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Searching for up to 100 curated homologs for WP_013836016.1 NCBI__GCF_000214825.1:WP_013836016.1 (388 a.a.)

Found high-coverage hits (≥70%) to 41 curated proteins.

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

hpfD / A0A374P995 3-hydroxypropane-1-sulfonate dehydrogenase from Hungatella hathewayi (see paper)
    31% identity, 93% coverage of query (144 bits)

Build an alignment

Build an alignment for WP_013836016.1 and 1 homologs with ≥ 30% identity

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Add sequences from UniProt, PDB, RefSeq, or MicrobesOnline (separate identifiers with commas or spaces):

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Change minimum %identity:

Additional hits (identity < 30%)

I3E949 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see 2 papers)
    29% identity, 92% coverage of query (133 bits)

I3E2P9 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see 4 papers)
    29% identity, 92% coverage of query (132 bits)

I3DVX6 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see paper)
    28% identity, 99% coverage of query (126 bits)

ADH4 / P10127 alcohol dehydrogenase IV (EC 1.1.1.1) from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (see 11 papers)
ADH4_YEAST / P10127 Alcohol dehydrogenase 4; Alcohol dehydrogenase IV; ADHIV; EC 1.1.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 11 papers)
    31% identity, 73% coverage of query (125 bits)

A0A0C1Q6R1 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Levilactobacillus brevis (see paper)
    30% identity, 78% coverage of query (116 bits)

ADH1_GEOTN / A4IP64 Long-chain-alcohol dehydrogenase 1; Alcohol dehydrogenase 1; ADH1; Fatty alcohol oxidoreductase 1; Glycerol dehydrogenase; EC 1.1.1.192; EC 1.1.1.6 from Geobacillus thermodenitrificans (strain NG80-2) (see paper)
A4IP64 alcohol dehydrogenase (EC 1.1.1.1); long-chain-alcohol dehydrogenase (EC 1.1.1.192) from Geobacillus thermodenitrificans (see paper)
    35% identity, 72% coverage of query (115 bits)

BT3767 L-lactaldehyde reductase FucO (EC 1.1.1.77) from Bacteroides thetaiotaomicron VPI-5482
    31% identity, 79% coverage of query (114 bits)

B1HX72 methanol dehydrogenase (EC 1.1.1.244) from Lysinibacillus sphaericus (see paper)
    29% identity, 74% coverage of query (112 bits)

A0NIJ1 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Oenococcus oeni (see paper)
    29% identity, 80% coverage of query (111 bits)

I3DX19 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see paper)
    28% identity, 83% coverage of query (111 bits)

I3DTP7 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see paper)
    28% identity, 83% coverage of query (110 bits)

F8GNE5 methanol dehydrogenase (EC 1.1.1.244) from Cupriavidus necator (see paper)
    27% identity, 88% coverage of query (109 bits)

mdh / P31005 NAD-dependent methanol dehydrogenase monomer (EC 1.1.1.244) from Bacillus methanolicus (see paper)
MEDH_BACMT / P31005 NAD-dependent methanol dehydrogenase; MDH; MEDH; Type 3 alcohol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see 6 papers)
P31005 methanol dehydrogenase (EC 1.1.1.244) from Bacillus methanolicus (see paper)
mdh methanol dehydrogenase; EC 1.1.1.244 from Bacillus methanolicus (see paper)
    28% identity, 83% coverage of query (108 bits)

adhB / P0DJA2 alcohol dehydrogenase II monomer (EC 1.1.1.1) from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 8 papers)
ADH2_ZYMMO / P0DJA2 Alcohol dehydrogenase 2; Alcohol dehydrogenase II; ADH II; EC 1.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
P0DJA2 alcohol dehydrogenase (EC 1.1.1.1) from Zymomonas mobilis subsp. mobilis (see paper)
    27% identity, 90% coverage of query (108 bits)

3owoA / P0DJA2 Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 with and without NAD cofactor (see paper)
    27% identity, 90% coverage of query (107 bits)

3bfjA / Q7WRJ3 Crystal structure analysis of 1,3-propanediol oxidoreductase (see paper)
    30% identity, 80% coverage of query (107 bits)

Q7WRJ3 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Klebsiella pneumoniae (see 3 papers)
    30% identity, 80% coverage of query (107 bits)

A0A1D3TV27 alcohol dehydrogenase (EC 1.1.1.1) from Anaerobium acetethylicum (see paper)
    29% identity, 75% coverage of query (107 bits)

pduQ / Q9XDN0 propanol dehydrogenase (EC 1.1.1.1) from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
PDUQ_SALTY / Q9XDN0 1-propanol dehydrogenase PduQ; Propanediol utilization protein PduQ; EC 1.1.-.- from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 3 papers)
    30% identity, 75% coverage of query (107 bits)

Q59477 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Klebsiella pneumoniae (see 2 papers)
    30% identity, 80% coverage of query (107 bits)

3ox4A Structures of iron-dependent alcohol dehydrogenase 2 from zymomonas mobilis zm4 complexed with NAD cofactor
    27% identity, 90% coverage of query (107 bits)

A3RL85 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Klebsiella pneumoniae (see paper)
    30% identity, 80% coverage of query (103 bits)

