Curated BLAST for Genomes

 

Curated BLAST

Searching in Pseudomonas fluorescens GW456-L13 (pseudo13_GW456_L13)

Found 17 curated entries in PaperBLAST's database that match '2.4.2.18' as complete word(s).

These curated entries have 11 distinct sequences.

Running ublast with E ≤ 0.01

Found 3 relevant proteins in Pseudomonas fluorescens GW456-L13, or try another query

PfGW456L13_1221: Anthranilate phosphoribosyltransferase (EC 2.4.2.18)
is similar to:
PaperBLAST

TRPD_XANCP / Q8PD71: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Xanthomonas campestris

48% id,
97% cov

TRPD_THET8 / Q5SH88: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Thermus thermophilus
TRPD_THETH / P83827: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Thermus thermophilus

42% id,
95% cov

Q9YGB4: anthranilate phosphoribosyltransferase (EC 2.4.2.18) from Thermococcus kodakarensis

38% id,
99% cov

More...

PfGW456L13_2658: Anthranilate phosphoribosyltransferase like (EC 2.4.2.18)
is similar to:
PaperBLAST

TRPD_SACS2 / P50384: Anthranilate phosphoribosyltransferase; EC 2.4.2.18 from Saccharolobus solfataricus
P50384: anthranilate phosphoribosyltransferase (EC 2.4.2.18) from Saccharolobus solfataricus

24% id,
63% cov

PfGW456L13_1220: Anthranilate synthase, amidotransferase component (EC 4.1.3.27) @ Para-aminobenzoate synthase, amidotransferase component (EC 2.6.1.85)
is similar to:
PaperBLAST

TRPGD_ECOLI / P00904: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Escherichia coli
TrpD / b1263: anthranilate synthase subunit TrpD (EC 2.4.2.18; EC 4.1.3.27) from Escherichia coli
trpD / P00904: anthranilate synthase subunit TrpD (EC 2.4.2.18) from Escherichia coli

42% id,
34% cov

TRPGD_SALTY / P00905: Bifunctional protein TrpGD; EC 4.1.3.27; EC 2.4.2.18 from Salmonella typhimurium

41% id,
34% 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 2 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory