Searching in Echinicola vietnamensis KMM 6221, DSM 17526 (Cola)
Found 13 curated entries in PaperBLAST's database that match '2.7.1.92' as complete word(s).
These curated entries have 11 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Echinicola vietnamensis KMM 6221, DSM 17526, or try another query
| Echvi_0561: Sugar kinases, ribokinase family is similar to: | PaperBLAST |
IOLC_BACSU / P42414: 5-dehydro-2-deoxygluconokinase; 2-deoxy-5-keto-D-gluconate kinase; DKG kinase; EC 2.7.1.92 from Bacillus subtilis | 27% id, 83% cov |
| Echvi_0156: Sugar kinases, ribokinase family is similar to: | PaperBLAST |
SMc01165: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Sinorhizobium meliloti | 27% id, 47% cov |
HSERO_RS12125: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Herbaspirillum seropedicae | 27% id, 46% cov |
AO353_21335: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Pseudomonas fluorescens | 25% id, 47% cov |
| Echvi_2804: Sugar kinases, ribokinase family is similar to: | PaperBLAST |
BPHYT_RS13910: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Burkholderia phytofirmans | 26% id, 44% cov |
Pf6N2E2_512: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Pseudomonas fluorescens | 23% id, 46% cov |
BWI76_RS03085: 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92); possible 5-dehydro-2-deoxyphosphogluconate aldolase DUF2090 (EC 4.1.2.29) from Klebsiella michiganensis | 23% id, 47% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory