |
B0VXM8: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Geobacillus stearothermophilus | 40% id, 95% cov |
Q1XGK3: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Pseudomonas putida | 36% id, 98% cov |
H281DRAFT_01663: 2-keto-4-pentenoate hydratase is similar to: | PaperBLAST |
praD / C4TP06: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Paenibacillus sp. | 39% id, 98% cov |
B0VXM8: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Geobacillus stearothermophilus | 39% id, 95% cov |
xylI / P49155: 4-oxalocrotonate decarboxylase subunit (EC 4.1.1.77) from Pseudomonas putida | 37% id, 100% cov |
H281DRAFT_05455: 2-keto-4-pentenoate hydratase is similar to: | PaperBLAST |
praD / C4TP06: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Paenibacillus sp. | 35% id, 96% cov |
B0VXM8: 2-oxo-3-hexenedioate decarboxylase (EC 4.1.1.77) from Geobacillus stearothermophilus | 29% id, 99% 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