Sites on a Tree

 

Searching for up to 100 curated homologs for GFF840 FitnessBrowser__psRCH2:GFF840 (245 a.a.)

Found high-coverage hits (≥70%) to 17 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

1mxsA / P00885 Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (kdpg) aldolase from pseudomonas putida. (see paper)
    67% identity, 87% coverage of query (298 bits)

P00885 2-dehydro-3-deoxy-phosphogluconate aldolase; KDPG-aldolase; Phospho-2-dehydro-3-deoxygluconate aldolase; Phospho-2-keto-3-deoxygluconate aldolase; EC 4.1.2.14 from Pseudomonas putida (Arthrobacter siderocapsulatus)
    66% identity, 87% coverage of query (295 bits)

kdgA / P38448 2-dehydro-3-deoxy-D-gluconate-6-phosphate aldolase (EC 4.1.2.55) from Dickeya dadantii (strain 3937) (see 2 papers)
    52% identity, 82% coverage of query (216 bits)

Kga / b1850 KHG/KDPG aldolase (EC 4.1.2.55; EC 4.1.2.14; EC 4.1.3.42; EC 4.1.1.112) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
eda / P0A955 KHG/KDPG aldolase (EC 4.1.2.55; EC 4.1.3.42; EC 4.1.1.112) from Escherichia coli (strain K12) (see 2 papers)
ALKH_ECOLI / P0A955 KHG/KDPG aldolase; EC 4.1.3.16; EC 4.1.2.14 from Escherichia coli (strain K12) (see 5 papers)
P0A955 4-Hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16); (4S)-4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.42) from Escherichia coli (see 5 papers)
eda / RF|NP_416364 KHG/KDPG aldolase; EC 4.1.2.14; EC 4.1.3.16 from Escherichia coli K12 (see 4 papers)
    52% identity, 73% coverage of query (200 bits)

1euaA Schiff base intermediate in kdpg aldolase from escherichia coli
    52% identity, 73% coverage of query (200 bits)

ALKD_PSEA6 / Q15X88 2-dehydro-3-deoxy-phosphogluconate aldolase; 2-keto-3-deoxy-6-phospho-D-gluconate aldolase; KDPG aldolase; EC 4.1.2.14 from Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
    50% identity, 80% coverage of query (198 bits)

2c0aB / P0A955 Mechanism of the class i kdpg aldolase (see paper)
    52% identity, 73% coverage of query (198 bits)

1wauA Structure of kdpg aldolase e45n mutant
    52% identity, 73% coverage of query (198 bits)

6oviA / Q5ZYF2 Crystal structure of kdpg aldolase from legionella pneumophila with pyruvate captured at low ph as a covalent carbinolamine intermediate
    48% identity, 77% coverage of query (193 bits)

3vcrA / D2YW47 Crystal structure of a putative kdpg (2-keto-3-deoxy-6- phosphogluconate) aldolase from oleispira antarctica (see paper)
    47% identity, 82% coverage of query (184 bits)

Q0K1X1 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) from Cupriavidus necator (see paper)
    46% identity, 84% coverage of query (177 bits)

5xsfA / Q00384 Crystal structure of the 2-keto-3-deoxy-6-phosphogluconate aldolase of zymomonas mobilis zm4 with 3-phosphoglycerate
    50% identity, 74% coverage of query (176 bits)

Q00384 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) from Zymomonas mobilis subsp. mobilis (see paper)
    50% identity, 74% coverage of query (175 bits)

eda / CAE53635.1 2-dehydro-3-deoxyphosphogluconate aldolase from Nonomuraea gerenzanensis (see paper)
    48% identity, 76% coverage of query (171 bits)

D4GV57 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) from Haloferax volcanii (see paper)
    35% identity, 80% coverage of query (95.5 bits)

Build an alignment

Build an alignment for GFF840 and 15 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%)

CA265_RS19860 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) from Pedobacter sp. GW460-11-11-14-LB5
    29% identity, 87% coverage of query (70.1 bits)

A0A0B6VQ18 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) from Flavobacterium sp. UMI-01 (see paper)
    28% identity, 71% coverage of query (54.3 bits)

Or start over

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory