Searching in Oscillibacter ruminantium GH1 (GCF_000307265.1)
Found 5 curated entries in PaperBLAST's database that match '1.1.1.173' as complete word(s).
These curated entries have 4 distinct sequences.
Running ublast with E ≤ 0.01
Found 8 relevant proteins in Oscillibacter ruminantium GH1, or try another query
fabG ON16_RS01385 WP_040658761.1: 3-oxoacyl-ACP reductase FabG is similar to: | PaperBLAST |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 42% id, 96% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 41% id, 97% cov |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 37% id, 97% cov |
fabG ON16_RS01680 WP_040658852.1: 3-oxoacyl-[acyl-carrier-protein] reductase is similar to: | PaperBLAST |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 39% id, 98% cov |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 39% id, 98% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 39% id, 96% cov |
ON16_RS09985 WP_040661679.1: 3-oxoacyl-ACP reductase family protein is similar to: | PaperBLAST |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 38% id, 99% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 37% id, 99% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 35% id, 97% cov |
ON16_RS13885 WP_040663927.1: SDR family NAD(P)-dependent oxidoreductase is similar to: | PaperBLAST |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 37% id, 99% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 36% id, 99% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 34% id, 99% cov |
ON16_RS15695 WP_040664056.1: gluconate 5-dehydrogenase is similar to: | PaperBLAST |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 35% id, 99% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 34% id, 99% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 32% id, 99% cov |
ON16_RS04320 WP_243441760.1: SDR family oxidoreductase is similar to: | PaperBLAST |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 35% id, 97% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 35% id, 96% cov |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 32% id, 97% cov |
ON16_RS14220 WP_040664062.1: glucose 1-dehydrogenase is similar to: | PaperBLAST |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 34% id, 98% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 32% id, 97% cov |
ON16_RS00855 WP_040658641.1: SDR family oxidoreductase is similar to: | PaperBLAST |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 29% id, 96% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 28% id, 96% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 27% id, 96% 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 8 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory