Searching in Pseudomonas simiae WCS417 (WCS417)
Found 36 curated entries in PaperBLAST's database that match '5.3.1.8' as complete word(s).
These curated entries have 29 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Pseudomonas simiae WCS417, or try another query
PS417_04790: mannose-1-phosphate guanylyltransferase is similar to: | PaperBLAST |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 98% id, 100% cov |
ALGA_PSEAE / P07874: Alginate biosynthesis protein AlgA; EC 5.3.1.8; EC 2.7.7.13 from Pseudomonas aeruginosa | 79% id, 98% cov |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 40% id, 100% cov |
PS417_09635: mannose-1-phosphate guanylyltransferase is similar to: | PaperBLAST |
ALGA_PSEAE / P07874: Alginate biosynthesis protein AlgA; EC 5.3.1.8; EC 2.7.7.13 from Pseudomonas aeruginosa | 44% id, 98% cov |
PH0925 / O58649: GDP-D-mannose pyrophosphorylase (EC 2.7.7.13; EC 5.3.1.8) from Pyrococcus horikoshii | 44% id, 99% cov |
algA / GI|31296823: alginate biosynthesis protein AlgA; EC 2.7.7.13; EC 5.3.1.8 from Pseudomonas fluorescens | 43% id, 97% cov |
PS417_24005: 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, 99% cov |
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 | 47% id, 7% cov |
PS417_27785: 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 | 28% id, 96% 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