Searching in Herbaspirillum aquaticum IEH 4430 (GCF_002213425.1)
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 7 relevant proteins in Herbaspirillum aquaticum IEH 4430, or try another query
| CEJ45_RS08600 CEJ45_08610 WP_088754739.1: FAD-binding oxidoreductase is similar to: | PaperBLAST |
SMc04384: (R)-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Sinorhizobium meliloti | 42% id, 99% cov |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 33% id, 96% 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 |
| CEJ45_RS09745 CEJ45_09755 WP_088754936.1: FAD-binding oxidoreductase is similar to: | PaperBLAST |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 41% 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 | 37% id, 100% cov |
Q9I6H4: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas aeruginosa | 37% id, 98% cov |
| CEJ45_RS15240 CEJ45_15245 WP_088755932.1: FAD-binding oxidoreductase is similar to: | PaperBLAST |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 35% 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 | 34% id, 98% cov |
D2HDH_HUMAN / Q8N465: D-2-hydroxyglutarate dehydrogenase, mitochondrial; EC 1.1.99.39 from Homo sapiens | 37% id, 87% cov |
| CEJ45_RS13990 CEJ45_13995 WP_088755700.1: FAD-linked oxidase C-terminal domain-containing protein 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 | 31% id, 98% cov |
Q9I6H4: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas aeruginosa | 30% id, 99% cov |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 29% id, 96% cov |
| CEJ45_RS14000 CEJ45_14005 WP_088755702.1: FAD-linked oxidase C-terminal domain-containing protein 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 | 30% id, 99% cov |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 30% id, 97% cov |
Q9I6H4: D-2-hydroxyglutarate dehydrogenase (EC 1.1.99.39) from Pseudomonas aeruginosa | 28% id, 99% cov |
| glcE CEJ45_RS13985 CEJ45_13990 WP_088755699.1: glycolate oxidase subunit GlcE is similar to: | PaperBLAST |
D2HDH_ARATH / O23240: D-2-hydroxyglutarate dehydrogenase, mitochondrial; AtD-2HGDH; EC 1.1.99.39 from Arabidopsis thaliana | 26% id, 44% cov |
D2HDH_RAT / P84850: D-2-hydroxyglutarate dehydrogenase, mitochondrial; EC 1.1.99.39 from Rattus norvegicus | 29% id, 32% cov |
| CEJ45_RS16430 CEJ45_16430 WP_088756132.1: FAD/FMN-binding oxidoreductase is similar to: | PaperBLAST |
D2HDH_XANCL / P0DV35: D-2-hydroxyglutarate dehydrogenase; D2HGDH; EC 1.1.99.39 from Xanthomonas citri | 29% id, 32% cov |
D2HDH_ARATH / O23240: D-2-hydroxyglutarate dehydrogenase, mitochondrial; AtD-2HGDH; EC 1.1.99.39 from Arabidopsis thaliana | 26% id, 33% cov |
D2HDH_HUMAN / Q8N465: D-2-hydroxyglutarate dehydrogenase, mitochondrial; EC 1.1.99.39 from Homo sapiens | 27% id, 28% 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 7 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory