Curated BLAST
Searching in Dechlorosoma suillum PS (PS)
Found 35 curated entries in PaperBLAST's database that match '1.1.1.3' as complete word(s).
These curated entries have 29 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Dechlorosoma suillum PS, or try another query
Dsui_2907: homoserine dehydrogenase
is similar to: | PaperBLAST |
DHOM_NEIG1 / Q5F8J4: NAD(+)-dependent homoserine dehydrogenase; NAD(+)-dependent HSD; NgHSD; EC 1.1.1.3 from Neisseria gonorrhoeae | 63% id,
100% cov |
Ga0059261_2711: homoserine dehydrogenase (EC 1.1.1.3) from Sphingomonas koreensis | 44% id,
97% cov |
DvMF_1412: homoserine dehydrogenase (EC 1.1.1.3) from Desulfovibrio vulgaris | 44% id,
94% cov |
D8WXQ1: homoserine dehydrogenase (EC 1.1.1.3) from Bacillus methanolicus | 40% id,
99% cov |
Q56R01: homoserine dehydrogenase (EC 1.1.1.3) from Streptomyces clavuligerus | 40% id,
99% cov |
DHOM_CORGL / P08499: Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Corynebacterium glutamicum
P08499: homoserine dehydrogenase (EC 1.1.1.3) from Corynebacterium glutamicum | 40% id,
96% cov |
DHOM_BACSU / P19582: Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Bacillus subtilis
P19582: homoserine dehydrogenase (EC 1.1.1.3) from Bacillus subtilis | 38% id,
99% cov |
P46806: homoserine dehydrogenase (EC 1.1.1.3) from Mycobacterium leprae | 38% id,
99% cov |
F9VNG5: homoserine dehydrogenase (EC 1.1.1.3) from Sulfurisphaera tokodaii | 35% id,
98% cov |
A0A0H2WVX4: homoserine dehydrogenase (EC 1.1.1.3) from Staphylococcus aureus | 42% id,
80% cov |
DHOM_LACLC / P52985: Homoserine dehydrogenase; HDH; EC 1.1.1.3 from Lactococcus lactis | 35% id,
96% cov |
Q5SL04: homoserine dehydrogenase (EC 1.1.1.3) from Thermus thermophilus | 36% id,
94% cov |
D8WXQ2: homoserine dehydrogenase (EC 1.1.1.3) from Bacillus methanolicus | 37% id,
82% cov |
O58802: homoserine dehydrogenase (EC 1.1.1.3) from Pyrococcus horikoshii | 28% id,
98% cov |
Q9WZ17: homoserine dehydrogenase (EC 1.1.1.3); aspartate kinase (EC 2.7.2.4) from Thermotoga maritima | 37% id,
54% cov |
CA265_RS23475: aspartate kinase; homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) from Pedobacter sp. | 28% id,
30% cov |
More... |
Dsui_2134: aspartate kinase, monofunctional class
is similar to: | PaperBLAST |
Q9WZ17: homoserine dehydrogenase (EC 1.1.1.3); aspartate kinase (EC 2.7.2.4) from Thermotoga maritima | 42% id,
54% cov |
BT2403: aspartate kinase / homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) from Bacteroides thetaiotaomicron | 30% id,
43% cov |
ThrD / b0002: fused aspartate kinase/homoserine dehydrogenase 1 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli
thrA / P00561: fused aspartate kinase/homoserine dehydrogenase 1 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli
P00561: homoserine dehydrogenase (EC 1.1.1.3); aspartate kinase (EC 2.7.2.4) from Escherichia coli | 31% id,
41% cov |
Echvi_2000: aspartate kinase / homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) from Echinicola vietnamensis | 29% id,
44% cov |
CA265_RS23475: aspartate kinase; homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) from Pedobacter sp. | 29% id,
44% cov |
AKH2_ARATH / O81852: Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana | 28% id,
45% cov |
AKH1_ARATH / Q9SA18: Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic; AK-HD 1; AK-HSDH 1; Beta-aspartyl phosphate homoserine 1; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana | 28% id,
43% cov |
O63067: homoserine dehydrogenase (EC 1.1.1.3) from Glycine max | 30% id,
39% cov |
MetM / b3940: fused aspartate kinase/homoserine dehydrogenase 2 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli
metL / P00562: fused aspartate kinase/homoserine dehydrogenase 2 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli | 23% id,
40% cov |
More... |
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 3 reading frames. These were all redundant with annotated proteins.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory