Searching in Methylohalobius crimeensis 10Ki (GCF_000421465.1)
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 Methylohalobius crimeensis 10Ki, or try another query
| H035_RS0106030 WP_022948102.1: phosphoribosyl-ATP diphosphatase is similar to: | PaperBLAST |
HP15_3195: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Marinobacter adhaerens | 64% id, 97% cov |
Psest_3944: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas stutzeri | 60% id, 96% cov |
PP_5015: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas putida | 60% id, 95% cov |
| mazG H035_RS0106710 WP_040574358.1: nucleoside triphosphate pyrophosphohydrolase is similar to: | PaperBLAST |
Q72CU7: phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) from Desulfovibrio vulgaris | 41% id, 96% cov |
| hisI H035_RS0106025 WP_022948101.1: phosphoribosyl-AMP cyclohydrolase 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, 51% 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 | 42% id, 35% 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 | 30% id, 16% cov |
| hisD H035_RS0104045 WP_321162852.1: histidinol dehydrogenase 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 | 35% id, 53% 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