Sites on a Tree

 

Searching for up to 100 curated homologs for BPHYT_RS25815 BPHYT_RS25815 deoxyribose-phosphate aldolase (336 a.a.)

Found high-coverage hits (≥70%) to 16 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

DEOC_HUMAN / Q9Y315 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Homo sapiens (Human) (see paper)
Q9Y315 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Homo sapiens (see paper)
    59% identity, 93% coverage of query (378 bits)

Tlr / b4381 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Escherichia coli K-12 substr. MG1655 (see 16 papers)
deoC / P0A6L0 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Escherichia coli (strain K12) (see 14 papers)
DEOC_ECOLI / P0A6L0 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Escherichia coli (strain K12) (see 4 papers)
deoC / RF|NP_418798 phosphodeoxyriboaldolase from Escherichia coli K12 (see paper)
    38% identity, 71% coverage of query (140 bits)

5el1A Crystal structure of deoxyribose-phosphate aldolase from escherichia coli (k58e-y96w mutant) after acetaldehyde treatment
    38% identity, 71% coverage of query (140 bits)

5ekyA Crystal structure of deoxyribose-phosphate aldolase from escherichia coli (k58e-y96w mutant)
    38% identity, 71% coverage of query (140 bits)

1jcjA / P0A6L0 Observation of covalent intermediates in an enzyme mechanism at atomic resolution (see paper)
    37% identity, 71% coverage of query (137 bits)

6z9iB Escherichia coli d-2-deoxyribose-5-phosphate aldolase - n21k mutant complex with reaction products
    37% identity, 71% coverage of query (137 bits)

Q7WT44 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Klebsiella pneumoniae (see paper)
    37% identity, 73% coverage of query (136 bits)

DEOC_SALTY / Q8ZJV8 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
    37% identity, 71% coverage of query (135 bits)

7p76A Re-engineered 2-deoxy-d-ribose-5-phosphate aldolase catalysing asymmetric michael addition reactions, schiff base complex with cinnamaldehyde
    35% identity, 76% coverage of query (129 bits)

A0A125YLW2 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Toxoplasma gondii (see paper)
    36% identity, 73% coverage of query (103 bits)

8forA Crystal structure of kemp eliminase ke70-core with bound transition state analogue
    33% identity, 71% coverage of query (102 bits)

3q2dA Optimization of the in silico designed kemp eliminase ke70 by computational design and directed evolution
    32% identity, 71% coverage of query (93.6 bits)

DEOC_PSEU2 / Q4ZMV1 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Pseudomonas syringae pv. syringae (strain B728a) (see paper)
    34% identity, 71% coverage of query (80.1 bits)

Build an alignment

Build an alignment for BPHYT_RS25815 and 13 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%)

D5AHU8 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Streptococcus suis (see paper)
    29% identity, 71% coverage of query (73.2 bits)

DEOC_ACIB4 / B5IEU6 Deoxyribose-phosphate aldolase; DERA; 2-deoxy-D-ribose 5-phosphate aldolase; Phosphodeoxyriboaldolase; Deoxyriboaldolase; EC 4.1.2.4 from Aciduliprofundum boonei (strain DSM 19572 / T469)
    30% identity, 72% coverage of query (69.7 bits)

C7E719 deoxyribose-phosphate aldolase (EC 4.1.2.4) from Paenibacillus sp. (see paper)
    29% identity, 73% coverage of query (66.6 bits)

Or start over

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory