Searching in Methylotuvimicrobium alcaliphilum 20Z (GCF_000968535.2)
Found 51 curated entries in PaperBLAST's database that match '1.5.5.2' as complete word(s).
These curated entries have 41 distinct sequences.
Running ublast with E ≤ 0.01
Found 10 relevant proteins in Methylotuvimicrobium alcaliphilum 20Z, or try another query
| putA MEALZ_RS08415 MEALZ_1726 WP_014148206.1: bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA is similar to: | PaperBLAST |
Sama_2676: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella amazonensis | 51% id, 98% cov |
Shewana3_0819: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Shewanella sp. | 50% id, 98% cov |
Psest_3079: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri | 49% id, 98% cov |
| MEALZ_RS02880 MEALZ_0588 WP_014147089.1: FAD-dependent oxidoreductase is similar to: | PaperBLAST |
Q8U022: proline dehydrogenase (EC 1.5.5.2) from Pyrococcus furiosus | 26% id, 94% cov |
O59445: proline dehydrogenase (EC 1.5.5.2) from Pyrococcus horikoshii | 26% id, 96% cov |
Q8U1G2: proline dehydrogenase (EC 1.5.5.2) from Pyrococcus furiosus | 25% id, 92% cov |
| lpdA MEALZ_RS06625 MEALZ_1357 WP_014147842.1: dihydrolipoyl dehydrogenase is similar to: | PaperBLAST |
Q76M76: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 27% id, 74% cov |
| MEALZ_RS19245 MEALZ_3921 WP_046061712.1: FAD-binding oxidoreductase is similar to: | PaperBLAST |
Q76M73: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 27% id, 58% cov |
Q5JFG2: proline dehydrogenase (EC 1.5.5.2) from Thermococcus kodakarensis | 26% id, 58% cov |
Q8U1G2: proline dehydrogenase (EC 1.5.5.2) from Pyrococcus furiosus | 25% id, 58% cov |
| lpdA MEALZ_RS07695 MEALZ_1578 WP_014148059.1: dihydrolipoyl dehydrogenase is similar to: | PaperBLAST |
Q76M76: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 23% id, 62% cov |
| MEALZ_RS19545 MEALZ_3979 WP_014150384.1: NAD-dependent succinate-semialdehyde dehydrogenase is similar to: | PaperBLAST |
Psest_3079: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Pseudomonas stutzeri | 27% id, 41% cov |
PGA1_c11750: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Phaeobacter inhibens | 28% id, 37% cov |
RR42_RS20125: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Cupriavidus basilensis | 30% id, 34% cov |
| MEALZ_RS07685 MEALZ_1576 WP_014148057.1: NAD-dependent succinate-semialdehyde dehydrogenase is similar to: | PaperBLAST |
RR42_RS20125: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Cupriavidus basilensis | 28% id, 32% cov |
HSERO_RS00905: L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88); Proline dehydrogenase (EC 1.5.5.2) from Herbaspirillum seropedicae | 26% id, 35% cov |
PUTA_ECOLI / P09546: Bifunctional protein PutA; EC 1.5.5.2; EC 1.2.1.88 from Escherichia coli | 27% id, 33% cov |
| mnmG MEALZ_RS01595 MEALZ_0324 WP_014146833.1: tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG is similar to: | PaperBLAST |
Q76M76: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 26% id, 24% cov |
| MEALZ_RS13475 MEALZ_2767 WP_084685613.1: TIGR03862 family flavoprotein is similar to: | PaperBLAST |
Q76M76: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 33% id, 16% cov |
| MEALZ_RS18045 MEALZ_3681 WP_014150092.1: NAD(P)/FAD-dependent oxidoreductase is similar to: | PaperBLAST |
Q76M76: proline dehydrogenase (EC 1.5.5.2) from Thermococcus profundus | 45% id, 10% 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 9 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory