Searching in Marinobacter adhaerens HP15 (Marino)
Found 1 curated entries in PaperBLAST's database that match '1.1.1.377' as complete word(s).
These curated entries have 1 distinct sequences.
Running ublast with E ≤ 0.01
Found 17 relevant proteins in Marinobacter adhaerens HP15, or try another query
HP15_2784: 3-ketoacyl-(acyl-carrier-protein) reductase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 35% id, 99% cov |
HP15_2213: 3-ketoacyl-(acyl-carrier-protein) reductase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 34% id, 99% cov |
HP15_2724: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 33% id, 98% cov |
HP15_3924: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 32% id, 99% cov |
HP15_825: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 32% id, 98% cov |
HP15_1707: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 32% id, 98% cov |
HP15_2855: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 30% id, 99% cov |
HP15_31: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 31% id, 97% cov |
HP15_59: 3-oxoacyl-[acyl-carrier-protein] reductase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 31% id, 98% cov |
HP15_2345: 3-oxoacyl-(acyl-carrier protein) reductase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 30% id, 97% cov |
HP15_1108: 3-ketoacyl-(acyl-carrier-protein) reductase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 28% id, 96% cov |
HP15_2543: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 28% id, 96% cov |
HP15_880: oxidoreductase, short chain dehydrogenase/reductase family is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 27% id, 94% cov |
HP15_2729: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 28% id, 86% cov |
HP15_3798: 3-hydroxybutyrate dehydrogenase is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 22% id, 97% cov |
HP15_13: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 26% id, 83% cov |
HP15_822: short-chain dehydrogenase/reductase SDR is similar to: | PaperBLAST |
RHAD_THEAC / Q9HK58: L-rhamnose 1-dehydrogenase (NADP(+)); RHAD; EC 1.1.1.377 from Thermoplasma acidophilum | 23% id, 91% 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 16 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory