Curated BLAST for Genomes

 

Curated BLAST

Searching in Calditerrivibrio nitroreducens DSM 19672 (GCF_000183405.1)

Found 21 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 4 relevant proteins in Calditerrivibrio nitroreducens DSM 19672, or try another query

CALNI_RS03705 Calni_0741 WP_013450865.1: 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

 44% id,
97% 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

 44% id,
92% cov

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

 43% id,
94% cov

More...

hemL CALNI_RS07435 Calni_1475 WP_013451594.1: glutamate-1-semialdehyde 2,1-aminomutase
is similar to:		 PaperBLAST

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

 28% id,
98% cov

ARGD_ECOLI / P18335: Acetylornithine/succinyldiaminopimelate aminotransferase; ACOAT; DapATase; Succinyldiaminopimelate transferase; EC 2.6.1.11; EC 2.6.1.17 from Escherichia coli
Dtu / b3359: N-acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase (EC 2.6.1.11; EC 2.6.1.17) from Escherichia coli
argD / P18335: N-acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase (EC 2.6.1.11; EC 2.6.1.17) from Escherichia coli

 33% id,
78% 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

 31% id,
83% cov

More...

CALNI_RS07780 Calni_1542 WP_013451661.1: aminotransferase class III-fold pyridoxal phosphate-dependent enzyme
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

 29% id,
89% 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

 31% id,
77% cov

ARGD_YEAST / P18544: Acetylornithine aminotransferase, mitochondrial; ACOAT; EC 2.6.1.11 from Saccharomyces cerevisiae
ARG8 / P18544: acetylornithine transaminase (EC 2.6.1.11) from Saccharomyces cerevisiae

 27% id,
87% cov

More...

bioA CALNI_RS05270 Calni_1052 WP_013451176.1: adenosylmethionine--8-amino-7-oxononanoate transaminase
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

 27% id,
90% cov

slr1022 / P73133: bifunctional acetylornithine transaminase/4-aminobutyrate—2-oxoglutarate transaminase (EC 2.6.1.19; EC 2.6.1.11) from Synechocystis sp.
P73133: acetylornithine transaminase (EC 2.6.1.11); 4-aminobutyrate-2-oxoglutarate transaminase (EC 2.6.1.19) from Synechococcus sp.

 26% id,
89% cov

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

 26% id,
87% 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 4 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory