Searching in Pseudomonas putida KT2440 (Putida)
Found 20 curated entries in PaperBLAST's database that match '3.7.1.2' as complete word(s).
These curated entries have 15 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Pseudomonas putida KT2440, or try another query
| PP_3205: Fumarylacetoacetate hydrolase family protein is similar to: | PaperBLAST |
Psest_3512: fumarylacetoacetate (FAA) hydrolase (EC 3.7.1.2) from Pseudomonas stutzeri | 54% id, 100% cov |
SO1670: fumarylacetoacetate hydrolase (EC 3.7.1.2) from Shewanella oneidensis | 51% id, 99% cov |
| PP_4620: Fumarylacetoacetase is similar to: | PaperBLAST |
FAAA_CAEEL / Q94272: Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Caenorhabditis elegans | 49% id, 98% cov |
FAH_ARATH / Q8RW90: Fumarylacetoacetase; Fumarylacetoacetate hydrolase; AtFAH; Protein SHORT-DAY SENSITIVE CELL DEATH 1; EC 3.7.1.2 from Arabidopsis thaliana | 47% id, 99% cov |
FAAA_HUMAN / P16930: Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Homo sapiens | 48% id, 97% cov |
| PP_1709: Fumarylacetoacetate hydrolase family protein is similar to: | PaperBLAST |
A0A0M3SVN7: fumarylacetoacetase (EC 3.7.1.2) from Cupriavidus gilardii | 47% id, 99% cov |
A0A1B0ZSC0: fumarylacetoacetase (EC 3.7.1.2) from Phaeobacter gallaeciensis | 37% id, 97% cov |
A0A0D5YDA5: fumarylacetoacetase (EC 3.7.1.2) from Acinetobacter baumannii | 33% id, 92% cov |
| PP_5153: putative isomerase/hydrolase is similar to: | PaperBLAST |
A0A0D5YDA5: fumarylacetoacetase (EC 3.7.1.2) from Acinetobacter baumannii | 44% id, 93% cov |
A0A0M3SVN7: fumarylacetoacetase (EC 3.7.1.2) from Cupriavidus gilardii | 39% id, 91% cov |
A0A1B0ZSC0: fumarylacetoacetase (EC 3.7.1.2) from Phaeobacter gallaeciensis | 34% id, 88% 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