Searching in Escherichia coli BW25113 (Keio)
Found 26 curated entries in PaperBLAST's database that match '4.1.1.20' as complete word(s).
These curated entries have 16 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Escherichia coli BW25113, or try another query
| b2838: diaminopimelate decarboxylase, PLP-binding (NCBI) is similar to: | PaperBLAST |
DCDA_ECOLI / P00861: Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Escherichia coli | 100% id, 100% cov |
Ga0059261_2051: diaminopimelate decarboxylase (EC 4.1.1.20) from Sphingomonas koreensis | 35% id, 96% cov |
Echvi_1295: diaminopimelate decarboxylase (EC 4.1.1.20) from Echinicola vietnamensis | 34% id, 96% cov |
| b2938: arginine decarboxylase (NCBI) is similar to: | PaperBLAST |
BT1374: diaminopimelate decarboxylase (EC 4.1.1.20) from Bacteroides thetaiotaomicron | 22% id, 79% cov |
Ga0059261_2051: diaminopimelate decarboxylase (EC 4.1.1.20) from Sphingomonas koreensis | 26% id, 66% cov |
DCDA_HELPX / B4XMC6: Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori | 27% id, 63% cov |
| b4024: aspartate kinase III (NCBI) is similar to: | PaperBLAST |
ABZR86_RS19560: aspartate kinase / diaminopimelate decarboxylase (EC 4.1.1.20; EC 2.7.2.4) from Dyella japonica | 33% id, 52% cov |
| b0002: bifunctional aspartokinase I/homeserine dehydrogenase I (NCBI) is similar to: | PaperBLAST |
ABZR86_RS19560: aspartate kinase / diaminopimelate decarboxylase (EC 4.1.1.20; EC 2.7.2.4) from Dyella japonica | 31% id, 52% cov |
| b3940: bifunctional aspartate kinase II/homoserine dehydrogenase II (NCBI) is similar to: | PaperBLAST |
ABZR86_RS19560: aspartate kinase / diaminopimelate decarboxylase (EC 4.1.1.20; EC 2.7.2.4) from Dyella japonica | 27% id, 60% 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 5 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory