Curated BLAST for Genomes

 

Curated BLAST

Searching in Methylohalobius crimeensis 10Ki (GCF_000421465.1)

Found 7 curated entries in PaperBLAST's database that match '2.6.1.78' as complete word(s).

These curated entries have 5 distinct sequences.

Running ublast with E ≤ 0.01

Found 5 relevant proteins in Methylohalobius crimeensis 10Ki, or try another query

H035_RS0116640 WP_022950092.1: pyridoxal phosphate-dependent aminotransferase
is similar to:
PaperBLAST

Q02635: aspartate transaminase (EC 2.6.1.1); aspartate-prephenate aminotransferase (EC 2.6.1.78); glutamate-prephenate aminotransferase (EC 2.6.1.79) from Sinorhizobium meliloti

53% id,
98% cov

AAPAT_CHLTE / Q8KDS8: Aspartate/prephenate aminotransferase; AspAT / PAT; EC 2.6.1.1; EC 2.6.1.78 from Chlorobaculum tepidum

51% id,
97% cov

AAPAT_THET8 / Q56232: Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.78 from Thermus thermophilus
Q56232: aspartate-prephenate aminotransferase (EC 2.6.1.78) from Thermus thermophilus

45% id,
98% cov

More...

H035_RS0108005 WP_022948472.1: pyridoxal phosphate-dependent aminotransferase
is similar to:
PaperBLAST

AAPAT_THET8 / Q56232: Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.78 from Thermus thermophilus
Q56232: aspartate-prephenate aminotransferase (EC 2.6.1.78) from Thermus thermophilus

34% id,
100% cov

AAPAT_CHLTE / Q8KDS8: Aspartate/prephenate aminotransferase; AspAT / PAT; EC 2.6.1.1; EC 2.6.1.78 from Chlorobaculum tepidum

31% id,
96% cov

Q02635: aspartate transaminase (EC 2.6.1.1); aspartate-prephenate aminotransferase (EC 2.6.1.78); glutamate-prephenate aminotransferase (EC 2.6.1.79) from Sinorhizobium meliloti

30% id,
97% cov

More...

H035_RS0106610 WP_022948202.1: pyridoxal phosphate-dependent aminotransferase
is similar to:
PaperBLAST

AAPAT_THET8 / Q56232: Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.78 from Thermus thermophilus
Q56232: aspartate-prephenate aminotransferase (EC 2.6.1.78) from Thermus thermophilus

36% id,
93% cov

AAPAT_CHLTE / Q8KDS8: Aspartate/prephenate aminotransferase; AspAT / PAT; EC 2.6.1.1; EC 2.6.1.78 from Chlorobaculum tepidum

35% id,
94% cov

Q02635: aspartate transaminase (EC 2.6.1.1); aspartate-prephenate aminotransferase (EC 2.6.1.78); glutamate-prephenate aminotransferase (EC 2.6.1.79) from Sinorhizobium meliloti

31% id,
93% cov

More...

alaC H035_RS0111195 WP_022949065.1: alanine transaminase
is similar to:
PaperBLAST

AAPAT_THET8 / Q56232: Aspartate/prephenate aminotransferase; AspAT / PAT; Transaminase A; EC 2.6.1.1; EC 2.6.1.78 from Thermus thermophilus
Q56232: aspartate-prephenate aminotransferase (EC 2.6.1.78) from Thermus thermophilus

31% id,
98% cov

Q02635: aspartate transaminase (EC 2.6.1.1); aspartate-prephenate aminotransferase (EC 2.6.1.78); glutamate-prephenate aminotransferase (EC 2.6.1.79) from Sinorhizobium meliloti

27% id,
97% cov

AAPAT_CHLTE / Q8KDS8: Aspartate/prephenate aminotransferase; AspAT / PAT; EC 2.6.1.1; EC 2.6.1.78 from Chlorobaculum tepidum

28% id,
89% cov

More...

dapC H035_RS0112235 WP_022949262.1: succinyldiaminopimelate transaminase
is similar to:
PaperBLAST

PAT_ARATH / Q9SIE1: Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase; AtAAT; AtPPA-AT; Protein MATERNAL EFFECT EMBRYO ARREST 17; EC 2.6.1.1; EC 2.6.1.78; EC 2.6.1.79 from Arabidopsis thaliana
Q9SIE1: aspartate transaminase (EC 2.6.1.1); aspartate-prephenate aminotransferase (EC 2.6.1.78); glutamate-prephenate aminotransferase (EC 2.6.1.79) from Arabidopsis thaliana

26% id,
82% cov

PAT_PETHY / E9L7A5: Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase; PhPPA-AT; EC 2.6.1.1; EC 2.6.1.78; EC 2.6.1.79 from Petunia hybrida

26% id,
82% 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 5 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory