Searching in Chlorobium limicola DSM 245 (GCF_000020465.1)
Found 34 curated entries in PaperBLAST's database that match '5.3.1.8' as complete word(s).
These curated entries have 28 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Chlorobium limicola DSM 245, or try another query
CLIM_RS08945 Clim_1775 WP_012466687.1: mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase is similar to: | PaperBLAST |
ALGA_PSEAE / P07874: Alginate biosynthesis protein AlgA; EC 5.3.1.8; EC 2.7.7.13 from Pseudomonas aeruginosa | 56% id, 98% cov |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 54% id, 97% cov |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 42% id, 99% cov |
glmM CLIM_RS01645 Clim_0319 WP_041465827.1: phosphoglucosamine mutase is similar to: | PaperBLAST |
ST0242 / Q976E4: hexose-6-phosphate mutase/isomerase (EC 5.3.1.8; EC 5.3.1.9; EC 5.4.2.10; EC 5.4.2.13) from Sulfurisphaera tokodaii | 28% id, 99% cov |
CLIM_RS01770 Clim_0341 WP_012465315.1: phosphoglucomutase/phosphomannomutase family protein is similar to: | PaperBLAST |
ST0242 / Q976E4: hexose-6-phosphate mutase/isomerase (EC 5.3.1.8; EC 5.3.1.9; EC 5.4.2.10; EC 5.4.2.13) from Sulfurisphaera tokodaii | 25% id, 98% cov |
CLIM_RS11050 Clim_2199 WP_317623571.1: mannose-1-phosphate guanylyltransferase is similar to: | PaperBLAST |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 31% id, 75% cov |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 31% id, 72% cov |
ALGA_PSEAE / P07874: Alginate biosynthesis protein AlgA; EC 5.3.1.8; EC 2.7.7.13 from Pseudomonas aeruginosa | 30% id, 73% 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