Curated BLAST for Genomes

 

Curated BLAST

Searching in Sinorhizobium meliloti 1021 (Smeli)

Found 19 curated entries in PaperBLAST's database that match '3.1.2.4' as complete word(s).

These curated entries have 16 distinct sequences.

Running ublast with E ≤ 0.01

Found 9 relevant proteins in Sinorhizobium meliloti 1021, or try another query

SM_b20752: 3-hydroxyisobutyryl-CoA hydrolase
is similar to:		 PaperBLAST

C3KM96: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Sinorhizobium fredii

 84% id,
99% cov

bch / Q81DR3: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Bacillus cereus
Q81DR3: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Bacillus cereus

 40% id,
95% cov

Psest_2439: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas stutzeri

 39% id,
98% cov

More...

SMc01153: enoyl-CoA hydratase
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.

 60% id,
100% cov

C3KM96: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Sinorhizobium fredii

 33% id,
68% cov

Pf1N1B4_4790: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas fluorescens

 32% id,
69% cov

More...

SMc01669: enoyl-CoA hydratase
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.

 35% id,
100% cov

RR42_RS28545: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Cupriavidus basilensis

 38% id,
51% cov

PS417_13835: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas simiae

 34% id,
56% cov

More...

SMc01641: carnitinyl-CoA dehydratase
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.

 32% id,
99% cov

PS417_13835: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas simiae

 27% id,
55% cov

Pf1N1B4_4790: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas fluorescens

 24% id,
59% cov

More...

SM_b21633: enoyl-CoA hydratase
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.

 32% id,
95% cov

HIBCH_YEAST / P28817: Small ribosomal subunit protein mS47; 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial; 3-hydroxyisobutyryl-coenzyme A hydrolase; HIB-CoA hydrolase; HIBYL-CoA-H; EC 3.1.2.4 from Saccharomyces cerevisiae

 26% id,
41% cov

SMc04398: enoyl-CoA hydratase
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.

 30% id,
99% cov

SM_b21126: enoyl-CoA hydratase
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.

 30% id,
96% cov

HIBC1_ARATH / Q9LKJ1: 3-hydroxyisobutyryl-CoA hydrolase 1; CoA-thioester hydrolase CHY1; EC 3.1.2.-; EC 3.1.2.4 from Arabidopsis thaliana
Q9LKJ1: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Arabidopsis thaliana

 28% id,
69% cov

SMc02227: fatty oxidation complex enoyl-COA hydratase/3-hydroxyacyl-COA dehydrogenase/3-hydroxybutyryl-COA epimerase
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.

 26% id,
94% cov

PGA1_c17350: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Phaeobacter inhibens

 24% id,
95% cov

SMa1408: dehydratase
is similar to:		 PaperBLAST

C3KM96: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Sinorhizobium fredii

 30% id,
72% cov

Psest_2439: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Pseudomonas stutzeri

 29% id,
70% cov

RR42_RS28545: 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) from Cupriavidus basilensis

 28% id,
66% cov

More...

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 9 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory