Curated BLAST for Genomes

 

Curated BLAST

Searching in Pseudomonas fluorescens GW456-L13 (pseudo13_GW456_L13)

Found 23 curated entries in PaperBLAST's database that match '2.6.1.9' as complete word(s).

These curated entries have 20 distinct sequences.

Running ublast with E ≤ 0.01

Found 8 relevant proteins in Pseudomonas fluorescens GW456-L13, or try another query

PfGW456L13_4999: Histidinol-phosphate aminotransferase (EC 2.6.1.9)
is similar to:
PaperBLAST

Pf6N2E2_3251: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Pseudomonas fluorescens

94% id,
100% cov

PP_0967: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Pseudomonas putida

83% id,
100% cov

Psest_3297: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Pseudomonas stutzeri

81% id,
100% cov

More...

PfGW456L13_2177: Biosynthetic Aromatic amino acid aminotransferase beta (EC 2.6.1.57)
is similar to:
PaperBLAST

hisC / P17731: histidinol-phosphate aminotransferase; tyrosine/phenylalanine aminotransferase (promiscuous) (EC 2.6.1.1; EC 2.6.1.9) from Bacillus subtilis

42% id,
98% cov

AZOBR_RS20485: histidinol-phosphate aminotransferase [EC:2.6.1.9] from Azospirillum brasilense

39% id,
97% cov

PGA1_c25240: histidinol-phosphate aminotransferase [EC:2.6.1.9] from Phaeobacter inhibens

40% id,
93% cov

More...

PfGW456L13_1928: Uncharacterized PLP-dependent aminotransferase YfdZ
is similar to:
PaperBLAST

HP15_2427: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Marinobacter adhaerens

29% id,
84% cov

PP_0967: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Pseudomonas putida

28% id,
85% cov

Psest_3297: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Pseudomonas stutzeri

28% id,
78% cov

More...

PfGW456L13_2252: Aspartate aminotransferase (EC 2.6.1.1)
is similar to:
PaperBLAST

AZOBR_RS20485: histidinol-phosphate aminotransferase [EC:2.6.1.9] from Azospirillum brasilense

25% id,
87% cov

PfGW456L13_4856: Aspartate aminotransferase (EC 2.6.1.1)
is similar to:
PaperBLAST

AZOBR_RS20485: histidinol-phosphate aminotransferase [EC:2.6.1.9] from Azospirillum brasilense

24% id,
90% cov

HIS8_ZYMMO / P34037: Histidinol-phosphate aminotransferase; Imidazole acetol phosphate aminotransferase; IAP aminotransferase; Imidazole acetol-phosphate transaminase; EC 2.6.1.9 from Zymomonas mobilis

25% id,
67% cov

PfGW456L13_1529: Valine--pyruvate aminotransferase (EC 2.6.1.66)
is similar to:
PaperBLAST

AZOBR_RS20485: histidinol-phosphate aminotransferase [EC:2.6.1.9] from Azospirillum brasilense

27% id,
78% cov

BT0202: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Bacteroides thetaiotaomicron

24% id,
67% cov

PfGW456L13_4239: L-threonine 3-O-phosphate decarboxylase (EC 4.1.1.81)
is similar to:
PaperBLAST

DvMF_0908: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Desulfovibrio vulgaris

30% id,
70% cov

DVU1029: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Desulfovibrio vulgaris

28% id,
72% cov

HIS8_ECOLI / P06986: Histidinol-phosphate aminotransferase; Imidazole acetol-phosphate transaminase; HPAT; HspAT; EC 2.6.1.9 from Escherichia coli
HisC / b2021: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Escherichia coli
hisC / P06986: histidinol-phosphate aminotransferase (EC 2.6.1.9) from Escherichia coli

30% id,
69% cov

More...

PfGW456L13_2059: Transcriptional regulator, GntR family domain / Aspartate aminotransferase (EC 2.6.1.1)
is similar to:
PaperBLAST

HIS8_NICPL / Q9FEW2: Histidinol-phosphate aminotransferase, chloroplastic; Imidazole acetol-phosphate transaminase; EC 2.6.1.9 from Nicotiana plumbaginifolia

25% id,
69% cov

HIS8_TOBAC / O82030: Histidinol-phosphate aminotransferase, chloroplastic; Imidazole acetol-phosphate transaminase; EC 2.6.1.9 from Nicotiana tabacum
O82030: histidinol-phosphate transaminase (EC 2.6.1.9) from Nicotiana tabacum

25% id,
69% 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 6 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory