Searching in Paraburkholderia bryophila 376MFSha3.1 (Burk376)
Found 21 curated entries in PaperBLAST's database that match '4.1.3.39' as complete word(s).
These curated entries have 13 distinct sequences.
Running ublast with E ≤ 0.01
Found 9 relevant proteins in Paraburkholderia bryophila 376MFSha3.1, or try another query
H281DRAFT_01666: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) is similar to: | PaperBLAST |
HOA_ECOLI / P51020: 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Escherichia coli | 84% id, 99% cov |
todH / P51018: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Pseudomonas putida | 83% id, 97% cov |
xylK / P51019: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Pseudomonas putida | 80% id, 98% cov |
H281DRAFT_03252: 2,4-dihydroxyhept-2-enedioate aldolase (EC 4.1.2.-) is similar to: | PaperBLAST |
Q47098: 4-hydroxy-2-oxoheptanedioate aldolase (EC 4.1.2.52); 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Escherichia coli | 60% id, 97% cov |
BPHF_RHOJR / O05151: 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.39 from Rhodococcus jostii | 56% id, 100% cov |
H281DRAFT_05315: 5-dehydro-4-deoxy-D-glucarate aldolase (EC 4.1.2.20) is similar to: | PaperBLAST |
Q47098: 4-hydroxy-2-oxoheptanedioate aldolase (EC 4.1.2.52); 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Escherichia coli | 48% id, 95% cov |
BPHF_RHOJR / O05151: 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.39 from Rhodococcus jostii | 44% id, 98% cov |
H281DRAFT_02229: 2-dehydro-3-deoxyglucarate aldolase is similar to: | PaperBLAST |
Q47098: 4-hydroxy-2-oxoheptanedioate aldolase (EC 4.1.2.52); 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Escherichia coli | 42% id, 93% cov |
BPHF_RHOJR / O05151: 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.39 from Rhodococcus jostii | 38% id, 95% cov |
H281DRAFT_03361: 2-keto-3-deoxy-L-rhamnonate aldolase RhmA is similar to: | PaperBLAST |
Q47098: 4-hydroxy-2-oxoheptanedioate aldolase (EC 4.1.2.52); 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Escherichia coli | 32% id, 94% cov |
H281DRAFT_05453: 4-hydroxy-2-oxoheptanedioate aldolase is similar to: | PaperBLAST |
Q47098: 4-hydroxy-2-oxoheptanedioate aldolase (EC 4.1.2.52); 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Escherichia coli | 29% id, 91% cov |
BPHF_RHOJR / O05151: 4-hydroxy-2-oxovalerate aldolase; HOA; EC 4.1.3.39 from Rhodococcus jostii | 32% id, 80% cov |
H281DRAFT_04556: 2-isopropylmalate synthase is similar to: | PaperBLAST |
P51017: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Pseudomonas putida | 27% id, 95% cov |
HOA_PSEUF / P51016: 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Pseudomonas sp. | 30% id, 38% cov |
H281DRAFT_04763: hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) is similar to: | PaperBLAST |
HOA_PSEUF / P51016: 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Pseudomonas sp. | 23% id, 86% cov |
HOA_ECOLI / P51020: 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39 from Escherichia coli | 23% id, 80% cov |
todH / P51018: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Pseudomonas putida | 24% id, 77% cov |
H281DRAFT_00385: 2-isopropylmalate synthase is similar to: | PaperBLAST |
P51017: 4-hydroxy-2-oxovalerate aldolase (EC 4.1.3.39) from Pseudomonas putida | 35% id, 20% cov |
HOA4_PARXL / P51015: 4-hydroxy-2-oxovalerate aldolase 4; HOA 4; 4-hydroxy-2-keto-pentanoic acid aldolase 4; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase 4; EC 4.1.3.39; EC 4.1.3.43 from Paraburkholderia xenovorans | 28% id, 20% 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 9 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory