Protein profile

PA5174

beta-ketoacyl synthase

Genome: NC_002516.2

Gene: PA5174 fabY Structure source: Experimental + AlphaFold UniProt Q9HU15
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Amino acids 634
Annotations 10
Features 18
PDB binders 4
Druggability 0.649

Overview

Basic information about this protein and its source genome.

Accession
PA5174
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA5174 fabY
Status
annotated
Amino acids
634
Structure source
Experimental + AlphaFold
EC
2.3.1.180
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein]. GO:0033818 Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2. GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
24.542
Human E-value
1.01e-10
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 0.649
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSRLPVIVGFGGYNAAGRSSFHHGFRRMVIESMDPQARQETLAGLAVMMKLVKAEGGRYLAEDGTPLSPEDIERRYAERIFASTLVRRIEPQYLDPDAVHWHKVLELSPAEGQALTFKASPKQLPEPLPANWSIAPAEDGEVLVSIHERCEFKVDSYRALTVKSAGQLPTGFEPGELYNSRFHPRGLQMSVVAATDAIRSTGIDWKTIVDNVQPDEIAVFSGSIMSQLDDNGFGGLMQSRLKGHRVSAKQLPLGFNSMPTDFINAYVLGSVGMTGSITGACATFLYNLQKGIDVITSGQARVVIVGNSEAPILPECIEGYSAMGALATEEGLRLIEGRDDVDFRRASRPFGENCGFTLAESSQYVVLMDDELALRLGADIHGAVTDVFINADGFKKSISAPGPGNYLTVAKAVASAVQIVGLDTVRHASFVHAHGSSTPANRVTESEILDRVASAFGIDGWPVTAVKAYVGHSLATASADQLISALGTFKYGILPGIKTIDKVADDVHQQRLSISNRDMRQDKPLEVCFINSKGFGGNNASGVVLSPRIAEKMLRKRHGQAAFAAYVEKREQTRAAARAYDQRALQGDLEIIYNFGQDLIDEHAIEVSAEQVTVPGFSQPLVYKKDARFSDMLD

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
  • GO:0033818 Catalysis of the reaction: acetyl-CoA + malonyl-[acyl-carrier protein] = acetoacyl-[acyl-carrier protein] + CoA + CO2.
  • GO:0006633 The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
  • GO:0009245 The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common.
  • GO:0009372 The cell-cell signaling process in which single-celled organisms carry out coordinated responses by monitoring their own population density, and often also that of other microbes, by producing small, diffusible, signal molecules, detecting the concentration of these molecules, and triggering a signal transduction pathway when a certain threshold is reached. Quorum sensing can occur amongst microbial communities in the environment or within host organisms.
  • GO:0019290 The chemical reactions and pathways resulting in the formation of siderophores, low molecular weight Fe(III)-chelating substances made by aerobic or facultatively anaerobic bacteria, especially when growing under iron deficient conditions. The complexes of Fe(3+)-siderophores have very high stability constants and are taken up by specific transport systems by microorganisms; the subsequent release of iron requires enzymatic action.
  • 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.

18 records
Show feature table
Start End DB Term Name
78 546 ProSiteProfiles PS52004 Ketosynthase family 3 (KS3) domain profile.
78 546 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
137 543 PANTHER PTHR11712 POLYKETIDE SYNTHASE-RELATED
137 543 InterPro IPR000794 Beta-ketoacyl synthase
382 496 Pfam PF02801 Beta-ketoacyl synthase, C-terminal domain
382 496 InterPro IPR014031 Beta-ketoacyl synthase, C-terminal
154 380 SUPERFAMILY SSF53901 Thiolase-like
154 380 InterPro IPR016039 Thiolase-like
1 606 Gene3D G3DSA:3.40.47.10 -
1 606 InterPro IPR016039 Thiolase-like
185 371 Pfam PF00109 Beta-ketoacyl synthase, N-terminal domain
185 371 InterPro IPR014030 Beta-ketoacyl synthase, N-terminal
5 549 SMART SM00825 Beta-ketoacyl synthase
5 549 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
125 544 CDD cd00828 elong_cond_enzymes
125 544 InterPro IPR047224 Fatty acid synthase subunit alpha-like, C-terminal
344 546 SUPERFAMILY SSF53901 Thiolase-like
344 546 InterPro IPR016039 Thiolase-like

3D Structure

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

3D visualization script Full viewer

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Structural evidence

1 + 1

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

Entry Method Resolution Chain Coverage Links Status
PDB 4CW4
X-ray 1.35 Å A
100.0% 1-634
PDBe RCSB PDBj File
Viewing
AlphaFold PA5174
AlphaFold — — full sequence — Loaded
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 0.649
2 0.493
5 0.215

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 19.18 0.836
2 16.24 0.774
3 4.98 0.225
4 3.11 0.104
5 2.83 0.088

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.

69 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
1LR
4JPF
G3XDA2 257.2 Da LogP 2.34 TPSA 86.6 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)Nc2cccc(c2O)C(=O)O
1X9
4LS7
O34340 223.3 Da LogP 1.11 TPSA 72.7 ✓ Ro5 ✓ Clean C/C=C/C/C=C/CCC(=O)[C@@H]1[C@@H](O1)C(=O)N
1XG
4LS8
O34340 225.3 Da LogP 1.09 TPSA 80.4 ✓ Ro5 ✓ Clean C/C=C/C/C=C/CCC(=O)[C@@H](CC(=O)N)O
N32
4F32
A4JL30 425.5 Da LogP 4.02 TPSA 123.9 ✓ Ro5 ✓ Clean C[C@@]1([C@@H]2C[C@@H]3CC[C@]2(CC3=C)C=CC1=O)CC…

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.