Searching in Shewanella loihica PV-4 (PV4)
Found 5 curated entries in PaperBLAST's database that match '3.7.1.21' as complete word(s).
These curated entries have 3 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Shewanella loihica PV-4, or try another query
Shew_1670: enoyl-CoA hydratase (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 28% id, 63% cov |
Shew_2864: 3-hydroxyacyl-CoA dehydrogenase, NAD-binding (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 30% id, 48% cov |
Shew_0019: multifunctional fatty acid oxidation complex subunit alpha (RefSeq) is similar to: | PaperBLAST |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 24% id, 43% cov |
BAMA_THAAR / O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; Beta-oxoacyl-CoA hydrolase; Oah; EC 3.7.1.21 from Thauera aromatica | 25% id, 36% cov |
Shew_1671: enoyl-CoA hydratase/isomerase (RefSeq) is similar to: | PaperBLAST |
BAMA_THAAR / O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; Beta-oxoacyl-CoA hydrolase; Oah; EC 3.7.1.21 from Thauera aromatica | 26% id, 37% cov |
BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens | 25% id, 36% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory