Sites on a Tree

 

Searching for up to 100 curated homologs for Pf6N2E2_1939 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1939 (811 a.a.)

Found high-coverage hits (≥70%) to 39 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

A0A2Z5U248 quinate/shikimate dehydrogenase (quinone) (EC 1.1.5.8) from Gluconobacter oxydans (see paper)
    37% identity, 96% coverage of query (513 bits)

quiA / Q59086 quinate/shikimate dehydrogenase (quinone) (EC 1.1.5.8) from Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) (see 2 papers)
    37% identity, 97% coverage of query (511 bits)

A0A2Z5U421 quinate/shikimate dehydrogenase (quinone) (EC 1.1.5.8) from Gluconobacter oxydans (see paper)
    37% identity, 96% coverage of query (511 bits)

D4P700 glucose 1-dehydrogenase (PQQ, quinone) (EC 1.1.5.2) from Pantoea ananatis (see paper)
    40% identity, 97% coverage of query (504 bits)

A0A0J6JEN3 glucose 1-dehydrogenase (PQQ, quinone) (EC 1.1.5.2) from Pseudomonas taetrolens (see paper)
    38% identity, 98% coverage of query (501 bits)

M9MJR9 glycerol dehydrogenase (acceptor) (EC 1.1.99.22) from Gluconobacter thailandicus (see paper)
    42% identity, 81% coverage of query (496 bits)

sldA / Q8KIL1 D-sorbitol dehydrogenase large subunit (EC 1.1.99.21) from Gluconobacter thailandicus (see 4 papers)
    42% identity, 81% coverage of query (493 bits)

P05465 soluble quinoprotein glucose dehydrogenase (EC 1.1.99.35) from Acinetobacter calcoaceticus (see 3 papers)
    37% identity, 98% coverage of query (491 bits)

Gcd / b0124 quinoprotein glucose dehydrogenase (EC 1.1.5.2) from Escherichia coli K-12 substr. MG1655 (see 21 papers)
gcd / P15877 quinoprotein glucose dehydrogenase (EC 1.1.5.2) from Escherichia coli (strain K12) (see 22 papers)
DHG_ECOLI / P15877 Quinoprotein glucose dehydrogenase; Glucose dehydrogenase [pyrroloquinoline-quinone]; EC 1.1.5.2 from Escherichia coli (strain K12) (see 3 papers)
gcd / GB|BAB96699.1 quinoprotein glucose dehydrogenase; EC 1.1.5.2 from Escherichia coli K12 (see 9 papers)
gcd / ECOCYC|GLUCDEHYDROG-MONOMER glucose dehydrogenase from Escherichia coli K12 (see paper)
    38% identity, 98% coverage of query (488 bits)

B9TTF1 quinate/shikimate dehydrogenase (quinone) (EC 1.1.5.8) from Gluconobacter oxydans (see paper)
    36% identity, 96% coverage of query (482 bits)

Q70JN9 gluconate 5-dehydrogenase (EC 1.1.1.69); D-sorbitol dehydrogenase (acceptor) (subunit 1/2) (EC 1.1.99.21) from Gluconobacter oxydans (see 2 papers)
    41% identity, 81% coverage of query (472 bits)

sldA / BAC02909.1 D-Sorbitol dehydrogenase from Gluconobacter oxydans (see paper)
    40% identity, 81% coverage of query (451 bits)

Build an alignment

Build an alignment for Pf6N2E2_1939 and 12 homologs with ≥ 30% identity

Select sequences

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

Or download the sequences

Change minimum %identity:

Additional hits (identity < 30%)

1kv9A / Q8GR64 Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
    26% identity, 74% coverage of query (151 bits)

QHED_PSEPU / Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 8 papers)
Q8GR64 alcohol dehydrogenase (azurin) (EC 1.1.9.1); aldehyde dehydrogenase (quinone) (EC 1.2.5.2) from Pseudomonas putida (see 2 papers)
    26% identity, 74% coverage of query (151 bits)

QGDA_PSEPU / Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 4 papers)
Q4W6G0 aldehyde dehydrogenase (quinone) (EC 1.2.5.2) from Pseudomonas putida (see paper)
    27% identity, 75% coverage of query (147 bits)

1yiqA / Q4W6G0 Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase adhiig from pseudomonas putida hk5. Compariison to the other quinohemoprotein alcohol dehydrogenase adhiib found in the same microorganism. (see paper)
    27% identity, 75% coverage of query (146 bits)

Q9KH03 aldehyde dehydrogenase (quinone) (EC 1.2.5.2) from Cupriavidus necator (see paper)
    26% identity, 74% coverage of query (144 bits)