DHAT_CITFR / P45513 1,3-propanediol dehydrogenase; 1,3-propanediol oxidoreductase; 3-hydroxypropionaldehyde reductase; EC 1.1.1.202 from Citrobacter freundii (see paper)
P45513 1,3-propanediol dehydrogenase (EC 1.1.1.202) from Citrobacter freundii (see paper)
dhaT / GB|AAB48848.1 1,3-propanediol dehydrogenase; EC 1.1.1.202 from Citrobacter freundii (see paper)
dhaT / AAB48848.1 1,3-propanediol dehydrogenase from Citrobacter freundii (see 4 papers)
    30% identity, 78% coverage of query (101 bits)

B0K4A2 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Thermoanaerobacter sp. X514 (see 2 papers)
    32% identity, 76% coverage of query (101 bits)

B0KBJ9 alcohol dehydrogenase (EC 1.1.1.1) from Thermoanaerobacter pseudethanolicus (see paper)
    32% identity, 76% coverage of query (100 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)
    28% identity, 73% coverage of query (100 bits)

HP15_3135 ethanol oxidation regulatory protein ercA from Marinobacter adhaerens HP15
    28% identity, 84% coverage of query (96.7 bits)

Q0PH30 alcohol dehydrogenase (EC 1.1.1.1) from Thermoanaerobacter ethanolicus (see paper)
    32% identity, 76% coverage of query (96.7 bits)

4HBDH_CUPNE / Q59104 4-hydroxybutyrate dehydrogenase; 4HbD; Gamma-hydroxybutyrate dehydrogenase; GHBDH; EC 1.1.1.61 from Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha) (see 2 papers)
Q59104 4-hydroxybutyrate dehydrogenase (EC 1.1.1.61) from Cupriavidus necator (see paper)
gbd / PRF|2104199G 4-hydroxybutyrate dehydrogenase; EC 1.1.1.61 from Cupriavidus necator (see paper)
    28% identity, 75% coverage of query (94.0 bits)

7bvpA / P0A9Q7 Adhe spirosome in extended conformation (see paper)
    30% identity, 83% coverage of query (92.4 bits)

6tqmA Escherichia coli adhe structure in its compact conformation
    30% identity, 83% coverage of query (92.4 bits)

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 K-12 substr. MG1655 (see 62 papers)
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 (strain K12) (see 64 papers)
ADHE_ECOLI / P0A9Q7 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli (strain K12) (see 13 papers)
ADHE_ECO57 / P0A9Q8 Bifunctional aldehyde-alcohol dehydrogenase AdhE; Alcohol dehydrogenase E; EC 1.2.1.10; EC 1.1.1.1 from Escherichia coli O157:H7 (see 2 papers)
P0A9Q7 alcohol dehydrogenase (EC 1.1.1.1); acetaldehyde dehydrogenase (acetylating) (EC 1.2.1.10) from Escherichia coli (see paper)
adhE / MB|P0A9Q7 aldehyde-alcohol dehydrogenase; EC 1.1.1.1; EC 1.2.1.10 from Escherichia coli K12 (see 12 papers)
    30% identity, 83% coverage of query (92.4 bits)

6scgA Structure of adhe form 1
    29% identity, 83% coverage of query (91.7 bits)

6jkpA Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense in complex with NAD+
    25% identity, 76% coverage of query (86.3 bits)

6jkoA / A0A0A7I0A5 Crystal structure of sulfoacetaldehyde reductase from bifidobacterium kashiwanohense (see paper)
    25% identity, 76% coverage of query (86.3 bits)

5yvrA Crystal structure of the h277a mutant of adh/d1, an archaeal halo- thermophilic red sea brine pool alcohol dehydrogenase
    25% identity, 85% coverage of query (79.0 bits)

5yvmA / A0A133UP32 Crystal structure of the archaeal halo-thermophilic red sea brine pool alcohol dehydrogenase adh/d1 bound to nzq (see paper)
    25% identity, 85% coverage of query (78.6 bits)

YqhD / b3011 NADPH-dependent aldehyde reductase YqhD (EC 1.1.1.2) from Escherichia coli K-12 substr. MG1655 (see 35 papers)
yqhD / Q46856 NADPH-dependent aldehyde reductase YqhD (EC 1.1.1.21; EC 1.1.1.2) from Escherichia coli (strain K12) (see 38 papers)
YQHD_ECOLI / Q46856 Alcohol dehydrogenase YqhD; EC 1.1.1.2 from Escherichia coli (strain K12) (see paper)
Q46856 alcohol dehydrogenase (NADP+) (EC 1.1.1.2) from Escherichia coli (see paper)
yqhD / RF|NP_417484 alcohol dehydrogenase yqhD; EC 1.1.1.- from Escherichia coli K12 (see 5 papers)
    28% identity, 77% coverage of query (55.8 bits)

1oj7B Structural genomics, unknown function crystal structure of e. Coli k- 12 yqhd
    28% identity, 77% coverage of query (55.8 bits)

1oj7A / Q46856 Structural genomics, unknown function crystal structure of e. Coli k- 12 yqhd (see paper)
    28% identity, 77% coverage of query (55.8 bits)

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by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory