Protein profile

PA1631

acyl-CoA dehydrogenase

Genome: NC_002516.2

Gene: PA1631 Structure source: AlphaFold UniProt Q9I391
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Amino acids 384
Annotations 6
Features 25
PDB binders 2
Druggability 0.702

Overview

Basic information about this protein and its source genome.

Accession
PA1631
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA1631
Status
annotated
Amino acids
384
Structure source
AlphaFold
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. GO:0009083 The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine. GO:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
52.727
Human E-value
3.79e-09
Gut microbiome off-target
hit
Essential (DEG)
Y
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 0.702
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MIRDPETLNLLLDSIRQFVRESLVPHEQEVAETDRIPEAIIARMREMGLFGLSIPEAYGGLGVTMEEEVSIAFELGRTSPAFRSLLGTNNGIGSQGIVIDGTEEQKRRYLPRLASGELLSSFCLTEPDSGSDAASLKTTAVRDGEHYVLNGTKRFITNAPQAGIYTVMARTDPAIRGAGGISAFVVERGTPGLSLGKPDRKMGQKGAHTCDVIFDDCRVPASQLIGGVEGVGFKTAMKVLDKGRLHIAAVCVGVAERMLEDALRYALERKQFGQPIAEFQLIQAMLADSKAEAYAARCMVIDAARQRDEGRDVGTEASCAKLFASEMCGRVADRAVQIFGGAGYIGDYGIERFYRDVRLFRIYEGTTQIQQLLIARNMIRAAQG

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0003995 Catalysis of the reaction: a 2,3-saturated acyl-CoA + H+ oxidized [electron-transfer flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein].
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0009083 The chemical reactions and pathways resulting in the breakdown of amino acids containing a branched carbon skeleton, comprising isoleucine, leucine and valine.
  • GO:0033539 A fatty acid beta-oxidation pathway in which the initial step of each oxidation cycle, which converts an acyl-CoA to a trans-2-enoyl-CoA, is catalyzed by acyl-CoA dehydrogenase; the electrons removed by oxidation pass through the respiratory chain to oxygen and leave H2O as the product. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and ends when only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively).
  • GO:0016627 Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records
Show feature table
Start End DB Term Name
235 379 FunFam G3DSA:1.20.140.10:FF:000001 Acyl-CoA dehydrogenase
232 378 Pfam PF00441 Acyl-CoA dehydrogenase, C-terminal domain
232 378 InterPro IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal
109 363 PIRSF PIRSF016578 PIGM
3 83 PIRSF PIRSF016578 PIGM
121 217 Pfam PF02770 Acyl-CoA dehydrogenase, middle domain
121 217 InterPro IPR006091 Acyl-CoA oxidase/dehydrogenase, middle domain
8 119 Gene3D G3DSA:1.10.540.10 -
8 119 InterPro IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
3 119 FunFam G3DSA:1.10.540.10:FF:000001 Very long-chain-specific acyl-CoA dehydrogenase, mitochondrial
337 356 ProSitePatterns PS00073 Acyl-CoA dehydrogenases signature 2.
337 356 InterPro IPR006089 Acyl-CoA dehydrogenase, conserved site
230 375 Gene3D G3DSA:1.20.140.10 -
120 234 FunFam G3DSA:2.40.110.10:FF:000001 Acyl-CoA dehydrogenase, mitochondrial
229 380 SUPERFAMILY SSF47203 Acyl-CoA dehydrogenase C-terminal domain-like
229 380 InterPro IPR036250 Acyl-CoA dehydrogenase-like, C-terminal
6 379 PANTHER PTHR43884 ACYL-COA DEHYDROGENASE
123 135 ProSitePatterns PS00072 Acyl-CoA dehydrogenases signature 1.
123 135 InterPro IPR006089 Acyl-CoA dehydrogenase, conserved site
7 117 Pfam PF02771 Acyl-CoA dehydrogenase, N-terminal domain
7 117 InterPro IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal
6 243 SUPERFAMILY SSF56645 Acyl-CoA dehydrogenase NM domain-like
6 243 InterPro IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
120 229 Gene3D G3DSA:2.40.110.10 -
120 229 InterPro IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain superfamily

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 PA1631
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 0.702

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.

28 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
COS
5OL2
A0A031WJ47 799.6 Da LogP -1.02 TPSA 346.6 3 viol. ✓ Clean CC(C)(CO[P@](=O)(O)O[P@](=O)(O)OC[C@@H]1[C@H]([…
FDA
4IV6
A0QTW7 787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…

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.