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Searching for up to 100 curated homologs for 16554 b2455 predicted aldehyde dehydrogenase, ethanolamine utilization protein (NCBI) (467 a.a.)

Found high-coverage hits (≥70%) to 67 curated proteins.

Removed hits that are identical to the query, leaving 66

You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.

Hits with ≥ 30% identity

eutE / P41793 acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
EUTE_SALTY / P41793 Acetaldehyde dehydrogenase (acetylating) EutE; Ethanolamine utilization protein EutE; EC 1.2.1.10 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 10 papers)
    94% identity, 100% coverage of query (870 bits)

adhE / E5Y379 acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Bilophila wadsworthia (strain 3_1_6) (see paper)
ADHE_BILW3 / E5Y379 Acetaldehyde dehydrogenase (acetylating); CoA-acylating acetaldehyde dehydrogenase; EC 1.2.1.10 from Bilophila wadsworthia (strain 3_1_6) (see paper)
    61% identity, 100% coverage of query (541 bits)

B0K315 acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. (see paper)
    52% identity, 94% coverage of query (450 bits)

pduP / Q9XDN1 CoA-dependent propanal dehydrogenase (EC 1.2.1.87) from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 8 papers)
PDUP_SALTY / Q9XDN1 Propanal dehydrogenase (CoA-propanoylating); Coenzyme-A-acylating propionaldehyde dehydrogenase; Propanediol utilization protein PduP; EC 1.2.1.87 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 9 papers)
    46% identity, 100% coverage of query (394 bits)

PDUP_CITFR / B1VB75 Propanal dehydrogenase (CoA-propanoylating); Coenzyme-A-acylating propionaldehyde dehydrogenase; Propanediol utilization protein PduP; EC 1.2.1.87 from Citrobacter freundii (see 2 papers)
    45% identity, 100% coverage of query (388 bits)

A9KN57 aldehyde dehydrogenase (NAD+) (EC 1.2.1.3) from Lachnoclostridium phytofermentans (see paper)
    43% identity, 100% coverage of query (380 bits)

4c3sA / A9KN57 Structure of a propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment (see paper)
    44% identity, 94% coverage of query (370 bits)

5jfmB / Q21A49 Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa (see paper)
    45% identity, 96% coverage of query (370 bits)

5jflA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound NAD+
    46% identity, 93% coverage of query (370 bits)

5jfmA Crystal structure of rhodopseudomonas palustris propionaldehyde dehydrogenase with bound propionyl-coa
    46% identity, 93% coverage of query (369 bits)

6gvsA Engineered glycolyl-coa reductase comprising 8 mutations with bound NADP+
    45% identity, 93% coverage of query (360 bits)

5dbvA Structure of a c269a mutant of propionaldehyde dehydrogenase from the clostridium phytofermentans fucose utilisation bacterial microcompartment
    43% identity, 94% coverage of query (355 bits)

A0A1D3TRQ6 acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Anaerobium acetethylicum (see paper)
    33% identity, 88% coverage of query (186 bits)

Q0PH30 alcohol dehydrogenase (EC 1.1.1.1) from Thermoanaerobacter ethanolicus (see paper)
    31% identity, 92% coverage of query (186 bits)

B0K4A2 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. X514 (see 2 papers)
    31% identity, 92% coverage of query (185 bits)

B0KBJ9 alcohol dehydrogenase (EC 1.1.1.1) from Thermoanaerobacter pseudethanolicus (see paper)
    31% identity, 92% coverage of query (184 bits)

A0A0H3W5K4 acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacterium saccharolyticum (see paper)
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 (see paper)
    30% identity, 93% coverage of query (179 bits)

A0A0H3W5V0 alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71) from Thermoanaerobacterium saccharolyticum (see paper)
    30% identity, 93% coverage of query (179 bits)

adhE2 / Q9ANR5 aldehyde dehydrogenase/alcohol dehydrogenase (EC 1.2.1.57) from Clostridium acetobutylicum (see 4 papers)
    32% identity, 79% coverage of query (174 bits)

5j7iB Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp (see paper)
    32% identity, 84% coverage of query (172 bits)

5j7iC Crystal structure of a geobacillus thermoglucosidasius acetylating aldehyde dehydrogenase in complex with adp
    32% identity, 84% coverage of query (172 bits)

adhE / P33744 alcohol/aldehyde dehydrogenase (EC 1.1.1.1; EC 1.2.1.10; EC 1.2.1.57) from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see 4 papers)
ADHE_CLOAB / P33744 Aldehyde-alcohol dehydrogenase; AAD; EC 1.1.1.1; EC 1.2.1.3 from Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) (see paper)
aad / GB|AAD04638.1 aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.10 from Clostridium acetobutylicum ATCC 824 (see paper)
aad / AAD04638.1 aldehyde-alcohol dehydrogenase from Clostridium acetobutylicum (see 2 papers)
    33% identity, 81% coverage of query (171 bits)

8cejA / P38947 Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa (see paper)
    31% identity, 86% coverage of query (163 bits)

sucD / P38947 succinate semialdehyde dehydrogenase subunit (EC 1.2.1.76) from Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) (see 3 papers)
sucD / GB|AAA92347.1 succinate-semialdehyde dehydrogenase [NAD(P)+]; EC 1.2.1.16 from Clostridium kluyveri DSM 555 (see paper)
    31% identity, 86% coverage of query (163 bits)

8cekA Succinyl-coa reductase from clostridium kluyveri (sucd) with NADPH
    31% identity, 86% coverage of query (163 bits)

8cejC Succinyl-coa reductase from clostridium kluyveri (sucd) with mesaconyl-c1-coa
    31% identity, 86% coverage of query (163 bits)

ADHE_STRPN / A0A0H2URT2 Aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.3 from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) (see paper)
    30% identity, 84% coverage of query (162 bits)

ADHE_STRP2 / A0A0H2ZM56 Aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.3 from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see paper)
    30% identity, 84% coverage of query (162 bits)

A0A0H3W5U9 alcohol dehydrogenase [NAD(P)+] (EC 1.1.1.71); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Acetivibrio thermocellus (see 3 papers)
A3DCI2 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Acetivibrio thermocellus (see 4 papers)
    31% identity, 76% coverage of query (160 bits)

ADH1 / A8JI07 alcohol dehydrogenase / acetaldehyde dehydrogenase (EC 1.2.1.10; EC 1.1.1.1) from Chlamydomonas reinhardtii (see 2 papers)
    31% identity, 79% coverage of query (159 bits)

Q1RS84 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Chlamydomonas reinhardtii (see paper)
    31% identity, 79% coverage of query (153 bits)

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Build an alignment for 16554 and 31 homologs with ≥ 30% identity

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Additional hits (identity < 30%)

ADH2_ENTH1 / Q24803 Aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM) (see 2 papers)
    29% identity, 91% coverage of query (145 bits)

adh2 / GB|AAA81906.1 aldehyde-alcohol dehydrogenase 2; EC 1.1.1.1; EC 1.2.1.10 from Entamoeba histolytica (see paper)
AAA81906.1 alcohol dehydrogenase 2 from Entamoeba histolytica (see paper)
    30% identity, 82% coverage of query (145 bits)

SQWD_ACHSX / A0A3A6N9T6 Sulfoacetaldehyde dehydrogenase; CoA-acylating sulfoacetaldehyde dehydrogenase; NAD(+)-dependent acylating sulfoacetaldehyde dehydrogenase; EC 1.2.1.- from Acholeplasma sp. (see paper)
    29% identity, 84% coverage of query (139 bits)

Q70YJ9 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Polytomella sp. Pringsheim 198.80 (see paper)
    31% identity, 76% coverage of query (138 bits)

