Searching in Echinicola vietnamensis KMM 6221, DSM 17526 (Cola)
Found 19 curated entries in PaperBLAST's database that match '3.1.2.4' as complete word(s).
These curated entries have 16 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Echinicola vietnamensis KMM 6221, DSM 17526, or try another query
| Echvi_4069: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 37% id, 99% cov |
Pf1N1B4_4790: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas fluorescens | 27% id, 78% cov |
AO353_25665: 3-hydroxy-isobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas fluorescens | 28% id, 76% cov |
| Echvi_0343: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 31% id, 97% cov |
HIBC1_ARATH / Q9LKJ1: 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana | 27% id, 49% cov |
| Echvi_2341: naphthoate synthase (dihydroxynaphthoic acid synthetase) is similar to: | PaperBLAST |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 29% id, 99% cov |
| Echvi_0069: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 29% id, 94% cov |
| Echvi_1069: 3-hydroxyacyl-CoA dehydrogenase is similar to: | PaperBLAST |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 25% id, 79% 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 5 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory