Searching in Klebsiella michiganensis M5al (Koxy)
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 8 relevant proteins in Klebsiella michiganensis M5al, or try another query
BWI76_RS18935: bifunctional imidazole glycerol-phosphate dehydratase/histidinol phosphatase is similar to: | PaperBLAST |
HisB / b2022: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli | 88% id, 100% cov |
HIS7_ECO57 / Q9S5G5: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Escherichia coli | 87% id, 100% cov |
HIS7_SPILD / D2QPE6: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Spirosoma linguale | 48% id, 100% cov |
BWI76_RS06160: alkaline phosphatase is similar to: | PaperBLAST |
PsiA / b0383: alkaline phosphatase (EC 3.1.3.1; EC 3.1.3.75; EC 3.1.3.41; EC 3.1.3.74; EC 3.1.3.99; EC 3.1.3.5; EC 3.1.3.6; EC 3.1.3.89; EC 3.1.3.91; EC 3.1.3.60; EC 3.1.3.15; EC 3.1.3.102; EC 3.1.3.108; EC 3.1.3.11; EC 3.1.3.20; EC 3.1.3.19; EC 3.1.3.3; EC 3.6.1.25; EC 3.6.1.1; EC 3.1.3.23; EC 3.1.3.38; EC 3.1.3.18; EC 3.1.3.68; EC 3.9.1.1) from Escherichia coli | 87% id, 100% cov |
BWI76_RS05890: haloacid dehalogenase is similar to: | PaperBLAST |
HP15_461: Histidinol-phosphatase (EC:3.1.3.15) from Marinobacter adhaerens | 37% id, 99% cov |
HIS9_PSEAE / Q9I6F6: Histidinol-phosphatase; Hol-Pase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Pseudomonas aeruginosa | 33% id, 99% cov |
HIS9_NEIM8 / P0DV34: Histidinol-phosphatase; Hol-Pase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Neisseria meningitidis | 33% id, 100% cov |
BWI76_RS07840: inositol monophosphatase family protein is similar to: | PaperBLAST |
HISN_MYCTU / P95189: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis | 32% id, 96% cov |
AZOBR_RS03845: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Azospirillum brasilense | 32% id, 86% cov |
PGA1_c21860: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Phaeobacter inhibens | 27% id, 96% cov |
BWI76_RS21175: inositol monophosphatase is similar to: | PaperBLAST |
AZOBR_RS03845: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Azospirillum brasilense | 30% id, 97% cov |
Ga0059261_2035: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Sphingomonas koreensis | 30% id, 95% cov |
HISN_MYCTU / P95189: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis | 28% id, 94% cov |
BWI76_RS02735: 3'(2'),5'-bisphosphate nucleotidase CysQ is similar to: | PaperBLAST |
HISN_MYCTU / P95189: Histidinol-phosphatase; HolPase; Histidinol-phosphate phosphatase; EC 3.1.3.15 from Mycobacterium tuberculosis | 32% id, 85% cov |
Ga0059261_2035: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Sphingomonas koreensis | 30% id, 84% cov |
PGA1_c21860: Histidinol-phosphatase [alternative form] (EC 3.1.3.15) from Phaeobacter inhibens | 29% id, 89% cov |
BWI76_RS10895: phosphatase is similar to: | PaperBLAST |
hisK / Q5SLG2: histidinol phosphate phosphatase subunit (EC 3.1.3.15) from Thermus thermophilus | 27% id, 93% cov |
BWI76_RS05370: D-glycero-beta-D-manno-heptose 1,7-bisphosphate 7-phosphatase is similar to: | PaperBLAST |
HIS7_ECO57 / Q9S5G5: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Escherichia coli | 34% id, 41% cov |
HisB / b2022: imidazoleglycerol-phosphate dehydratase / histidinol-phosphatase (EC 4.2.1.19; EC 3.1.3.15) from Escherichia coli | 34% id, 40% cov |
HIS7_SPILD / D2QPE6: Histidine biosynthesis bifunctional protein HisB; EC 3.1.3.15; EC 4.2.1.19 from Spirosoma linguale | 32% id, 37% 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 8 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory