Searching in Pseudomonas fluorescens FW300-N2E2 (pseudo6_N2E2)
Found 23 curated entries in PaperBLAST's database that match '3.6.1.31' as complete word(s).
These curated entries have 18 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Pseudomonas fluorescens FW300-N2E2, or try another query
Pf6N2E2_3783: Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) is similar to: | PaperBLAST |
AO356_09525: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 100% id, 100% cov |
Pf1N1B4_1566: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 98% id, 100% cov |
AO353_12360: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 98% id, 100% cov |
Pf6N2E2_5724: Nucleoside triphosphate pyrophosphohydrolase MazG (EC 3.6.1.8) is similar to: | PaperBLAST |
Q72CU7: phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) from Desulfovibrio vulgaris | 34% id, 96% cov |
Pf6N2E2_3782: Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) is similar to: | PaperBLAST |
HisE / b2026: putative bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase (EC 3.5.4.19; EC 3.6.1.31) from Escherichia coli | 39% id, 48% cov |
HIS2_ARATH / O82768: Histidine biosynthesis bifunctional protein hisIE, chloroplastic; Protein HISTIDINE BIOSYNTHESIS 2; EC 3.5.4.19; EC 3.6.1.31 from Arabidopsis thaliana | 45% id, 40% cov |
HIS2_YEAST / P00815: Histidine biosynthesis trifunctional protein; EC 3.5.4.19; EC 3.6.1.31; EC 1.1.1.23 from Saccharomyces cerevisiae | 35% id, 13% cov |
Pf6N2E2_3252: Histidinol dehydrogenase (EC 1.1.1.23) is similar to: | PaperBLAST |
HIS2_YEAST / P00815: Histidine biosynthesis trifunctional protein; EC 3.5.4.19; EC 3.6.1.31; EC 1.1.1.23 from Saccharomyces cerevisiae | 36% id, 50% 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