Searching in Herbaspirillum seropedicae SmR1 (HerbieS)
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 Herbaspirillum seropedicae SmR1, or try another query
| HSERO_RS17860: 5-carboxymethyl-2-hydroxymuconate isomerase is similar to: | PaperBLAST |
A0A0M3SVN7: fumarylacetoacetase (EC 3.7.1.2) from Cupriavidus gilardii | 61% id, 97% cov |
A0A1B0ZSC0: fumarylacetoacetase (EC 3.7.1.2) from Phaeobacter gallaeciensis | 48% id, 95% cov |
A0A0D5YDA5: fumarylacetoacetase (EC 3.7.1.2) from Acinetobacter baumannii | 34% id, 91% cov |
| HSERO_RS05610: 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 |
FAAA_HUMAN / P16930: Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Homo sapiens | 48% id, 99% cov |
FAAA_RAT / P25093: Fumarylacetoacetase; FAA; Beta-diketonase; Fumarylacetoacetate hydrolase; EC 3.7.1.2 from Rattus norvegicus | 47% id, 99% cov |
| HSERO_RS05065: 2-keto-4-pentenoate hydratase is similar to: | PaperBLAST |
Psest_3512: fumarylacetoacetate (FAA) hydrolase (EC 3.7.1.2) from Pseudomonas stutzeri | 49% id, 98% cov |
SO1670: fumarylacetoacetate hydrolase (EC 3.7.1.2) from Shewanella oneidensis | 48% id, 99% cov |
| HSERO_RS06355: ureidoglycolate lyase is similar to: | PaperBLAST |
K0A9N9: fumarylacetoacetase (EC 3.7.1.2) from Exiguobacterium antarcticum | 35% id, 99% cov |
A0A1B0ZSC0: fumarylacetoacetase (EC 3.7.1.2) from Phaeobacter gallaeciensis | 34% id, 95% cov |
A0A076VF18: fumarylacetoacetase (EC 3.7.1.2) from Rhodotorula diobovata | 40% id, 66% 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