Searching in Desulfogranum mediterraneum DSM 13871 (GCF_000429965.1)
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 Desulfogranum mediterraneum DSM 13871, or try another query
| G494_RS0120230 WP_084457146.1: 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 | 51% id, 98% cov |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 49% id, 97% cov |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 47% id, 100% cov |
| glmM G494_RS0102820 WP_028583310.1: 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 | 29% id, 100% cov |
| G494_RS0120225 WP_028585974.1: phosphomannomutase/phosphoglucomutase 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 | 26% id, 99% cov |
| G494_RS0100740 WP_051305193.1: phosphomannose isomerase type II C-terminal cupin domain is similar to: | PaperBLAST |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 50% id, 24% cov |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 50% id, 23% cov |
ALGA_PSEAE / P07874: Alginate biosynthesis protein AlgA; EC 5.3.1.8; EC 2.7.7.13 from Pseudomonas aeruginosa | 48% id, 22% 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