Searching in Methylocapsa aurea KYG (GCF_000746085.1)
Found 7 curated entries in PaperBLAST's database that match '4.2.1.116' as complete word(s).
These curated entries have 5 distinct sequences.
Running ublast with E ≤ 0.01
Found 20 relevant proteins in Methylocapsa aurea KYG, or try another query
| DL86_RS15400 WP_036263857.1: enoyl-CoA hydratase/isomerase family protein is similar to: | PaperBLAST |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 32% id, 98% cov |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 30% id, 96% cov |
| fadB DL86_RS06940 WP_036259721.1: fatty acid oxidation complex subunit alpha FadB is similar to: | PaperBLAST |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 37% id, 76% cov |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 34% id, 72% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 33% id, 73% cov |
| DL86_RS00860 WP_036257290.1: enoyl-CoA hydratase-related protein is similar to: | PaperBLAST |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 28% id, 97% cov |
| DL86_RS01770 WP_036257477.1: enoyl-CoA hydratase/isomerase family protein is similar to: | PaperBLAST |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 31% id, 81% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 30% id, 82% cov |
| DL86_RS07960 WP_036260031.1: 3-hydroxyacyl-CoA dehydrogenase NAD-binding domain-containing protein 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. | 26% id, 92% cov |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 33% id, 67% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 28% id, 69% cov |
| fabG DL86_RS06380 WP_036259611.1: 3-oxoacyl-[acyl-carrier-protein] reductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 39% id, 25% cov |
| DL86_RS06685 WP_156964509.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 24% id, 36% cov |
| phbB DL86_RS05195 WP_036258924.1: acetoacetyl-CoA reductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 34% id, 25% cov |
| acs DL86_RS03890 WP_036258617.1: acetate--CoA ligase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 32% id, 24% cov |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 31% id, 14% cov |
| DL86_RS06500 WP_036259457.1: 3-hydroxybutyrate dehydrogenase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 30% id, 25% cov |
| DL86_RS13605 WP_036262521.1: oxidoreductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 27% id, 27% cov |
| DL86_RS12180 WP_036261783.1: 3-hydroxybutyrate dehydrogenase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 27% id, 26% cov |
| acsA DL86_RS18225 WP_036264504.1: acetate--CoA ligase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 30% id, 23% cov |
| DL86_RS03260 WP_036258220.1: SDR family oxidoreductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 30% id, 20% cov |
| DL86_RS12320 WP_036261813.1: SDR family oxidoreductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 29% id, 20% cov |
| DL86_RS00710 WP_202899140.1: SDR family oxidoreductase is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 23% id, 24% cov |
| DL86_RS11345 WP_084572863.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 24% id, 17% cov |
| DL86_RS15085 WP_051953540.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 27% id, 12% cov |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 35% id, 4% cov |
| DL86_RS04015 WP_036258642.1: hybrid non-ribosomal peptide synthetase/type I polyketide synthase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 25% id, 13% cov |
| DL86_RS06695 WP_156964510.1: non-ribosomal peptide synthetase is similar to: | PaperBLAST |
pcs / A9WEU4: propionyl-CoA synthase subunit (EC 1.3.1.84; EC 4.2.1.116; EC 6.2.1.36) from Chloroflexus aurantiacus | 26% id, 10% 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 16 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory