Protein profile

PA2815

acyl-CoA dehydrogenase

Genome: NC_002516.2

Gene: PA2815 Structure source: AlphaFold UniProt Q9I028
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Amino acids 815
Annotations 9
Features 38
PDB binders 3
Druggability 0.765

Overview

Basic information about this protein and its source genome.

Accession
PA2815
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2815
Status
annotated
Amino acids
815
Structure source
AlphaFold
EC
1.3.8.7 1.3.8.8
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:0004466 Catalysis of the reaction: a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons. GO:0070991 Catalysis of the reaction: a medium-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a medium-chain trans-(2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. A medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons. 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).

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
38.542
Human E-value
5.03e-10
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
CytoplasmicMembrane

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 0.765
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 7 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

7
  • 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:0004466 Catalysis of the reaction: a long-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. A long-chain fatty acid has an aliphatic tail containing 13 to 22 carbons.
  • GO:0070991 Catalysis of the reaction: a medium-chain 2,3-saturated fatty acyl-CoA + H+ + oxidized [electron-transfer flavoprotein] = a medium-chain trans-(2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]. A medium-chain fatty acid has an aliphatic tail containing 6 to 12 carbons.
  • 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.

38 records
Show feature table
Start End DB Term Name
605 815 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
23 40 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
240 338 Pfam PF02770 Acyl-CoA dehydrogenase, middle domain
240 338 InterPro IPR006091 Acyl-CoA oxidase/dehydrogenase, middle domain
1 19 Phobius SIGNAL_PEPTIDE Signal peptide region
363 509 FunFam G3DSA:1.20.140.10:FF:000009 Acyl-CoA dehydrogenase
2 19 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
363 513 SUPERFAMILY SSF47203 Acyl-CoA dehydrogenase C-terminal domain-like
363 513 InterPro IPR036250 Acyl-CoA dehydrogenase-like, C-terminal
65 544 Phobius CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the cytoplasm.
122 238 Gene3D G3DSA:1.10.540.10 -
122 238 InterPro IPR037069 Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily
3 14 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
1 16 SignalP_EUK SignalP-TM SignalP-TM
43 64 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
1 2 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
75 524 PANTHER PTHR48083 MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED
363 508 Pfam PF00441 Acyl-CoA dehydrogenase, C-terminal domain
363 508 InterPro IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal
566 584 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
138 236 Pfam PF02771 Acyl-CoA dehydrogenase, N-terminal domain
138 236 InterPro IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal
545 565 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
239 362 Gene3D G3DSA:2.40.110.10 -
239 362 InterPro IPR046373 Acyl-CoA oxidase/dehydrogenase, middle domain superfamily
239 362 FunFam G3DSA:2.40.110.10:FF:000010 Acyl-CoA dehydrogenase
517 802 Pfam PF09317 Acyl-CoA dehydrogenase, C-terminal, bacterial type
517 802 InterPro IPR015396 Acyl-CoA dehydrogenase, C-terminal, bacterial-type
123 358 SUPERFAMILY SSF56645 Acyl-CoA dehydrogenase NM domain-like
123 358 InterPro IPR009100 Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily
649 669 Coils Coil Coil
45 67 TMHMM TMhelix Region of a membrane-bound protein predicted to be embedded in the membrane.
20 42 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
210 510 CDD cd00567 ACAD
123 238 FunFam G3DSA:1.10.540.10:FF:000004 Acyl-CoA dehydrogenase
15 19 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
585 604 Phobius TRANSMEMBRANE Region of a membrane-bound protein predicted to be embedded in the membrane.
363 508 Gene3D G3DSA:1.20.140.10 -

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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA2815
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
3 0.765
4 0.761

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.

18 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
CAA
1JQI
P15651 851.6 Da LogP -1.36 TPSA 380.7 3 viol. ✓ Clean CC(=O)CC(=O)SCCNC(=O)CCNC(=O)[C@@H](C(C)(C)CO[P…
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.