SauS / Q0K845 sulfoacetaldehyde dehydrogenase (acylating) subunit (EC 1.2.1.81) from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (see paper)
SAUS_CUPNH / Q0K845 Sulfoacetaldehyde dehydrogenase (acylating); EC 1.2.1.81 from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) (see paper)
Q0K845 sulfoacetaldehyde dehydrogenase (acylating) (EC 1.2.1.81) from Cupriavidus necator (see paper)
    31% identity, 76% coverage of query (134 bits)

Noca_4822 / A1SC71 2-hydroxyethyl-CoM 2-dehydrogenase from Nocardioides sp. (strain ATCC BAA-499 / JS614) (see 2 papers)
    29% identity, 83% coverage of query (116 bits)

ASC1_DIDFA / A0A5C1REZ4 Aldehyde dehydrogenase; Ascochitine biosynthesis cluster protein 1; EC 1.2.1.3 from Didymella fabae (Leaf and pod spot disease fungus) (Ascochyta fabae) (see paper)
    25% identity, 82% coverage of query (77.8 bits)

AldH / b1300 γ-glutamyl-γ-aminobutyraldehyde dehydrogenase (EC 1.2.1.19; EC 1.2.1.24; EC 1.2.1.99) from Escherichia coli K-12 substr. MG1655 (see 6 papers)
puuC / P23883 γ-glutamyl-γ-aminobutyraldehyde dehydrogenase (EC 1.2.1.19; EC 1.2.1.24; EC 1.2.1.99) from Escherichia coli (strain K12) (see 6 papers)
PUUC_ECOLI / P23883 NADP/NAD-dependent aldehyde dehydrogenase PuuC; ALDH; 3-hydroxypropionaldehyde dehydrogenase; Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase; EC 1.2.1.5 from Escherichia coli (strain K12) (see 2 papers)
P23883 4-(gamma-glutamylamino)butanal dehydrogenase (EC 1.2.1.99) from Escherichia coli (see 3 papers)
puuC / BAD88708.1 gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase from Escherichia coli K-12 (see paper)
    26% identity, 82% coverage of query (76.3 bits)

Sama_3009 Succinylglutamic semialdehyde dehydrogenase (EC 1.2.1.71) from Shewanella amazonensis SB2B
    27% identity, 70% coverage of query (69.3 bits)

AL3B3_MOUSE / J3QMK6 Aldehyde dehydrogenase family 3 member B3; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
J3QMK6 long-chain-aldehyde dehydrogenase (EC 1.2.1.48) from Mus musculus (see paper)
    25% identity, 73% coverage of query (62.0 bits)

AL3B2_MOUSE / E9Q3E1 Aldehyde dehydrogenase family 3 member B2; Aldehyde dehydrogenase 8; EC 1.2.1.3 from Mus musculus (Mouse) (see paper)
E9Q3E1 long-chain-aldehyde dehydrogenase (EC 1.2.1.48) from Mus musculus (see paper)
    25% identity, 73% coverage of query (59.7 bits)

2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
    24% identity, 72% coverage of query (58.9 bits)

2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
    24% identity, 72% coverage of query (58.9 bits)

2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
    24% identity, 72% coverage of query (58.9 bits)

2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
    24% identity, 72% coverage of query (58.9 bits)

2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
    24% identity, 72% coverage of query (58.9 bits)

2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP
    24% identity, 72% coverage of query (58.9 bits)

2bhqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound product glutamate.
    24% identity, 72% coverage of query (58.9 bits)

2bhpA / Q5SI02 Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD. (see paper)
    24% identity, 72% coverage of query (58.9 bits)

2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
    24% identity, 72% coverage of query (58.9 bits)

4iymC / Q92RW4 Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
    22% identity, 71% coverage of query (55.1 bits)

AL3B1_HUMAN / P43353 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Homo sapiens (Human) (see 2 papers)
P43353 aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) from Homo sapiens (see paper)
    23% identity, 73% coverage of query (54.7 bits)

3jz4A / P25526 Crystal structure of e. Coli NADP dependent enzyme (see paper)
    25% identity, 74% coverage of query (54.3 bits)

GabD / b2661 succinate-semialdehyde dehydrogenase (NADP+) GabD (EC 1.2.1.79) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
gabD / P25526 succinate-semialdehyde dehydrogenase (NADP+) GabD (EC 1.2.1.79; EC 1.2.1.20) from Escherichia coli (strain K12) (see 22 papers)
GABD_ECOLI / P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see 4 papers)
P25526 succinate-semialdehyde dehydrogenase (NADP+) (EC 1.2.1.79) from Escherichia coli K-12 (see paper)
GB|AAC75708.1 succinate-semialdehyde dehydrogenase [NAD(P)+]; EC 1.2.1.16 from Escherichia coli K12 (see 5 papers)
    26% identity, 74% coverage of query (54.3 bits)

1ad3A / P11883 Class 3 aldehyde dehydrogenase complex with nicotinamide-adenine- dinucleotide (see paper)
    23% identity, 73% coverage of query (53.5 bits)

4zz7A / G5CZI2 Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
    23% identity, 76% coverage of query (53.1 bits)

AL3A1_HUMAN / P30838 Aldehyde dehydrogenase, dimeric NADP-preferring; ALDHIII; Aldehyde dehydrogenase 3; Aldehyde dehydrogenase family 3 member A1; EC 1.2.1.5 from Homo sapiens (Human) (see 2 papers)
P30838 aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) from Homo sapiens (see 8 papers)
    23% identity, 73% coverage of query (53.1 bits)

8bb8A Crystal structure of human aldehyde dehydrogenase aldh3a1 in complex with octanal
    23% identity, 73% coverage of query (52.8 bits)

4l1oB / P30838 Crystal structure of human aldh3a1 with inhibitor 1-{[4-(1,3- benzodioxol-5-ylmethyl)piperazin-1-yl]methyl}-1h-indole-2,3-dione
    23% identity, 73% coverage of query (51.6 bits)

3szbA Crystal structure of human aldh3a1 modified with the beta-elimination product of aldi-1; 1-phenyl- 2-propen-1-one
    23% identity, 73% coverage of query (51.2 bits)

4l2oA Crystal structure of human aldh3a1 with its selective inhibitor 1-(4- fluorophenyl)sulfonyl-2-methylbenzimidazole
    23% identity, 73% coverage of query (51.2 bits)

4h80A Crystal structure of human aldh3a1 with its isozyme selective inhibitor - n-[4-(4-methylsulfonyl-2-nitroanilino)phenyl]acetamide
    23% identity, 73% coverage of query (51.2 bits)

ALDH3A2 / P51648 fatty aldehyde dehydrogenase (EC 1.2.1.3; EC 1.2.1.94; EC 1.2.1.39) from Homo sapiens (see 10 papers)
AL3A2_HUMAN / P51648 Aldehyde dehydrogenase family 3 member A2; Aldehyde dehydrogenase 10; Fatty aldehyde dehydrogenase; Microsomal aldehyde dehydrogenase; EC 1.2.1.3; EC 1.2.1.94 from Homo sapiens (Human) (see 11 papers)
P51648 long-chain-aldehyde dehydrogenase (EC 1.2.1.48) from Homo sapiens (see paper)
    23% identity, 74% coverage of query (48.1 bits)

AL3B1_MOUSE / Q80VQ0 Aldehyde dehydrogenase family 3 member B1; Aldehyde dehydrogenase 7; EC 1.2.1.28; EC 1.2.1.5; EC 1.2.1.7 from Mus musculus (Mouse) (see 2 papers)
Q80VQ0 aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) from Mus musculus (see paper)
    22% identity, 73% coverage of query (48.1 bits)

6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
    23% identity, 74% coverage of query (44.7 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory