Searching in Sphingomonas koreensis DSMZ 15582 (Korea)
Found 2 curated entries in PaperBLAST's database that match 'acetohydroxy acid synthase%large' as complete word(s).
These curated entries have 2 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Sphingomonas koreensis DSMZ 15582, or try another query
Ga0059261_0068: acetolactate synthase, large subunit (EC 2.2.1.6) is similar to: | PaperBLAST |
ilvB / AAL99356.1: acetohydroxy acid synthase large subunit from Geobacillus stearothermophilus | 50% id, 97% cov |
ilvB / AAV52901.1: acetohydroxy acid synthase large subunit from Streptomyces cinnamonensis | 47% id, 94% cov |
Ga0059261_0603: Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] is similar to: | PaperBLAST |
ilvB / AAL99356.1: acetohydroxy acid synthase large subunit from Geobacillus stearothermophilus | 31% id, 98% cov |
ilvB / AAV52901.1: acetohydroxy acid synthase large subunit from Streptomyces cinnamonensis | 32% id, 91% cov |
Ga0059261_1674: Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] is similar to: | PaperBLAST |
ilvB / AAL99356.1: acetohydroxy acid synthase large subunit from Geobacillus stearothermophilus | 30% id, 98% cov |
Ga0059261_0285: Thiamine pyrophosphate-requiring enzymes [acetolactate synthase, pyruvate dehydrogenase (cytochrome), glyoxylate carboligase, phosphonopyruvate decarboxylase] is similar to: | PaperBLAST |
ilvB / AAL99356.1: acetohydroxy acid synthase large subunit from Geobacillus stearothermophilus | 29% id, 97% cov |
ilvB / AAV52901.1: acetohydroxy acid synthase large subunit from Streptomyces cinnamonensis | 30% id, 88% 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