Searching in Methylocella silvestris BL2 (GCF_000021745.1)
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 Methylocella silvestris BL2, or try another query
MSIL_RS12990 Msil_2548 WP_012591541.1: phosphoribosyl-ATP diphosphatase is similar to: | PaperBLAST |
CCNA_03854: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Caulobacter crescentus | 52% id, 92% cov |
Ga0059261_1051: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Sphingomonas koreensis | 49% id, 93% cov |
PfGW456L13_303: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 41% id, 99% cov |
mazG MSIL_RS02730 Msil_0537 WP_012589579.1: nucleoside triphosphate pyrophosphohydrolase is similar to: | PaperBLAST |
Q72CU7: phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) from Desulfovibrio vulgaris | 34% id, 99% cov |
hisI MSIL_RS01815 Msil_0355 WP_012589404.1: 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 | 46% id, 44% 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 | 33% id, 34% cov |
HIS2_SCHPO / O59667: Histidine biosynthesis bifunctional protein his7; EC 3.5.4.19; EC 3.6.1.31 from Schizosaccharomyces pombe | 37% id, 21% cov |
hisD MSIL_RS15640 Msil_3070 WP_012592048.1: 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 | 37% id, 54% 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