Searching in Paenacidovorax caeni R-24608 (GCF_001298675.1)
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 Paenacidovorax caeni R-24608, or try another query
BN2503_RS06965 WP_054255928.1: hydroxymethylglutaryl-CoA lyase 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 | 57% id, 100% 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 | 57% id, 90% cov |
HMGCL_HUMAN / P35914: Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens | 56% id, 90% cov |
BN2503_RS06985 WP_054255932.1: enoyl-CoA hydratase/isomerase family protein 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 | 33% id, 43% cov |
BN2503_RS05070 WP_054255554.1: enoyl-CoA hydratase 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, 41% cov |
BN2503_RS10715 WP_054256652.1: enoyl-CoA hydratase 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 | 27% id, 41% 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