Searching in Sinorhizobium meliloti 1021 (Smeli)
Found 56 curated entries in PaperBLAST's database that match '4.1.1.19' as complete word(s).
These curated entries have 40 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Sinorhizobium meliloti 1021, or try another query
| SMa0682: decarboxylase (lysine, ornithine, arginine) is similar to: | PaperBLAST |
E8X9U7: arginine decarboxylase (EC 4.1.1.19) from Salmonella enterica | 39% id, 99% cov |
ADIA_ECOLI / P28629: Biodegradative arginine decarboxylase; ADC; EC 4.1.1.19 from Escherichia coli | 38% id, 98% cov |
Q5NT93: arginine decarboxylase (EC 4.1.1.19) from Selenomonas ruminantium | 28% id, 33% cov |
| SMa0680: amino acid (ornithine, lysine, arginine) decarboxylase is similar to: | PaperBLAST |
E8X9U7: arginine decarboxylase (EC 4.1.1.19) from Salmonella enterica | 33% id, 89% cov |
ADIA_ECOLI / P28629: Biodegradative arginine decarboxylase; ADC; EC 4.1.1.19 from Escherichia coli | 33% id, 90% cov |
Q5NT93: arginine decarboxylase (EC 4.1.1.19) from Selenomonas ruminantium | 35% id, 10% cov |
| SMc02983: ornithine, DAP, or arginine decarboxylase is similar to: | PaperBLAST |
ADC / Q96A70: arginine decarboxylase (EC 4.1.1.19) from Homo sapiens | 30% id, 76% cov |
ADC / P49726: arginine decarboxylase (EC 4.1.1.19) from Solanum lycopersicum | 22% id, 66% cov |
P74576: arginine decarboxylase (EC 4.1.1.19) from Synechocystis sp. | 25% id, 46% cov |
| SMc00723: diaminopimelate DAP decarboxylase is similar to: | PaperBLAST |
ADC / P49726: arginine decarboxylase (EC 4.1.1.19) from Solanum lycopersicum | 25% id, 59% cov |
Psest_3366: Biosynthetic arginine decarboxylase (EC 4.1.1.19) from Pseudomonas stutzeri | 28% id, 45% cov |
A0A076IP90: arginine decarboxylase (EC 4.1.1.19) from Phocaeicola dorei | 23% id, 52% 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