Curated BLAST for Genomes

 

Curated BLAST

Searching in Pseudomonas fluorescens FW300-N1B4 (pseudo1_N1B4)

Found 15 curated entries in PaperBLAST's database that match '1.1.99.39' as complete word(s).

These curated entries have 10 distinct sequences.

Running ublast with E ≤ 0.01

Found 6 relevant proteins in Pseudomonas fluorescens FW300-N1B4, or try another query

Pf1N1B4_2274: D-2-hydroxyglutarate dehydrogenase
is similar to:
PaperBLAST

D2HDH_STUS1 / A4VGK4: D-2-hydroxyglutarate dehydrogenase; D-2-HG dehydrogenase; D2HGDH; D-malate dehydrogenase; EC 1.1.99.39; EC 1.1.99.- from Stutzerimonas stutzeri

92% id,
100% cov

Q9I6H4: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas aeruginosa

89% id,
100% cov

D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri

54% id,
97% cov

More...

Pf1N1B4_4229: Glycolate dehydrogenase (EC 1.1.99.14), subunit GlcD
is similar to:
PaperBLAST

D2HDH_PSEPK / Q88EH0: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Pseudomonas putida
ydiJ / Q88EH0: (R)-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas putida
PP_4493: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas putida

85% id,
94% cov

D2HDH_PANAA / A0A0H3KZS3: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Pantoea ananatis

52% id,
93% cov

D2HDH_ECOLI / P77748: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Escherichia coli
ydiJ / P77748: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Escherichia coli

51% id,
93% cov

Pf1N1B4_4424: D-2-hydroxyglutarate dehydrogenase
is similar to:
PaperBLAST

D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri

41% id,
99% cov

D2HDH_STUS1 / A4VGK4: D-2-hydroxyglutarate dehydrogenase; D-2-HG dehydrogenase; D2HGDH; D-malate dehydrogenase; EC 1.1.99.39; EC 1.1.99.- from Stutzerimonas stutzeri

36% id,
100% cov

SMc04384: (R)-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Sinorhizobium meliloti

36% id,
97% cov

More...

Pf1N1B4_5862: Glycolate dehydrogenase (EC 1.1.99.14), subunit GlcD
is similar to:
PaperBLAST

D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri

32% id,
97% cov

D2HDH_STUS1 / A4VGK4: D-2-hydroxyglutarate dehydrogenase; D-2-HG dehydrogenase; D2HGDH; D-malate dehydrogenase; EC 1.1.99.39; EC 1.1.99.- from Stutzerimonas stutzeri

30% id,
98% cov

Q9I6H4: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas aeruginosa

29% id,
99% cov

More...

Pf1N1B4_1190: Predicted D-lactate dehydrogenase, Fe-S protein, FAD/FMN-containing
is similar to:
PaperBLAST

D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri

26% id,
62% cov

D2HDH_ARATH / O23240: D-2-hydroxyglutarate dehydrogenase, mitochondrial; AtD-2HGDH; EC 1.1.99.39 from Arabidopsis thaliana

29% id,
48% cov

D2HDH_STUS1 / A4VGK4: D-2-hydroxyglutarate dehydrogenase; D-2-HG dehydrogenase; D2HGDH; D-malate dehydrogenase; EC 1.1.99.39; EC 1.1.99.- from Stutzerimonas stutzeri

23% id,
61% cov

More...

Pf1N1B4_4228: Glycolate dehydrogenase (EC 1.1.99.14), subunit GlcD
is similar to:
PaperBLAST

D2HDH_PSEPK / Q88EH0: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Pseudomonas putida
ydiJ / Q88EH0: (R)-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas putida
PP_4493: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas putida

84% id,
6% cov

D2HDH_ECOLI / P77748: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Escherichia coli
ydiJ / P77748: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Escherichia coli

48% id,
6% cov

D2HDH_PANAA / A0A0H3KZS3: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Pantoea ananatis

48% id,
6% 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 6 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory