Curated BLAST
Searching in Pseudomonas fluorescens GW456-L13 (pseudo13_GW456_L13)
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 15 relevant proteins in Pseudomonas fluorescens GW456-L13, or try another query
PfGW456L13_2505: Acetaldehyde dehydrogenase, acetylating, (EC 1.2.1.10) in gene cluster for degradation of phenols, cresols, catechol is similar to: | PaperBLAST |
ACDH4_PARXL / Q79AF6: Acetaldehyde dehydrogenase 4; Acetaldehyde dehydrogenase [acetylating] 4; Propanal dehydrogenase (CoA-propanoylating); EC 1.2.1.10; EC 1.2.1.87 from Paraburkholderia xenovorans Q79AF6: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10); propanal dehydrogenase (CoA-propanoylating) (EC 1.2.1.87) from Paraburkholderia xenovorans | 75% id, 98% cov |
ACDH_MYCTU / P9WQH3: Propanal dehydrogenase (CoA-propanoylating); Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.87; EC 1.2.1.10 from Mycobacterium tuberculosis | 56% id, 98% cov |
ACDH_ECOLI / P77580: Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Escherichia coli MhpF / b0351: acetaldehyde dehydrogenase (acetylating) MhpF (EC 1.2.1.10) from Escherichia coli mhpF / GB|AAZ87107.1: acetaldehyde dehydrogenase; EC 1.2.1.10 from Escherichia coli mhpF / P77580: acetaldehyde dehydrogenase (acetylating) MhpF (EC 1.2.1.10) from Escherichia coli | 56% id, 97% cov |
ACDH_PSEUF / Q52060: Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. dmpF / Q52060: acetaldehyde dehydrogenase (acylating) (EC 1.2.1.10) from Pseudomonas sp. Q52060: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Pseudomonas sp. | 55% id, 99% cov |
ACDH_PSESP / Q9KWS1: Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; EC 1.2.1.10 from Pseudomonas sp. | 56% id, 96% cov |
ACDH_THET8 / Q53WH9: Acetaldehyde dehydrogenase; Acetaldehyde dehydrogenase [acetylating]; Propanal dehydrogenase (CoA-propanoylating); Propanaldehyde dehydrogenase; EC 1.2.1.10; EC 1.2.1.87 from Thermus thermophilus Q53WH9: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10); propanal dehydrogenase (CoA-propanoylating) (EC 1.2.1.87) from Thermus thermophilus | 55% id, 96% cov |
todI / Q51949: acylating aldehyde dehydrogenase (EC 1.2.1.10) from Pseudomonas putida | 54% id, 98% cov |
More... |
PfGW456L13_1214: Alcohol dehydrogenase (EC 1.1.1.1) 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 | 37% id, 47% cov |
B0K4A2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. | 37% id, 46% cov |
adh2 / GB|AAA81906.1: aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 35% id, 47% cov |
ADH2_ENTH1 / Q24803: Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 35% id, 47% cov |
A0A1D3TRQ6: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Anaerobium acetethylicum | 34% id, 47% 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 | 34% 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 | 32% 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 | 32% id, 43% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 32% id, 43% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 32% id, 43% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 29% id, 45% cov |
More... |
PfGW456L13_3512: Alcohol dehydrogenase (EC 1.1.1.1); Acetaldehyde dehydrogenase (EC 1.2.1.10) 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 | 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 |
B0K4A2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. | 31% id, 46% cov |
A0A1D3TRQ6: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Anaerobium acetethylicum | 29% 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 | 29% id, 47% 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 | 30% id, 44% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 28% id, 43% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 28% id, 43% 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 | 25% id, 47% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 27% id, 43% cov |
More... |
PfGW456L13_1083: Betaine aldehyde dehydrogenase (EC 1.2.1.8) is similar to: | PaperBLAST |
B0K315: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. | 29% id, 50% 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 | 23% id, 47% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 22% id, 42% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 22% id, 35% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 23% id, 31% cov |
More... |
PfGW456L13_2712: Alcohol dehydrogenase (EC 1.1.1.1) is similar to: | PaperBLAST |
A0A1D3TRQ6: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Anaerobium acetethylicum | 29% id, 47% cov |
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 | 29% id, 47% cov |
B0K4A2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. | 29% 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 | 29% id, 45% cov |
adh2 / GB|AAA81906.1: aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 29% id, 45% cov |
ADH2_ENTH1 / Q24803: Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica | 29% id, 45% 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 | 28% id, 46% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 26% id, 45% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 28% id, 40% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 28% id, 40% 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 | 24% id, 46% cov |
More... |
PfGW456L13_495: Succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16) is similar to: | PaperBLAST |
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 | 21% id, 45% cov |
PfGW456L13_3737: Aldehyde dehydrogenase (EC 1.2.1.3) is similar to: | PaperBLAST |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 25% id, 37% 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 | 24% id, 35% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 27% id, 29% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 27% id, 29% cov |
More... |
PfGW456L13_2: Methylmalonate-semialdehyde dehydrogenase (EC 1.2.1.27) is similar to: | PaperBLAST |
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 | 22% id, 35% cov |
ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii | 23% id, 32% cov |
Q1RS84: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii | 23% id, 32% cov |
Q70YJ9: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. | 21% id, 33% 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 11 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.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory