Searching in Herbaspirillum seropedicae SmR1 (HerbieS)
Found 8 curated entries in PaperBLAST's database that match '4.3.1.9' as complete word(s).
These curated entries have 6 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Herbaspirillum seropedicae SmR1, or try another query
HSERO_RS09495: thioredoxin reductase is similar to: | PaperBLAST |
GLCAL_PSEFL / Q93HX6: Glucosaminate ammonia-lyase; D-glucosaminate dehydratase alpha-subunit; GlcNA-DH alpha subunit; GlcNADH-alpha; EC 4.3.1.9 from Pseudomonas fluorescens | 68% id, 98% cov |
HSERO_RS08720: amino acid deaminase is similar to: | PaperBLAST |
AO356_00450: D-glucosaminate dehydratase (EC 4.3.1.9) from Pseudomonas fluorescens | 50% id, 99% cov |
Pf6N2E2_2047: D-glucosaminate dehydratase (EC 4.3.1.9) from Pseudomonas fluorescens | 50% id, 99% cov |
AO353_21740: D-glucosaminate dehydratase (EC 4.3.1.9) from Pseudomonas fluorescens | 50% id, 97% cov |
HSERO_RS21535: NADH dehydrogenase is similar to: | PaperBLAST |
GLCAL_PSEFL / Q93HX6: Glucosaminate ammonia-lyase; D-glucosaminate dehydratase alpha-subunit; GlcNA-DH alpha subunit; GlcNADH-alpha; EC 4.3.1.9 from Pseudomonas fluorescens | 32% id, 95% cov |
HSERO_RS08085: ferredoxin--NADP reductase is similar to: | PaperBLAST |
GLCAL_PSEFL / Q93HX6: Glucosaminate ammonia-lyase; D-glucosaminate dehydratase alpha-subunit; GlcNA-DH alpha subunit; GlcNADH-alpha; EC 4.3.1.9 from Pseudomonas fluorescens | 25% id, 95% cov |
HSERO_RS05720: alanine racemase is similar to: | PaperBLAST |
AO353_21740: D-glucosaminate dehydratase (EC 4.3.1.9) from Pseudomonas fluorescens | 24% id, 87% cov |
PS417_12125 / A0A1N7U313: glucosaminate ammonia-lyase (EC 4.3.1.9) from Pseudomonas simiae | 23% id, 88% cov |
Pf6N2E2_2047: D-glucosaminate dehydratase (EC 4.3.1.9) from Pseudomonas fluorescens | 23% id, 89% 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 5 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory