Protein profile

PA2249

branched-chain alpha-keto acid dehydrogenase complex lipoamide acyltransferase

Genome: NC_002516.2

Gene: bkdB PA2249 Structure source: AlphaFold UniProt Q9I1M0
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Amino acids 428
Annotations 4
Features 28
PDB binders 5
Druggability 0.585

Overview

Basic information about this protein and its source genome.

Accession
PA2249
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
bkdB PA2249
Status
annotated
Amino acids
428
Structure source
AlphaFold
EC
2.3.1.168
GO
GO:0043754 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2-methylpropanoyl-CoA = N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein] + CoA. In addition to transferring the 2-methylpropanoyl group when acting on the oxoacid corresponding with valine, this activity also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups when acting on the oxo acids corresponding with leucine and isoleucine. GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules. GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
31.313
Human E-value
1.0499999999999999e-40
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Selected Druggability evidence

Selected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.

FPocket 0.585
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 3 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

3
  • GO:0043754 Catalysis of the reaction: N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2-methylpropanoyl-CoA = N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein] + CoA. In addition to transferring the 2-methylpropanoyl group when acting on the oxoacid corresponding with valine, this activity also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups when acting on the oxo acids corresponding with leucine and isoleucine.
  • GO:0006096 The chemical reactions and pathways resulting in the breakdown of a carbohydrate into pyruvate, with the concomitant production of a small amount of ATP and the reduction of NAD(P) to NAD(P)H. Glycolysis begins with the metabolism of a carbohydrate to generate products that can enter the pathway and ends with the production of pyruvate. Pyruvate may be converted to acetyl-coenzyme A, ethanol, lactate, or other small molecules.
  • GO:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).

Sequence Features

Domain/signature hits from InterPro and related databases.

28 records
Show feature table
Start End DB Term Name
88 146 MobiDBLite mobidb-lite consensus disorder prediction
192 427 SUPERFAMILY SSF52777 CoA-dependent acyltransferases
188 426 Gene3D G3DSA:3.30.559.10 -
188 426 InterPro IPR023213 Chloramphenicol acetyltransferase-like domain superfamily
120 134 MobiDBLite mobidb-lite consensus disorder prediction
188 427 FunFam G3DSA:3.30.559.10:FF:000007 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
5 76 Pfam PF00364 Biotin-requiring enzyme
5 76 InterPro IPR000089 Biotin/lipoyl attachment
3 96 SUPERFAMILY SSF51230 Single hybrid motif
3 96 InterPro IPR011053 Single hybrid motif
6 77 CDD cd06849 lipoyl_domain
133 181 FunFam G3DSA:4.10.320.10:FF:000002 Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
3 78 ProSiteProfiles PS50968 Biotinyl/lipoyl domain profile.
3 78 InterPro IPR000089 Biotin/lipoyl attachment
140 177 ProSiteProfiles PS51826 Peripheral subunit-binding (PSBD) domain profile.
140 177 InterPro IPR004167 Peripheral subunit-binding domain
139 173 Pfam PF02817 e3 binding domain
139 173 InterPro IPR004167 Peripheral subunit-binding domain
133 178 SUPERFAMILY SSF47005 Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex
133 178 InterPro IPR036625 E3-binding domain superfamily
28 57 ProSitePatterns PS00189 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site.
28 57 InterPro IPR003016 2-oxo acid dehydrogenase, lipoyl-binding site
3 86 Gene3D G3DSA:2.40.50.100 -
198 427 Pfam PF00198 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
198 427 InterPro IPR001078 2-oxoacid dehydrogenase acyltransferase, catalytic domain
128 179 Gene3D G3DSA:4.10.320.10 -
128 179 InterPro IPR036625 E3-binding domain superfamily
5 427 PANTHER PTHR43178 DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2249
AlphaFold — — full sequence — Viewing
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

Pockets (FPOCKET)

Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).

FPOCKET Sticks Spheres Surfaces Druggability Labels Zoom Positions
1 0.585
2 0.255

Ligand evidence

Ligands grouped by evidence source. PDB ligands keep the source crystal visible, and loaded crystals can be opened directly in the structure viewer.

47 records

Structural evidence inferred from similar proteins. The source crystal indicates where the ligand was observed; the UniProt column identifies the homologous protein carrying that ligand.

Show only:
Ligand Source crystal UniProt (homolog) MW · LogP · TPSA Lipinski PAINS SMILES
CAO
1EAC
P10802 783.5 Da LogP -1.39 TPSA 366.8 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
DTT
1EAC
P10802 154.3 Da LogP -0.43 TPSA 40.5 ✓ Ro5 ✓ Clean C([C@@H]([C@H](CS)O)O)S
LPM
1EAB
P10802 207.4 Da LogP 1.65 TPSA 43.1 ✓ Ro5 ✓ Clean C(CCC(=O)N)C[C@H](CCS)S
RDC
2Q8I
P10515 364.8 Da LogP 2.69 TPSA 96.4 ✓ Ro5 ✓ Clean C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(c…
RED
1Y8N
P10515 208.3 Da LogP 2.25 TPSA 37.3 ✓ Ro5 ✓ Clean C(CCC(=O)O)C[C@H](CCS)S

PDB and ChEMBL records on this protein are shown in full. ChEMBL records from similar proteins are capped at the top 100 per protein (by pchembl) and ZINC at the top 50 (Tanimoto ≥ 0.5). ADME columns are descriptor-based screening flags, not experimental toxicity results.