Curated BLAST for Genomes

 

Curated BLAST

Searching in Paraburkholderia bryophila 376MFSha3.1 (Burk376)

Found 35 curated entries in PaperBLAST's database that match '2.3.3.9' as complete word(s).

These curated entries have 22 distinct sequences.

Running ublast with E ≤ 0.01

Found 8 relevant proteins in Paraburkholderia bryophila 376MFSha3.1, or try another query

H281DRAFT_00576: malate synthase
is similar to:
PaperBLAST

BPHYT_RS12305: Malate synthase (EC 2.3.3.9) from Burkholderia phytofirmans

94% id,
100% cov

Q5YLB8: malate synthase (EC 2.3.3.9) from Paracoccidioides brasiliensis

56% id,
94% cov

acuE: malate synthase; EC 2.3.3.9 from Emericella nidulans

56% id,
94% cov

More...

H281DRAFT_00963: malate synthase
is similar to:
PaperBLAST

Psest_0354: Malate synthase G (EC 2.3.3.9) from Pseudomonas stutzeri

66% id,
100% cov

MASZ_ECOLI / P37330: Malate synthase G; MSG; EC 2.3.3.9 from Escherichia coli
Glc / b2976: malate synthase G (EC 2.3.3.9) from Escherichia coli
glcB / P37330: malate synthase G (EC 2.3.3.9) from Escherichia coli

65% id,
100% cov

MASZ_MYCTO / P9WK16: Malate synthase G; EC 2.3.3.9 from Mycobacterium tuberculosis
MASZ_MYCTU / P9WK17: Malate synthase G; EC 2.3.3.9 from Mycobacterium tuberculosis
glcB / P9WK17: malate synthase G (EC 2.3.3.9) from Mycobacterium tuberculosis
P9WK17: malate synthase (EC 2.3.3.9) from Mycobacterium tuberculosis

61% id,
97% cov

More...

H281DRAFT_00580: isocitrate lyase
is similar to:
PaperBLAST

GCP_CAEEL / Q10663: Bifunctional glyoxylate cycle protein; Gex-3-interacting protein 7; EC 4.1.3.1; EC 2.3.3.9 from Caenorhabditis elegans

61% id,
44% cov

H281DRAFT_05549: citrate lyase subunit beta / citryl-CoA lyase
is similar to:
PaperBLAST

CLYBL_MOUSE / Q8R4N0: Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein, mitochondrial; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Mus musculus

29% id,
87% cov

CLYBL_HUMAN / Q8N0X4: Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Homo sapiens
CLYBL / Q8N0X4: malate/β-methylmalate synthase (EC 2.3.3.9) from Homo sapiens

29% id,
87% cov

H281DRAFT_02940: beta-methylmalyl-CoA/L-malyl-CoA lyase (EC 4.1.3.24)
is similar to:
PaperBLAST

CLYBL_HUMAN / Q8N0X4: Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Homo sapiens
CLYBL / Q8N0X4: malate/β-methylmalate synthase (EC 2.3.3.9) from Homo sapiens

30% id,
86% cov

CLYBL_MOUSE / Q8R4N0: Citramalyl-CoA lyase, mitochondrial; (3S)-malyl-CoA thioesterase; Beta-methylmalate synthase; Citrate lyase subunit beta-like protein, mitochondrial; Citrate lyase beta-like; Malate synthase; EC 4.1.3.25; EC 3.1.2.30; EC 2.3.3.-; EC 2.3.3.9 from Mus musculus

29% id,
86% cov

H281DRAFT_02542: 2-Methylisocitrate lyase, PEP mutase family
is similar to:
PaperBLAST

GCP_CAEEL / Q10663: Bifunctional glyoxylate cycle protein; Gex-3-interacting protein 7; EC 4.1.3.1; EC 2.3.3.9 from Caenorhabditis elegans

32% id,
20% cov

H281DRAFT_02892: carboxyvinyl-carboxyphosphonate phosphorylmutase
is similar to:
PaperBLAST

GCP_CAEEL / Q10663: Bifunctional glyoxylate cycle protein; Gex-3-interacting protein 7; EC 4.1.3.1; EC 2.3.3.9 from Caenorhabditis elegans

35% id,
14% cov

H281DRAFT_06209: carboxyvinyl-carboxyphosphonate phosphorylmutase
is similar to:
PaperBLAST

GCP_CAEEL / Q10663: Bifunctional glyoxylate cycle protein; Gex-3-interacting protein 7; EC 4.1.3.1; EC 2.3.3.9 from Caenorhabditis elegans

31% id,
13% 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 8 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory