Searching in Pseudomonas fluorescens GW456-L13 (pseudo13_GW456_L13)
Found 21 curated entries in PaperBLAST's database that match '1.14.13.9' as complete word(s).
These curated entries have 13 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Pseudomonas fluorescens GW456-L13, or try another query
PfGW456L13_899: 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase (EC 1.14.13.-) is similar to: | PaperBLAST |
Q8ISJ5: kynurenine 3-monooxygenase (EC 1.14.13.9) from Anopheles stephensi | 27% id, 74% cov |
KMO_AEDAE / Q86PM2: Kynurenine 3-monooxygenase; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Aedes aegypti | 25% id, 76% cov |
KMO_HUMAN / O15229: Kynurenine 3-monooxygenase; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Homo sapiens | 23% id, 72% cov |
PfGW456L13_2467: 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is similar to: | PaperBLAST |
KMO_PSEFL / Q84HF5: Kynurenine 3-monooxygenase; PfKMO; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Pseudomonas fluorescens | 30% id, 23% cov |
PfGW456L13_2155: tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (EC 2.1.1.61) / FAD-dependent cmnm(5)s(2)U34 oxidoreductase is similar to: | PaperBLAST |
KMO_PSEFL / Q84HF5: Kynurenine 3-monooxygenase; PfKMO; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Pseudomonas fluorescens | 37% id, 17% cov |
orf19.5443: kynurenine 3-monooxygenase; EC 1.14.13.9 from Candida albicans | 33% id, 17% cov |
PfGW456L13_1040: D-amino acid dehydrogenase small subunit (EC 1.4.99.1) is similar to: | PaperBLAST |
KMO_MOUSE / Q91WN4: Kynurenine 3-monooxygenase; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Mus musculus | 35% id, 16% cov |
KMO_RAT / O88867: Kynurenine 3-monooxygenase; Kynurenine 3-hydroxylase; EC 1.14.13.9 from Rattus norvegicus | 34% id, 16% 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