Curated BLAST
Searching in Pedobacter sp. GW460-11-11-14-LB5 (Pedo557)
Found 41 curated entries in PaperBLAST's database that match '1.2.1.10' as complete word(s).
These curated entries have 22 distinct sequences.
Running ublast with E ≤ 0.01
Found 2 relevant proteins in Pedobacter sp. GW460-11-11-14-LB5, or try another query
CA265_RS24860: alcohol dehydrogenase
is similar to: | PaperBLAST |
A0A0H3W5K4: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacterium saccharolyticum
I3VSF1: alcohol dehydrogenase (EC 1.1.1.1); L-lactate dehydrogenase (EC 1.1.1.27); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacterium saccharolyticum | 33% id,
47% cov |
A0A1D3TRQ6: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Anaerobium acetethylicum | 32% id,
47% cov |
B0K4A2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. | 33% id,
46% cov |
A0A0H3W5U9: alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Acetivibrio thermocellus
A3DCI2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Acetivibrio thermocellus | 31% id,
47% cov |
ADHE_ECO57 / P0A9Q8: Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli
ADHE_ECOLI / P0A9Q7: Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli
AdhE / b1241: fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE (EC 1.1.1.1; EC 1.2.1.10) from Escherichia coli
adhE / MB|P0A9Q7: aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.10 from Escherichia coli
adhE / P0A9Q7: fused acetaldehyde-CoA dehydrogenase and iron-dependent alcohol dehydrogenasealdehyde/alcohol dehydrogenase AdhE (EC 1.1.1.1; EC 1.2.1.10) from Escherichia coli
P0A9Q7: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Escherichia coli | 31% id,
46% cov |
adh2 / GB|AAA81906.1: aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 31% id,
47% cov |
ADH2_ENTH1 / Q24803: Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 31% id,
47% cov |
aad / GB|AAD04638.1: aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.10 from Clostridium acetobutylicum
adhE / P33744: alcohol/aldehyde dehydrogenase (EC 1.1.1.1; EC 1.2.1.10; EC 1.2.1.57) from Clostridium acetobutylicum | 27% id,
47% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 29% id,
43% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 29% id,
43% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 26% id,
44% 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 1 reading frames. Except for 1 reading frames, these were redundant with annotated proteins.
These remaining reading frames may be pseudogenes, omissions in the genome annotation,
or N-terminal extensions of annotated proteins.
6062136-6063305 (frame -1) on NZ_CP021237
is similar to: | PaperBLAST |
A0A0H3W5K4: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacterium saccharolyticum
I3VSF1: alcohol dehydrogenase (EC 1.1.1.1); L-lactate dehydrogenase (EC 1.1.1.27); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacterium saccharolyticum
Also see hits to annotated proteins above | 33% id,
48% cov |
B0K4A2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp.
Also see hits to annotated proteins above | 32% id,
47% cov |
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory