Curated BLAST for Genomes

 

Curated BLAST

Searching in Pseudomonas fluorescens FW300-N1B4 (pseudo1_N1B4)

Found 30 curated entries in PaperBLAST's database that match '3.1.3.15'.

These curated entries have 23 distinct sequences.

Running ublast with E ≤ 0.01

Found 7 relevant proteins in Pseudomonas fluorescens FW300-N1B4, or try another query

Pf1N1B4_2282: Phosphoserine phosphatase (EC 3.1.3.3)
is similar to:
PaperBLAST

Psest_3864: Histidinol-phosphatase (EC:3.1.3.15) from Pseudomonas stutzeri

73% id,
100% cov

HIS9_PSEAE / Q9I6F6: Histidinol-phosphatase; Hol-Pase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Pseudomonas aeruginosa

73% id,
100% cov

HP15_461: Histidinol-phosphatase (EC:3.1.3.15) from Marinobacter adhaerens

54% id,
100% cov

More...

Pf1N1B4_3743: Phosphoserine phosphatase (EC 3.1.3.3)
is similar to:
PaperBLAST

HIS9_PSEAE / Q9I6F6: Histidinol-phosphatase; Hol-Pase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Pseudomonas aeruginosa

42% id,
98% cov

HP15_461: Histidinol-phosphatase (EC:3.1.3.15) from Marinobacter adhaerens

39% id,
98% cov

Psest_3864: Histidinol-phosphatase (EC:3.1.3.15) from Pseudomonas stutzeri

39% id,
98% cov

More...

Pf1N1B4_869: Inositol-1-monophosphatase (EC 3.1.3.25)
is similar to:
PaperBLAST

PGA1_c21860: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Phaeobacter inhibens

33% id,
98% cov

HISN_STRCO / Q9K4B1: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Streptomyces coelicolor

34% id,
95% cov

HISN_MYCTU / P95189: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis
P95189: histidinol-phosphatase (EC 3.1.3.15) from Mycobacterium tuberculosis

32% id,
97% cov

More...

Pf1N1B4_1668: 3'(2'),5'-bisphosphate nucleotidase (EC 3.1.3.7)
is similar to:
PaperBLAST

AZOBR_RS03845: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Azospirillum brasilense

32% id,
98% cov

HISN_MYCTU / P95189: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis
P95189: histidinol-phosphatase (EC 3.1.3.15) from Mycobacterium tuberculosis

34% id,
89% cov

PGA1_c21860: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Phaeobacter inhibens

32% id,
89% cov

More...

Pf1N1B4_1434: Phosphoserine phosphatase (EC 3.1.3.3)
is similar to:
PaperBLAST

Psest_3864: Histidinol-phosphatase (EC:3.1.3.15) from Pseudomonas stutzeri

29% id,
95% cov

HIS9_PSEAE / Q9I6F6: Histidinol-phosphatase; Hol-Pase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Pseudomonas aeruginosa

26% id,
95% cov

Pf1N1B4_1627: Imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19)
is similar to:
PaperBLAST

HisB / b2022: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli
hisB / P06987: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli

46% id,
56% cov

HIS7_ECO57 / Q9S5G5: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Escherichia coli

46% id,
56% cov

HIS7_SPILD / D2QPE6: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Spirosoma linguale

48% id,
53% cov

More...

Pf1N1B4_1921: D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase (EC 3.1.1.-); Histidinol-phosphatase (EC 3.1.3.15)
is similar to:
PaperBLAST

HisB / b2022: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli
hisB / P06987: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli

31% id,
38% cov

HIS7_ECO57 / Q9S5G5: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Escherichia coli

31% id,
38% 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 7 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory