Searching in Acidovorax sp. GW101-3H11 (acidovorax_3H11)
Found 15 curated entries in PaperBLAST's database that match '1.2.1.38' as complete word(s).
These curated entries have 11 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Acidovorax sp. GW101-3H11, or try another query
| Ac3H11_2950: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) is similar to: | PaperBLAST |
SMc01801: N-acetylglutamylphosphate reductase (EC 1.2.1.38) from Sinorhizobium meliloti | 53% id, 99% cov |
Ga0059261_0351: N-acetylglutamylphosphate reductase (EC 1.2.1.38) from Sphingomonas koreensis | 49% id, 97% cov |
ARGC_GEOSE / Q07906: N-acetyl-gamma-glutamyl-phosphate reductase; AGPR; N-acetyl-glutamate semialdehyde dehydrogenase; NAGSA dehydrogenase; EC 1.2.1.38 from Geobacillus stearothermophilus | 31% id, 78% cov |
| Ac3H11_1253: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) is similar to: | PaperBLAST |
SMc01801: N-acetylglutamylphosphate reductase (EC 1.2.1.38) from Sinorhizobium meliloti | 46% id, 99% cov |
Ga0059261_0351: N-acetylglutamylphosphate reductase (EC 1.2.1.38) from Sphingomonas koreensis | 47% id, 96% cov |
CA265_RS18540: N-succinylglutamylphosphate reductase (EC 1.2.1.38) from Pedobacter sp. | 27% id, 95% cov |
| Ac3H11_1907: Acetylglutamate kinase (EC 2.7.2.8) is similar to: | PaperBLAST |
ARG56_SCHPO / P31318: Protein arg11, mitochondrial; EC 1.2.1.38; EC 2.7.2.8 from Schizosaccharomyces pombe | 28% id, 31% cov |
ARG56_YEAST / Q01217: Protein ARG5,6, mitochondrial; EC 1.2.1.38; EC 2.7.2.8 from Saccharomyces cerevisiae | 26% id, 34% cov |
| Ac3H11_900: N-acetylglutamate synthase (EC 2.3.1.1) is similar to: | PaperBLAST |
ARG56_SCHPO / P31318: Protein arg11, mitochondrial; EC 1.2.1.38; EC 2.7.2.8 from Schizosaccharomyces pombe | 28% id, 23% 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