Searching in Phaeobacter inhibens BS107 (Phaeo)
Found 9 curated entries in PaperBLAST's database that match '1.1.1.343' as complete word(s).
These curated entries have 6 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Phaeobacter inhibens BS107, or try another query
PGA1_c07180: 2-hydroxy-3-oxopropionate reductase-like protein is similar to: | PaperBLAST |
6PGD_HALVD / D4GST8: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating; 6PGDH; EC 1.1.1.343 from Haloferax volcanii | 24% id, 97% cov |
PGA1_c17360: 3-hydroxyisobutyrate dehydrogenase MmsB is similar to: | PaperBLAST |
6PGDH_GLUOX / G5EBD7: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating; 6PGDH; EC 1.1.1.343 from Gluconobacter oxydans | 24% id, 94% cov |
A9H324: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) (EC 1.1.1.343) from Gluconacetobacter diazotrophicus | 31% id, 48% cov |
PGA1_c23050: putative 2-hydroxy-3-oxopropionate reductase is similar to: | PaperBLAST |
A9H324: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) (EC 1.1.1.343) from Gluconacetobacter diazotrophicus | 24% id, 86% cov |
A0A1J5NX54: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) (EC 1.1.1.343); phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) (EC 1.1.1.44) from Moorella thermoacetica | 30% id, 65% cov |
6PGDH_GLUOX / G5EBD7: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating; 6PGDH; EC 1.1.1.343 from Gluconobacter oxydans | 25% id, 67% cov |
PGA1_c14880: putative 3-hydroxyisobutyrate dehydrogenase is similar to: | PaperBLAST |
Q9WYR9: phosphogluconate dehydrogenase (NAD+-dependent, decarboxylating) (EC 1.1.1.343); phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating) (EC 1.1.1.44) from Thermotoga maritima | 40% id, 9% 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 4 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory