Searching in Pseudomonas stutzeri RCH2 (psRCH2)
Found 3 curated entries in PaperBLAST's database that match '1.2.1.77' as complete word(s).
These curated entries have 2 distinct sequences.
Running ublast with E ≤ 0.01
Found 6 relevant proteins in Pseudomonas stutzeri RCH2, or try another query
| Psest_0375: NAD-dependent aldehyde dehydrogenases is similar to: | PaperBLAST |
BOXD_AROEV / Q84HH8: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; EC 1.2.1.77 from Aromatoleum evansii | 29% id, 83% cov |
| Psest_3654: succinate-semialdehyde dehydrogenase is similar to: | PaperBLAST |
BOXD_AROEV / Q84HH8: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; EC 1.2.1.77 from Aromatoleum evansii | 29% id, 85% cov |
| Psest_4237: succinate-semialdehyde dehydrogenase is similar to: | PaperBLAST |
BOXD_AROEV / Q84HH8: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; EC 1.2.1.77 from Aromatoleum evansii | 28% id, 83% cov |
| Psest_2634: glycine betaine aldehyde dehydrogenase is similar to: | PaperBLAST |
BOXD_AROEV / Q84HH8: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; EC 1.2.1.77 from Aromatoleum evansii | 27% id, 84% cov |
| Psest_3079: delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain) is similar to: | PaperBLAST |
BOXD_AROEV / Q84HH8: 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; EC 1.2.1.77 from Aromatoleum evansii | 26% id, 86% cov |
Q13WK4: aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5); 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) (EC 1.2.1.77) from Paraburkholderia xenovorans | 26% id, 86% cov |
| Psest_0855: NAD-dependent aldehyde dehydrogenases is similar to: | PaperBLAST |
Q13WK4: aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5); 3,4-dehydroadipyl-CoA semialdehyde dehydrogenase (NADP+) (EC 1.2.1.77) from Paraburkholderia xenovorans | 25% id, 80% 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