Searching in Clostridium kluyveri DSM 555 (GCF_000016505.1)
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 Clostridium kluyveri DSM 555, or try another query
mazG CKL_RS00760 CKL_0156 WP_011988752.1: nucleoside triphosphate pyrophosphohydrolase is similar to: | PaperBLAST |
Q72CU7: phosphoribosyl-ATP diphosphatase (EC 3.6.1.31) from Desulfovibrio vulgaris | 39% id, 95% cov |
hisE CKL_RS06410 CKL_1302 WP_041700783.1: phosphoribosyl-ATP diphosphatase is similar to: | PaperBLAST |
AO356_09525: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 38% id, 86% cov |
PS417_01850: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas simiae | 37% id, 86% cov |
PfGW456L13_303: phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) from Pseudomonas fluorescens | 37% id, 86% cov |
hisI CKL_RS06405 CKL_1301 WP_012101688.1: 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 | 50% 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 | 42% id, 33% 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 | 38% id, 13% cov |
hisD CKL_RS06375 CKL_1295 WP_012101682.1: 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 | 38% 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