Protein profile

PA4814

2,4-dienoyl-CoA reductase

Genome: NC_002516.2

Gene: fadH2 PA4814 Structure source: AlphaFold UniProt Q9HUZ6
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Amino acids 681
Annotations 6
Features 22
PDB binders 3
Druggability 0.73

Overview

Basic information about this protein and its source genome.

Accession
PA4814
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
fadH2 PA4814
Status
annotated
Amino acids
681
Structure source
AlphaFold
GO
GO:0008670 Catalysis of the reactions: a 4,5-saturated-(2E)-enoyl-CoA + NADP+ = a (2E,4E)-dienoyl-CoA + H+ + NADPH, and a (2E,4Z)-dienoyl-CoA + H+ + NADPH = a 4,5-saturated-(2E)-enoyl-CoA + NADP+. GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms. GO:0046872 Binding to a metal ion. GO:0033543 A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to trans-2-enoyl-CoA by 2,4-dienoyl-CoA reductase and delta3-delta2-enoyl-CoA isomerase; trans-2-enoyl-CoA returns to the core beta-oxidation pathway for further degradation. 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:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
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 0.73
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MRTPYPPLAAAPYPHLLAPLDLGFTRLRNRVVMGSMHTGLEDRLWDFGKLAAYYRERARGGVGLIVTGGFAPCREGWLLPFGSSLTSALEVPAHRRLTQAVHAEGGKILLQILHAGRYGYHPMAVSASPLKSPISWFTPRELSERGIRKTIRAFVRCARLAKAAAYDGVEVMGSEGYLLNQFLCPRTNRRDDQWGGPLENRMRLALEIVRGIRRIVGQRFILCYRLSLLDLVEGGNTWDEVRRIALALEEAGITLLNTGIGWHESRVPTIVTSVPRAAFAEVSARLRHELKVPVIASNRINTPEVAESLLATDKADLVSMARPLLADPQFVAKAGAGRAEEINTCIACNQACLDHAFANRRATCLVNPRAAFETELRYRKARTQKRIAVIGAGPAGLSAACVAAERGHRVSLFEASGEIGGQFNLAKRIPGKEEFRETLRYFRVRLERLGVDLRLGHRVRQGELDGQFDDVVVATGIQPRRPRIDGIGGPTVLSYVDVLRGAPVGARVAIVGAGGIGFDVAAFLVAAPSDGQPRALGEWLAEWGVDLDNSQPGGLREPAPTRPARQVWLLQRKPGAPGAQLGKTSGWVHRAHLRHNAVRMLGGVEYLKIDERGLLIRVDGVERWLEVDNVVICAGQEPLRELQIRQATESLRFHLIGGARVAGELDAKRAIREGAMLAARL

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6
  • GO:0008670 Catalysis of the reactions: a 4,5-saturated-(2E)-enoyl-CoA + NADP+ = a (2E,4E)-dienoyl-CoA + H+ + NADPH, and a (2E,4Z)-dienoyl-CoA + H+ + NADPH = a 4,5-saturated-(2E)-enoyl-CoA + NADP+.
  • GO:0010181 Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
  • GO:0046872 Binding to a metal ion.
  • GO:0033543 A fatty acid beta-oxidation pathway by which fatty acids having cis-double bonds on even-numbered carbons are degraded. In this pathway, the intermediate 2,4-dienoyl-CoA is converted to trans-2-enoyl-CoA by 2,4-dienoyl-CoA reductase and delta3-delta2-enoyl-CoA isomerase; trans-2-enoyl-CoA returns to the core beta-oxidation pathway for further degradation. 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:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records
Show feature table
Start End DB Term Name
507 525 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
627 643 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
387 406 PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature
12 379 FunFam G3DSA:3.20.20.70:FF:000082 NADPH-dependent 2,4-dienoyl-CoA reductase
16 340 Pfam PF00724 NADH:flavin oxidoreductase / NADH oxidase family
16 340 InterPro IPR001155 NADH:flavin oxidoreductase/NADH oxidase, N-terminal
16 368 CDD cd02930 DCR_FMN
385 643 Pfam PF07992 Pyridine nucleotide-disulphide oxidoreductase
385 643 InterPro IPR023753 FAD/NAD(P)-binding domain
12 379 Gene3D G3DSA:3.20.20.70 Aldolase class I
12 379 InterPro IPR013785 Aldolase-type TIM barrel
13 681 PANTHER PTHR42917 2,4-DIENOYL-COA REDUCTASE
386 408 PRINTS PR00411 Pyridine nucleotide disulphide reductase class-I signature
628 642 PRINTS PR00411 Pyridine nucleotide disulphide reductase class-I signature
679 681 Coils Coil Coil
385 674 Gene3D G3DSA:3.40.50.720 -
11 372 SUPERFAMILY SSF51395 FMN-linked oxidoreductases
480 634 Gene3D G3DSA:3.50.50.60 -
480 634 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
479 636 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
479 636 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
343 527 SUPERFAMILY SSF51971 Nucleotide-binding domain

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 PA4814
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 0.73
8 0.285

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.

3 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
FLC
6L6J
A0A0L8AFM7 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
J5H
6QKR
E1YD54 921.7 Da LogP 1.13 TPSA 363.6 3 viol. ✓ Clean CC(C)(COP(=O)(O)OP(=O)(O)OC[C@@H]1[C@H]([C@H]([…
MDE
1PS9
P42593 994.9 Da LogP 0.91 TPSA 382.6 3 viol. ✓ Clean CCCCC[C@@H](C\C=C\C(=O)SCCNC(=O)CCNC(C(=O)C(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.