Searching in Dinoroseobacter shibae DFL-12 (Dino)
Found 6 curated entries in PaperBLAST's database that match '1.1.1.60' as complete word(s).
These curated entries have 4 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Dinoroseobacter shibae DFL-12, or try another query
| Dshi_3047: 6-phosphogluconate dehydrogenase NAD-binding (RefSeq) is similar to: | PaperBLAST |
Q8ZLV8: 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) from Salmonella enterica | 35% id, 98% cov |
GARR_ECOLI / P0ABQ2: 2-hydroxy-3-oxopropionate reductase; Tartronate semialdehyde reductase; TSAR; EC 1.1.1.60 from Escherichia coli | 35% id, 99% cov |
glxR / P77161: tartronate semialdehyde reductase 2 (EC 1.1.1.60) from Escherichia coli | 35% id, 98% cov |
| Dshi_1752: 3-hydroxyisobutyrate dehydrogenase (RefSeq) is similar to: | PaperBLAST |
GARR_ECOLI / P0ABQ2: 2-hydroxy-3-oxopropionate reductase; Tartronate semialdehyde reductase; TSAR; EC 1.1.1.60 from Escherichia coli | 34% id, 95% cov |
Q8ZLV8: 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) from Salmonella enterica | 34% id, 95% cov |
glxR / P77161: tartronate semialdehyde reductase 2 (EC 1.1.1.60) from Escherichia coli | 33% id, 96% cov |
| Dshi_4221: 2-hydroxy-3-oxopropionate reductase (RefSeq) is similar to: | PaperBLAST |
GARR_ECOLI / P0ABQ2: 2-hydroxy-3-oxopropionate reductase; Tartronate semialdehyde reductase; TSAR; EC 1.1.1.60 from Escherichia coli | 32% id, 97% cov |
Q8ZLV8: 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) from Salmonella enterica | 32% id, 97% cov |
glxR / P77161: tartronate semialdehyde reductase 2 (EC 1.1.1.60) from Escherichia coli | 30% id, 96% cov |
| Dshi_2443: 6-phosphogluconate dehydrogenase NAD-binding (RefSeq) is similar to: | PaperBLAST |
glxR / P77161: tartronate semialdehyde reductase 2 (EC 1.1.1.60) from Escherichia coli | 28% id, 87% 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