Searching in Paraburkholderia bryophila 376MFSha3.1 (Burk376)
Found 7 curated entries in PaperBLAST's database that match '4.3.1.1' as complete word(s).
These curated entries have 4 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Paraburkholderia bryophila 376MFSha3.1, or try another query
H281DRAFT_04314: fumarase, class II is similar to: | PaperBLAST |
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp. | 43% id, 98% cov |
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni | 41% id, 98% cov |
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa | 43% id, 91% cov |
H281DRAFT_00025: fumarase, class II is similar to: | PaperBLAST |
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp. | 40% id, 99% cov |
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni | 37% id, 98% cov |
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa | 37% id, 98% cov |
H281DRAFT_02592: fumarase, class II is similar to: | PaperBLAST |
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp. | 40% id, 99% cov |
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni | 38% id, 99% cov |
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa | 37% id, 95% cov |
H281DRAFT_01595: 3-carboxy-cis,cis-muconate cycloisomerase is similar to: | PaperBLAST |
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa | 26% id, 88% cov |
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp. | 22% id, 70% cov |
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni | 24% id, 60% cov |
H281DRAFT_02594: 3-carboxy-cis,cis-muconate cycloisomerase is similar to: | PaperBLAST |
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni | 25% id, 43% 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 6 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory