Curated BLAST for Genomes

 

Curated BLAST

Searching in Clostridium acetobutylicum ATCC 824 (GCF_000008765.1)

Found 22 curated entries in PaperBLAST's database that match '2.6.1.11' as complete word(s).

These curated entries have 14 distinct sequences.

Running ublast with E ≤ 0.01

Found 5 relevant proteins in Clostridium acetobutylicum ATCC 824, or try another query

CA_RS12260 CA_C2388 WP_010965684.1: aspartate aminotransferase family protein
is similar to:		 PaperBLAST

2ordA / Q9X2A5: Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution

 53% id,
97% cov

HP15_3042: acetylornithine aminotransferase (EC 2.6.1.11); succinylornithine aminotransferase (EC 2.6.1.81) from Marinobacter adhaerens

 47% id,
92% cov

ARUC_PSEAE / O30508: Succinylornithine transaminase/acetylornithine aminotransferase; ACOAT; SOAT; Succinylornithine aminotransferase; EC 2.6.1.11; EC 2.6.1.81 from Pseudomonas aeruginosa
aruC / O30508: succinylornithine transaminase subunit (EC 2.6.1.13; EC 2.6.1.11; EC 2.6.1.81) from Pseudomonas aeruginosa

 46% id,
95% cov

More...

gabT CA_RS07495 CA_C1427 WP_010964736.1: 4-aminobutyrate--2-oxoglutarate transaminase
is similar to:		 PaperBLAST

GabT / b2662: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli
gabT / P22256: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli

 42% id,
98% cov

AstC / b1748: succinylornithine transaminase (EC 2.6.1.81; EC 2.6.1.11) from Escherichia coli
astC / P77581: succinylornithine transaminase (EC 2.6.1.81; EC 2.6.1.11) from Escherichia coli

 34% id,
92% cov

HP15_3042: acetylornithine aminotransferase (EC 2.6.1.11); succinylornithine aminotransferase (EC 2.6.1.81) from Marinobacter adhaerens

 32% id,
98% cov

More...

CA_RS02090 CA_C0368 WP_014518834.1: aspartate aminotransferase family protein
is similar to:		 PaperBLAST

GabT / b2662: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli
gabT / P22256: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli

 40% id,
97% cov

2ordA / Q9X2A5: Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution

 41% id,
93% cov

B1XNF8: acetylornithine transaminase (EC 2.6.1.11); 4-aminobutyrate-2-oxoglutarate transaminase (EC 2.6.1.19) from Synechococcus sp.

 40% id,
91% cov

More...

hemL CA_RS00545 CA_C0099 WP_010963426.1: glutamate-1-semialdehyde 2,1-aminomutase
is similar to:		 PaperBLAST

AstC / b1748: succinylornithine transaminase (EC 2.6.1.81; EC 2.6.1.11) from Escherichia coli
astC / P77581: succinylornithine transaminase (EC 2.6.1.81; EC 2.6.1.11) from Escherichia coli

 33% id,
91% cov

2ordA / Q9X2A5: Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution

 28% id,
94% cov

HP15_3042: acetylornithine aminotransferase (EC 2.6.1.11); succinylornithine aminotransferase (EC 2.6.1.81) from Marinobacter adhaerens

 31% id,
80% cov

More...

bioA CA_RS07165 CA_C1362 WP_010964671.1: adenosylmethionine--8-amino-7-oxononanoate transaminase
is similar to:		 PaperBLAST

GabT / b2662: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli
gabT / P22256: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19; EC 2.6.1.48; EC 2.6.1.11) from Escherichia coli

 30% id,
95% cov

AZOBR_RS19025: acetylornithine/N-succinyldiaminopimelate aminotransferase [EC:2.6.1.11 2.6.1.17] from Azospirillum brasilense

 30% id,
94% cov

2ordA / Q9X2A5: Crystal structure of acetylornithine aminotransferase (ec 2.6.1.11) (acoat) (tm1785) from thermotoga maritima at 1.40 a resolution

 27% id,
96% cov

More...

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.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory