Curated BLAST for Genomes

 

Curated BLAST

Searching in Escherichia coli BW25113 (Keio)

Found 3 curated entries in PaperBLAST's database that match '2.6.1.84' as complete word(s).

These curated entries have 1 distinct sequences.

Running ublast with E ≤ 0.01

Found 4 relevant proteins in Escherichia coli BW25113, or try another query

b0600: putative aminotransferase (NCBI)
is similar to:
PaperBLAST

ARUH_PSEAE / Q9HUI9: Arginine--pyruvate transaminase AruH; EC 2.6.1.84 from Pseudomonas aeruginosa
aruH / Q9HUI9: L-arginine:pyruvate transaminase subunit (EC 2.6.1.84) from Pseudomonas aeruginosa
Q9HUI9: arginine-pyruvate transaminase (EC 2.6.1.84) from Pseudomonas aeruginosa

32% id,
91% cov

b2379: hypothetical protein (NCBI)
is similar to:
PaperBLAST

ARUH_PSEAE / Q9HUI9: Arginine--pyruvate transaminase AruH; EC 2.6.1.84 from Pseudomonas aeruginosa
aruH / Q9HUI9: L-arginine:pyruvate transaminase subunit (EC 2.6.1.84) from Pseudomonas aeruginosa
Q9HUI9: arginine-pyruvate transaminase (EC 2.6.1.84) from Pseudomonas aeruginosa

30% id,
91% cov

b4340: fused predicted DNA-binding transcriptional regulator/predicted aminotransferase (NCBI)
is similar to:
PaperBLAST

ARUH_PSEAE / Q9HUI9: Arginine--pyruvate transaminase AruH; EC 2.6.1.84 from Pseudomonas aeruginosa
aruH / Q9HUI9: L-arginine:pyruvate transaminase subunit (EC 2.6.1.84) from Pseudomonas aeruginosa
Q9HUI9: arginine-pyruvate transaminase (EC 2.6.1.84) from Pseudomonas aeruginosa

28% id,
96% cov

b2290: aspartate aminotransferase (NCBI)
is similar to:
PaperBLAST

ARUH_PSEAE / Q9HUI9: Arginine--pyruvate transaminase AruH; EC 2.6.1.84 from Pseudomonas aeruginosa
aruH / Q9HUI9: L-arginine:pyruvate transaminase subunit (EC 2.6.1.84) from Pseudomonas aeruginosa
Q9HUI9: arginine-pyruvate transaminase (EC 2.6.1.84) from Pseudomonas aeruginosa

29% id,
86% 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.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory