Curated BLAST for Genomes

 

Curated BLAST

Searching in Thiomicrorhabdus arctica DSM 13458 (GCF_000381085.1)

Found 2 curated entries in PaperBLAST's database that match 'acetohydroxybutanoate synthase, catalytic subunit' as complete word(s).

These curated entries have 1 distinct sequences.

Running ublast with E ≤ 0.01

Found 4 relevant proteins in Thiomicrorhabdus arctica DSM 13458, or try another query

F612_RS0100795 WP_019555837.1: acetolactate synthase 3 large subunit
is similar to:
PaperBLAST

IlvI / b0077: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli
ilvI / P00893: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli

61% id,
99% cov

F612_RS0110970 WP_019557819.1: acetolactate synthase large subunit
is similar to:
PaperBLAST

IlvI / b0077: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli
ilvI / P00893: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli

33% id,
98% cov

F612_RS0106535 WP_169335986.1: thiamine pyrophosphate-binding protein
is similar to:
PaperBLAST

IlvI / b0077: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli
ilvI / P00893: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli

28% id,
93% cov

F612_RS0108960 WP_019557431.1: acetolactate synthase large subunit
is similar to:
PaperBLAST

IlvI / b0077: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli
ilvI / P00893: acetolactate synthase / acetohydroxybutanoate synthase, catalytic subunit (EC 2.2.1.6) from Escherichia coli

26% id,
99% 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