1kb0A / Q46444 Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
    27% identity, 75% coverage of query (143 bits)

qheDH / Q46444 alcohol dehydrogenase (azurin) (EC 1.1.9.1) from Comamonas testosteroni (see 3 papers)
QHED_COMTE / Q46444 Quinohemoprotein alcohol dehydrogenase; QH-ADH; Alcohol dehydrogenase (azurin); PQQ-containing alcohol dehydrogenase; PQQ-dependent ADH; Quinohaemoprotein ethanol dehydrogenase type I; QH-EDHI; EC 1.1.9.1 from Comamonas testosteroni (Pseudomonas testosteroni) (see 2 papers)
Q46444 alcohol dehydrogenase (azurin) (EC 1.1.9.1) from Comamonas testosteroni (see paper)
    27% identity, 75% coverage of query (140 bits)

bdh / Q9AF95 1-butanol dehydrogenase (cytochrome c) (EC 1.1.2.9) from Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / NBRC 103042 / IAM 12574 / Bu B1211) (see 3 papers)
BDH_THABB / Q9AF95 1-butanol dehydrogenase (cytochrome c); BDH; NAD-independent 1-butanol dehydrogenase; PQQ-containing alcohol dehydrogenase; Quinohemoprotein; EC 1.1.2.9 from Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / NBRC 103042 / IAM 12574 / Bu B1211) (Pseudomonas butanovora) (see 3 papers)
Q9AF95 1-butanol dehydrogenase (cytochrome c) (EC 1.1.2.9) from Thauera butanivorans (see paper)
    26% identity, 74% coverage of query (127 bits)

6zcvA / Q88JH0 Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
    24% identity, 73% coverage of query (122 bits)

B1N7J5 alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8) from Pseudomonas putida (see paper)
pedH / GI|150014706 quinoprotein decanol dehydrogenase; EC 1.1.-.- from Pseudomonas putida (see paper)
    24% identity, 73% coverage of query (122 bits)

C5AXV8 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Methylorubrum extorquens (see paper)
    24% identity, 75% coverage of query (117 bits)

6fkwA Europium-containing methanol dehydrogenase
    25% identity, 74% coverage of query (114 bits)

4maeA / I0JWN7 Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
    25% identity, 74% coverage of query (113 bits)

7o6zA / A0A7R8L7W4 Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
    23% identity, 74% coverage of query (109 bits)

7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase
    23% identity, 74% coverage of query (109 bits)

Q88JH5 alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8) from Pseudomonas putida (see 2 papers)
    23% identity, 75% coverage of query (108 bits)

pedE / B1N7J0 quinoprotein alcohol dehydrogenase from Pseudomonas putida (see 5 papers)
B1N7J0 alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8) from Pseudomonas putida (see paper)
pedE / GI|150014701 quinoprotein phenylethanol dehydrogenase; EC 1.1.-.- from Pseudomonas putida (see paper)
    23% identity, 75% coverage of query (108 bits)

4mh1B Crystal structure and functional studies of quinoprotein l-sorbose dehydrogenase from ketogulonicigenium vulgare y25 (see paper)
    24% identity, 76% coverage of query (107 bits)

exaA / Q9Z4J7 alcohol dehydrogenase (cytochrome c550) monomer (EC 1.1.2.8) from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
QEDH_PSEAE / Q9Z4J7 Quinoprotein ethanol dehydrogenase; QEDH; Quinoprotein alcohol dehydrogenase (cytochrome c); Quinoprotein alcohol dehydrogenase (cytochrome c550); EC 1.1.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 6 papers)
Q9Z4J7 alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8) from Pseudomonas aeruginosa (see paper)
    23% identity, 75% coverage of query (105 bits)

1flgA / Q9Z4J7 Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
    23% identity, 75% coverage of query (105 bits)

QEDH_PSEPU / A8R3S4 Quinoprotein ethanol dehydrogenase; QEDH; Quinoprotein alcohol dehydrogenase (cytochrome c); Quinoprotein alcohol dehydrogenase (cytochrome c550); Quinoprotein alcohol dehydrogenase ADH I; ADH I; EC 1.1.2.8 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
    22% identity, 75% coverage of query (98.6 bits)

N0B5Z3 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Hyphomicrobium denitrificans (see paper)
    23% identity, 75% coverage of query (98.6 bits)

A0A0A8K0T2 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Methyloceanibacter caenitepidi (see paper)
    22% identity, 80% coverage of query (97.4 bits)

boh / Q9AGW3 1-butanol dehydrogenase (EC 1.1.5.11) from Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / NBRC 103042 / IAM 12574 / Bu B1211) (see 2 papers)
BOH_THABB / Q9AGW3 1-butanol dehydrogenase (quinone); PQQ-containing alcohol dehydrogenase; Quinoprotein alcohol dehydrogenase; EC 1.1.5.11 from Thauera butanivorans (strain ATCC 43655 / DSM 2080 / JCM 20651 / NBRC 103042 / IAM 12574 / Bu B1211) (Pseudomonas butanovora) (see 2 papers)
Q9AGW3 aldehyde dehydrogenase (quinone) (EC 1.2.5.2) from Thauera butanivorans (see paper)
    24% identity, 75% coverage of query (93.6 bits)

A0A0A8JZD4 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Methyloceanibacter caenitepidi (see paper)
    22% identity, 74% coverage of query (93.2 bits)

A0A0A8K4A4 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Methyloceanibacter caenitepidi (see paper)
    22% identity, 74% coverage of query (90.5 bits)

A0A1E3VNN9 lanthanide-dependent methanol dehydrogenase (EC 1.1.2.10) from Methyloceanibacter stevinii (see paper)
    23% identity, 74% coverage of query (87.4 bits)

Or start over

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory