Searching in Pseudomonas stutzeri RCH2 (psRCH2)
Found 13 curated entries in PaperBLAST's database that match '4.2.1.18' as complete word(s).
These curated entries have 11 distinct sequences.
Running ublast with E ≤ 0.01
Found 10 relevant proteins in Pseudomonas stutzeri RCH2, or try another query
Psest_1082: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
liuC / Q88FM3: 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas putida | 71% id, 97% cov |
Pf6N2E2_2193: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas fluorescens | 68% id, 97% cov |
AO356_01590: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas fluorescens | 68% id, 97% cov |
Psest_3109: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 39% id, 99% cov |
Fer4 / Q4PEN0: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Ustilago maydis | 34% id, 94% cov |
SM_b21126: 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Sinorhizobium meliloti | 30% id, 100% cov |
Psest_2437: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 36% id, 98% cov |
CA265_RS09125: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pedobacter sp. | 31% id, 97% cov |
Fer4 / Q4PEN0: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Ustilago maydis | 33% id, 92% cov |
Psest_4235: 3-hydroxyacyl-CoA dehydrogenase is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 34% id, 93% cov |
F4JML5: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Arabidopsis thaliana | 33% id, 83% cov |
Fer4 / Q4PEN0: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Ustilago maydis | 37% id, 68% cov |
Psest_2654: fatty oxidation complex, alpha subunit FadB is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 32% id, 86% cov |
AUHM_MOUSE / Q9JLZ3: Methylglutaconyl-CoA hydratase, mitochondrial; 3-MG-CoA hydratase; AU-specific RNA-binding enoyl-CoA hydratase; AU-binding enoyl-CoA hydratase; muAUH; Itaconyl-CoA hydratase; EC 4.2.1.18; EC 4.2.1.56 from Mus musculus | 37% id, 65% cov |
F4JML5: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Arabidopsis thaliana | 34% id, 71% cov |
Psest_3110: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 30% id, 92% cov |
Psest_2076: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
liuC / Q88FM3: 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas putida | 28% id, 96% cov |
Pf6N2E2_2193: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas fluorescens | 28% id, 90% cov |
AO356_01590: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas fluorescens | 28% id, 90% cov |
Psest_1079: Isopropylmalate/homocitrate/citramalate synthases is similar to: | PaperBLAST |
hlyA: 3-hydroxy-3-methylglutaryl-coenzyme A lyase/3-methylglutaconyl-coenzyme A hydratase; EC 4.1.3.4; EC 4.2.1.18 from Emericella nidulans | 50% id, 50% cov |
Psest_2439: Enoyl-CoA hydratase/carnithine racemase is similar to: | PaperBLAST |
Q1D5Y4: methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Myxococcus xanthus | 31% id, 63% cov |
liuC / Q88FM3: 3-methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas putida | 27% id, 67% cov |
Pf6N2E2_2193: Methylglutaconyl-CoA hydratase (EC 4.2.1.18) from Pseudomonas fluorescens | 25% id, 61% cov |
Psest_2661: Isopropylmalate/homocitrate/citramalate synthases is similar to: | PaperBLAST |
hlyA: 3-hydroxy-3-methylglutaryl-coenzyme A lyase/3-methylglutaconyl-coenzyme A hydratase; EC 4.1.3.4; EC 4.2.1.18 from Emericella nidulans | 36% id, 52% 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 10 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory