Curated BLAST for Genomes

 

Curated BLAST

Searching in Pantoea rwandensis LMG 26275 (GCF_002095475.1)

Found 5 curated entries in PaperBLAST's database that match '5.3.3.18' as complete word(s).

These curated entries have 3 distinct sequences.

Running ublast with E ≤ 0.01

Found 4 relevant proteins in Pantoea rwandensis LMG 26275, or try another query

HA51_RS04965 HA51_04915 WP_084932587.1: enoyl-CoA hydratase/isomerase family protein
is similar to:
PaperBLAST

Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus

30% id,
98% cov

PAAG_ECOLI / P77467: 1,2-epoxyphenylacetyl-CoA isomerase; EC 5.3.3.18 from Escherichia coli
YdbT / b1394: putative ring 1,2-epoxyphenylacetyl-CoA isomerase (oxepin-CoA forming) (EC 5.3.3.18) from Escherichia coli
P77467: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Escherichia coli

29% id,
100% cov

fadJ HA51_RS11045 HA51_10915 WP_084934563.1: fatty acid oxidation complex subunit alpha FadJ
is similar to:
PaperBLAST

Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus

29% id,
96% cov

H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila

30% id,
69% cov

HA51_RS05000 HA51_04950 WP_084932602.1: enoyl-CoA hydratase/isomerase family protein
is similar to:
PaperBLAST

Q5SLK3: 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) from Thermus thermophilus

33% id,
81% cov

H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila

31% id,
79% cov

fadB HA51_RS26560 HA51_26255 WP_084938412.1: fatty acid oxidation complex subunit alpha FadB
is similar to:
PaperBLAST

H281DRAFT_05722: 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) from Paraburkholderia bryophila

29% id,
74% 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.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory