Curated BLAST for Genomes

 

Curated BLAST

Searching in Pseudomonas simiae WCS417 (WCS417)

Found 5 curated entries in PaperBLAST's database that match '3.3.2.12' as complete word(s).

These curated entries have 2 distinct sequences.

Running ublast with E ≤ 0.01

Found 11 relevant proteins in Pseudomonas simiae WCS417, or try another query

PS417_13845: enoyl-CoA hydratase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

34% id,
94% cov

PS417_10680: enoyl-CoA hydratase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

31% id,
93% cov

PS417_12870: enoyl-CoA hydratase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

27% id,
93% cov

PS417_21215: 3-hydroxyacyl-CoA dehydrogenase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

34% id,
71% cov

PS417_11445: enoyl-CoA hydratase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

30% id,
74% cov

PS417_13835: crotonase
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

32% id,
60% cov

PS417_18205: aldehyde dehydrogenase
is similar to:
PaperBLAST

PAAZ_ECOLI / P77455: Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli
YdbN / b1387: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
paaZ / P77455: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
P77455: oxepin-CoA hydrolase (EC 3.3.2.12) from Escherichia coli

26% id,
72% cov

PS417_02175: transcriptional regulator
is similar to:
PaperBLAST

PAAZ_ECOLI / P77455: Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli
YdbN / b1387: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
paaZ / P77455: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
P77455: oxepin-CoA hydrolase (EC 3.3.2.12) from Escherichia coli

25% id,
71% cov

PS417_07575: multifunctional fatty acid oxidation complex subunit alpha
is similar to:
PaperBLAST

H281DRAFT_04594: putative oxepin-CoA hydrolase (EC 3.3.2.12) from Paraburkholderia bryophila

26% id,
60% cov

PS417_22080: 3-hydroxybutyryl-CoA dehydratase
is similar to:
PaperBLAST

PAAZ_ECOLI / P77455: Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli
YdbN / b1387: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
paaZ / P77455: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
P77455: oxepin-CoA hydrolase (EC 3.3.2.12) from Escherichia coli

35% id,
20% cov

PS417_24775: dehydratase
is similar to:
PaperBLAST

PAAZ_ECOLI / P77455: Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli
YdbN / b1387: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
paaZ / P77455: fused 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde dehydrogenase and oxepin-CoA hydrolase (EC 3.3.2.12; EC 1.2.1.91; EC 4.2.1.55) from Escherichia coli
P77455: oxepin-CoA hydrolase (EC 3.3.2.12) from Escherichia coli

36% id,
15% 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 11 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory