Searching in Dokdonella koreensis DS-123 (GCF_001632775.1)
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 18 relevant proteins in Dokdonella koreensis DS-123, or try another query
I596_RS12940 I596_2758 WP_067648668.1: 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 | 45% id, 100% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 44% id, 100% cov |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 40% id, 98% cov |
I596_RS04715 I596_1020 WP_067644904.1: enoyl-CoA hydratase is similar to: | PaperBLAST |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 39% id, 96% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 35% id, 97% cov |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 33% id, 98% cov |
I596_RS08905 I596_1918 WP_067646635.1: enoyl-CoA hydratase-related 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. | 31% id, 100% cov |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 29% id, 98% cov |
I596_RS02240 I596_485 WP_067643566.1: 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. | 34% id, 71% cov |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 37% id, 64% cov |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 33% id, 72% cov |
I596_RS07555 I596_1634 WP_067646009.1: crotonase/enoyl-CoA hydratase family protein is similar to: | PaperBLAST |
acuH / Q5LWT8: acryloyl-CoA hydratase (EC 4.2.1.116) from Ruegeria pomeroyi | 27% id, 77% cov |
HPCD_METS5 / A4YI89: 3-hydroxypropionyl-coenzyme A dehydratase; 3-hydroxypropionyl-CoA dehydratase; EC 4.2.1.116 from Metallosphaera sedula | 26% id, 66% cov |
acuK / C8YX87: acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) from Halomonas sp. | 31% id, 46% cov |
fabG I596_RS15900 I596_3393 WP_067650170.1: 3-oxoacyl-ACP reductase FabG is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 37% id, 25% cov |
fabG I596_RS10645 I596_2280 WP_067647514.1: 3-oxoacyl-ACP reductase FabG is similar to: | PaperBLAST |
FOX2 / A0A1D8PJ13: D-specific enoyl-CoA hydratase (EC 4.2.1.119; EC 4.2.1.116) from Candida albicans | 35% id, 25% cov |
acs I596_RS00340 I596_72 WP_067642555.1: 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 | 33% 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 | 35% id, 9% cov |
phbB I596_RS05490 I596_1189 WP_067645282.1: 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 | 30% id, 26% cov |
phbB I596_RS05500 I596_1192 WP_067645286.1: 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 | 29% id, 26% cov |
I596_RS05290 I596_1146 WP_067645188.1: AMP-binding protein 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, 30% cov |
I596_RS02455 I596_529 WP_067643684.1: 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 | 29% id, 25% cov |
I596_RS00535 I596_111 WP_067642663.1: 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, 25% cov |
prpE I596_RS03300 I596_712 WP_067644159.1: propionate--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, 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 | 32% id, 12% cov |
I596_RS08880 I596_1913 WP_067646623.1: SDR family NAD(P)-dependent 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 | 28% id, 25% cov |
I596_RS07110 I596_1541 WP_067645861.1: 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, 23% cov |
I596_RS06495 I596_1413 WP_067645647.1: 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, 27% cov |
I596_RS06330 I596_1378 WP_067645581.1: 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase family protein 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 | 28% 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 17 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory