Searching in Escherichia coli BW25113 (Keio)
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 14 relevant proteins in Escherichia coli BW25113, or try another query
b1093: 3-oxoacyl-[acyl-carrier-protein] reductase (NCBI) 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, 97% cov |
lra1 / Q1NEJ0: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Sphingomonas sp. | 36% id, 98% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 33% id, 99% cov |
b2137: predicted oxidoreductase with NAD(P)-binding Rossmann-fold domain (NCBI) 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 | 36% 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. | 34% id, 98% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 33% id, 97% cov |
b2774: putative oxidoreductase (VIMSS) 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, 98% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 33% 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. | 32% id, 98% cov |
b2842: 2-deoxy-D-gluconate 3-dehydrogenase (NCBI) 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. | 36% 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 | 33% id, 97% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 32% id, 97% cov |
b3003: oxidoreductase (NCBI) is similar to: | PaperBLAST |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 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. | 34% id, 98% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 34% id, 97% cov |
b0596: 2,3-dihydroxybenzoate-2,3-dehydrogenase (NCBI) 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. | 35% id, 96% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 32% id, 98% cov |
b1619: 7-alpha-hydroxysteroid dehydrogenase (NCBI) 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. | 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 | 34% id, 98% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 34% id, 96% cov |
b4249: predicted oxidoreductase with NAD(P)-binding Rossmann-fold domain (NCBI) 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. | 34% 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 | 34% id, 96% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 31% id, 96% cov |
b2426: putative oxidoreductase (VIMSS) is similar to: | PaperBLAST |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 34% 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 | 34% 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. | 33% id, 98% cov |
b4266: gluconate 5-dehydrogenase (NCBI) is similar to: | PaperBLAST |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 31% 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 | 28% id, 98% cov |
b2902: predicted NAD(P)-binding oxidoreductase with NAD(P)-binding Rossmann-fold domain (NCBI) 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. | 32% id, 94% cov |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 31% id, 95% cov |
RM1DH_PICST / A3LZU7: L-rhamnose-1-dehydrogenase; EC 1.1.1.173 from Scheffersomyces stipitis | 27% id, 95% cov |
b2705: 3-ketoacyl-(acyl-carrier-protein) reductase (NCBI) is similar to: | PaperBLAST |
BPHYT_RS28235: L-rhamnose-1-dehydrogenase ( EC 1.1.1.173) from Burkholderia phytofirmans | 30% 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. | 29% id, 97% cov |
b1271: short chain dehydrogenase (NCBI) 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. | 24% id, 94% cov |
lra1 / C1DMX5: NAD(P)+-dependent L-rhamnose 1-dehydrogenase (EC 1.1.1.378; EC 1.1.1.173) from Azotobacter vinelandii | 23% id, 97% cov |
b0493: short chain dehydrogenase (NCBI) 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 | 26% id, 84% 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 13 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory