Searching in Shewanella oneidensis MR-1 (MR1)
Found 17 curated entries in PaperBLAST's database that match '4.1.3.4' as complete word(s).
These curated entries have 12 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Shewanella oneidensis MR-1, or try another query
| SO1893: hydroxymethylglutaryl-CoA lyase (NCBI ptt file) is similar to: | PaperBLAST |
LIUE_PSEAE / Q9I2A0: 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase; HIHG-CoA lyase; HMG-CoA lyase; (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase; 3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase; EC 4.1.3.26; EC 4.1.3.4 from Pseudomonas aeruginosa | 58% id, 98% cov |
HMGCL_RAT / P97519: Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Rattus norvegicus | 60% id, 94% cov |
HMGCL_MOUSE / P38060: Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Mus musculus | 60% id, 94% cov |
| SO4236: 2-isopropylmalate synthase (NCBI ptt file) is similar to: | PaperBLAST |
HMGCL_BACSU / O34873: Hydroxymethylglutaryl-CoA lyase YngG; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Bacillus subtilis | 24% id, 97% cov |
| SO1895: enoyl-CoA hydratase/isomerase family protein (NCBI ptt file) 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 | 31% id, 43% cov |
| SO0572: enoyl-CoA hydratase/isomerase family protein (NCBI ptt file) 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 | 31% id, 34% 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