Curated BLAST for Genomes

 

Curated BLAST

Searching in Azospirillum brasilense Sp245 (azobra)

Found 40 curated entries in PaperBLAST's database that match '1.2.1.10' as complete word(s).

These curated entries have 21 distinct sequences.

Running ublast with E ≤ 0.01

Found 9 relevant proteins in Azospirillum brasilense Sp245, or try another query

AZOBR_RS32240: acetaldehyde dehydrogenase
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

75% id,
99% cov

A0A0H3W5U9: alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum
A3DCI2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum

63% id,
99% 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

58% id,
100% cov

More...

AZOBR_RS32475: aldehyde Dehydrogenase
is similar to:
PaperBLAST

EUTE_ECOLI / P77445: Acetaldehyde dehydrogenase (acetylating) EutE; Ethanolamine utilization protein EutE; EC 1.2.1.10 from Escherichia coli
YffX / b2455: acetaldehyde dehydrogenase (acetylating) EutE (EC 1.2.1.10) from Escherichia coli
eutE / P77445: acetaldehyde dehydrogenase (acetylating) EutE (EC 1.2.1.10) from Escherichia coli

33% id,
91% cov

EUTE_SALTY / P41793: Acetaldehyde dehydrogenase (acetylating) EutE; Ethanolamine utilization protein EutE; EC 1.2.1.10 from Salmonella typhimurium
eutE / P41793: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Salmonella typhimurium

32% id,
90% cov

ADHE_BILW3 / E5Y379: Acetaldehyde dehydrogenase (acetylating); CoA-acylating acetaldehyde dehydrogenase; EC 1.2.1.10 from Bilophila wadsworthia
adhE / E5Y379: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Bilophila wadsworthia

29% id,
92% cov

More...

AZOBR_RS29750: aldehyde dehydrogenase
is similar to:
PaperBLAST

B0K315: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp.

26% id,
97% cov

AZOBR_RS27605: 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

31% id,
46% cov

A0A0H3W5U9: alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum
A3DCI2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum

31% id,
41% 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

29% id,
40% cov

More...

AZOBR_RS28580: 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

29% id,
47% cov

ADH2_ENTHI / Q24803: Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica
adh2 / GB|AAA81906.1: aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica

28% id,
46% 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

30% id,
44% cov

More...

AZOBR_RS06065: 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

26% id,
44% cov

ADH2_ENTHI / Q24803: Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica
adh2 / GB|AAA81906.1: aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica

28% id,
39% 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

25% id,
41% cov

More...

AZOBR_RS26520: alcohol dehydrogenase
is similar to:
PaperBLAST

A0A0H3W5U9: alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum
A3DCI2: alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Hungateiclostridium thermocellum

25% id,
44% cov

AZOBR_RS23265: hypothetical protein
is similar to:
PaperBLAST

EUTE_SALTY / P41793: Acetaldehyde dehydrogenase (acetylating) EutE; Ethanolamine utilization protein EutE; EC 1.2.1.10 from Salmonella typhimurium
eutE / P41793: acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Salmonella typhimurium

25% id,
35% cov

AZOBR_RS22500: methylmalonate-semialdehyde dehydrogenase
is similar to:
PaperBLAST

ADH1 / A8JI07: alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii

22% id,
34% 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 6 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory