Curated BLAST for Genomes

 

Curated BLAST

Searching in Xanthobacter autotrophicus Py2 (GCF_000017645.1)

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 Xanthobacter autotrophicus Py2, or try another query

XAUT_RS07445 Xaut_1488 WP_041576535.1: 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

52% id,
99% cov

gcl XAUT_RS11905 Xaut_2367 WP_012114387.1: glyoxylate carboligase
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

32% id,
95% cov

XAUT_RS14070 Xaut_2795 WP_012114786.1: 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

31% id,
96% cov

oxc XAUT_RS02450 Xaut_0486 WP_011996144.1: oxalyl-CoA decarboxylase
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

25% id,
96% 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