Curated BLAST for Genomes

 

Curated BLAST

Searching in Escherichia coli BW25113 (Keio)

Found 5 curated entries in PaperBLAST's database that match '3.7.1.21'.

These curated entries have 3 distinct sequences.

Running ublast with E ≤ 0.01

Found 2 relevant proteins in Escherichia coli BW25113, or try another query

b2262: naphthoate synthase (NCBI)
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

34% id,
51% 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
O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase (EC 3.7.1.21) from Thauera aromatica

31% id,
48% cov

BAMA_SYNAS / Q2LXU2: 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 Syntrophus aciditrophicus
bamA / Q2LXU2: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase monomer (EC 3.7.1.21) from Syntrophus aciditrophicus

27% id,
48% cov

b1394: enoyl-CoA hydratase (NCBI)
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
O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase (EC 3.7.1.21) from Thauera aromatica

28% id,
45% cov

BAMA_SYNAS / Q2LXU2: 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 Syntrophus aciditrophicus
bamA / Q2LXU2: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase monomer (EC 3.7.1.21) from Syntrophus aciditrophicus

28% 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 2 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory