KpATCC43816 Protein target profile

fabB

Accession: VK055_4800

Gene: fabB AIK83327.1 3D evidence: AlphaFold DB model + ColabFold model Metabolism 10 reactions UniProt A0A0H3GR90
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Length 398
Pocket druggability (P2Rank · AlphaFold DB model) 0.742
Metabolic reactions 10
Chokepoint Yes
Direct ligand evidence 0 67 total records
Functional annotation 1 EC 4 GO
Target summary

Strong target candidate with converging metabolic, structural and chemical evidence.

Automated synthesis of the evidence currently loaded. Review the underlying records before prioritizing this protein.

Main supporting evidence

Metabolic chokepoint Catalyzes a reaction that is the only producer or consumer of a metabolite in the imported metabolic model. Central metabolic position More central than 91.5% of genes in this genome. No isoenzyme backup detected Imported GPR rules do not show an alternative enzyme for the catalyzed reaction set. Core gene across strains Marked as conserved by both pan-genome tools: Roary and CoreCruncher. Review the complete evidence below

Risks to review

Human similarity Top human hit identity: 34.807%. This target also has a predicted binding pocket (P2Rank 0.74) — check the ligand evidence before deprioritizing on off-target risk alone. Microbiome similarity 199 of 4744 screened genomes (4.2%) have a significant similarity hit. This target also has a predicted binding pocket (P2Rank 0.74) — check the ligand evidence before deprioritizing on off-target risk alone.

Evidence coverage

Core evidence streams are available for this target.
Terms and data sources used on this page

PDB: experimentally determined structures from the Protein Data Bank. These are the strongest structural evidence, but may cover only part of the protein.

AlphaFold DB model: a precomputed predicted structure downloaded from AlphaFold Database/UniProt, not an experiment performed here.

ColabFold model: a predicted structure generated for this workspace; interpret it with coverage and confidence.

pLDDT: confidence score for predicted structures. High values support local geometry; low values mean the region should not drive pocket interpretation.

FPocket / P2Rank: software tools that predict possible ligand-binding pockets on a 3D structure. They are useful screening signals, not experimental validation.

Druggability: a pocket-based estimate of whether a small molecule could bind productively. It does not mean a drug already exists.

PDB ligand: a compound observed in an experimental structure. Direct same-protein records are stronger than homolog-transferred records.

ChEMBL: a public database of measured compound bioactivity. Direct entries are stronger than entries transferred from similar proteins.

ZINC: a purchasable-compound database. Here it marks proposed candidates from chemical similarity, not measured binders.

LigQ / LigQ_2: an internal Target pipeline step that gathers PDB, ChEMBL, and ZINC ligand evidence for each protein.

Off-target: sequence similarity to proteins we prefer not to hit, such as human proteins or beneficial gut microbiome proteins.

DEG: Database of Essential Genes. A match suggests the protein resembles genes known to be essential in other organisms.

Roary / CoreCruncher: pan-genome tools used to decide whether a gene is core across analyzed strains or accessory/strain-specific.

EC / GO: functional annotations: EC describes enzyme reactions; GO describes biological process, molecular function, or cellular component.

KEGG pathway: a curated metabolic route label used here to group reactions imported from the metabolic model.

Chokepoint: a metabolic reaction that is the only producer or consumer of a metabolite in the imported model.

Prioritization evidence

Selectivity, essentiality, structural confidence, conservation, and predicted binding-site evidence.

Off-target risk

Human off-target
Hit
Human identity (%)
34.807 Lower values reduce human off-target concern.
Human E-value
3.5400000000000004e-58
Gut microbiome similarity
4.2% of screened genomes Lower prevalence suggests narrower overlap with the screened gut microbiome.

Essentiality

Essential (DEG)
Y
DEG identity (%)
96.962 Higher values support similarity to known essential genes.
DEG E-value
0.0 Smaller values mean stronger essential-gene similarity.

Structure confidence

ColabFold pLDDT
97.56 0-100 confidence; >70 supports local structural interpretation.

Binding-site evidence

AlphaFold DB / UniProt model

P2Rank's binding-site probability is the primary druggability signal shown across the app; FPocket's druggability score is shown alongside it for comparison. Both estimate small-molecule pocket quality after applying the curated structure priority — neither is experimental binding evidence. The 3D viewer may show a different loaded structure, so visible pockets can differ.

Druggability (P2Rank) 0.742
Structure A0A0H3GR90
Pocket Pocket 1
Druggability (FPocket) 0.588
Structure A0A0H3GR90
Pocket Pocket 11
ColabFold model
P2Rank 0.821 · Pocket 1
FPocket 0.804 · Pocket 2
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 199 / 4744 genomes with a hit
Prevalence 4.2%

Metabolic context

Reactions catalyzed, pathway membership, and centrality in the genome-scale metabolic network.

Explore metabolic network

Attractive metabolic target: catalyzes a producing chokepoint reaction, no isoenzyme backup detected, more central than 91.5% of genes in this genome.

Relative network centrality 91.5% more central than 91.5% of genes in this genome
Chokepoint Chokepoint gene
Pathways

No specific KEGG pathway assigned - this reaction either has no KEGG mapping, or only matches a generic overview map with no route-level information.

Catalyzed reactions

10 reactions mapped to this gene in the metabolic model. Open the full network to see each one, with substrates/products and the reaction-reaction map.

Imported from KpATCC43816.sbml · 2026-07-09

Sequence

Primary amino-acid sequence viewer.

MGIVSSIGNNQQEVLASLREGRSGITFSQELKDSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAYLSMEQAVADAGLAPEAYQNNPRVGLIAGSGGGSPKFQVFGADAMRSPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISSACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEFDAMGALSTKYNDTPEKASRTYDANRDGFVIAGGGGMVVVEELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCMQMAMHGVDTPIDYLNSHGTSTPVGDVKELGAIREVFGDNSPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINVEELDEQAAGLNIVTKPTDAKLTTVMSNSFGFGGTNATLVMRKYNA

Functional annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Subcellular localization

Localization
Cytoplasmic

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0004315 Catalysis of the reaction: acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO2 + [acyl-carrier protein].
  • 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:0016746 Catalysis of the transfer of an acyl group from one compound (donor) to another (acceptor).
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Sequence domains and features

Domain and signature matches imported from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
1 393 CDD cd00834 KAS_I_II
1 393 InterPro IPR000794 Beta-ketoacyl synthase
146 162 ProSitePatterns PS00606 Ketosynthase family 3 (KS3) active site signature.
146 162 InterPro IPR018201 Beta-ketoacyl synthase, active site
1 395 ProSiteProfiles PS52004 Ketosynthase family 3 (KS3) domain profile.
1 395 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
1 238 Pfam PF00109 Beta-ketoacyl synthase, N-terminal domain
1 238 InterPro IPR014030 Beta-ketoacyl synthase, N-terminal
252 398 Gene3D G3DSA:3.40.47.10 -
252 398 InterPro IPR016039 Thiolase-like
1 251 FunFam G3DSA:3.40.47.10:FF:000006 3-oxoacyl-[acyl-carrier-protein] synthase I
1 245 SUPERFAMILY SSF53901 Thiolase-like
1 245 InterPro IPR016039 Thiolase-like
1 251 Gene3D G3DSA:3.40.47.10 -
1 251 InterPro IPR016039 Thiolase-like
3 398 SMART SM00825 Beta-ketoacyl synthase
3 398 InterPro IPR020841 Polyketide synthase, beta-ketoacyl synthase domain
207 396 SUPERFAMILY SSF53901 Thiolase-like
207 396 InterPro IPR016039 Thiolase-like
246 353 Pfam PF02801 Beta-ketoacyl synthase, C-terminal domain
246 353 InterPro IPR014031 Beta-ketoacyl synthase, C-terminal
252 397 FunFam G3DSA:3.40.47.10:FF:000005 3-oxoacyl-[acyl-carrier-protein] synthase I
1 396 PANTHER PTHR11712 POLYKETIDE SYNTHASE-RELATED
1 396 InterPro IPR000794 Beta-ketoacyl synthase

3D structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; AlphaFold DB and ColabFold models typically cover the full protein but remain computational predictions.

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Pocket score High Medium Low
How colors and pocket overlays are used
Uniform protein color marks the displayed model as a single molecular object.
Experimental PDB structures may be colored by chain to distinguish subunits or copies present in the file.
Pocket colors and alpha spheres are evidence overlays for predicted binding cavities; they are not alternative protein chains.
'Alpha spheres' is FPocket's own cavity-shape geometry, imported when available and aligned with the loaded structure.
'Pocket atoms'/'Predicted site atoms' show the pocket's residue atoms instead: P2Rank reports residues rather than alpha spheres, and FPocket falls back to this when alpha-sphere geometry is unavailable or doesn't align.
'No pocket geometry' means neither alpha spheres nor residue-position data could be found for that pocket; the layer just highlights the same residues as 'Nearby residues'.
Pocket details Inspect a specific pocket, or open the full viewer

Binding pockets · P2Rank

Druggability (P2Rank): high ≥ 0.5 · medium 0.2–0.49 · low < 0.2

Pocket 1 P2Rank #1
0.742
Likely same site as FPocket 1 0.8 Å 17 shared residues 100% of smaller site
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Surrounding area
Pocket 2 P2Rank #2
0.523
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Surrounding area
Pocket 3 P2Rank #3
0.031
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Surrounding area
Pocket 4 P2Rank #4
0.004
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Surrounding area
Pocket 5 P2Rank #5
0.003
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Surrounding area

Binding pockets · FPocket

Druggability (FPocket): high ≥ 0.7 · medium 0.4–0.69 · low < 0.4

Pocket 1 FPocket #11
0.588
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Surrounding area
Pocket 2 FPocket #1
0.466 Unusual size
Likely same site as P2Rank 1 0.8 Å 17 shared residues 100% of smaller site
Show in viewer
Surrounding area
All structural evidence 0 experimental · 2 predicted

Structural evidence

0 + 2

Experimental PDB entries plus predicted AlphaFold DB or ColabFold models. Click Switch to display a different loaded structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold DB AF_A0A0H3GR90
AlphaFold DB — — full sequence — Viewing
ColabFold VK055_4800
ColabFold — — full sequence — Loaded

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.

67 records
Chemistry signal

Structural ligand evidence is available for this target.

Direct evidence 0 same-protein records
Transferred evidence 17 records from similar proteins
Structural ligands 17 0 loaded crystals
Measured bioactivity 0 direct and transferred ChEMBL records
Proposed compounds 50 similarity-based ZINC candidates
Best available ligand signal
07K PDB via homolog 158.2 Da · LogP 2.13 · TPSA 38.9 Open detail RCSB PDB
07L PDB via homolog Detail RCSB PDB
1LR PDB via homolog Detail RCSB PDB
1X9 PDB via homolog Detail RCSB PDB
1XG PDB via homolog Detail RCSB PDB

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
07K RCSB PDB
3U0E
Q2YQQ9 158.2 Da LogP 2.13 TPSA 38.9 ✓ Ro5 ✓ Clean Cc1cccc2c1nccc2N
07L RCSB PDB
3U0F
Q2YQQ9 162.1 Da LogP 1.50 TPSA 50.4 ✓ Ro5 ✓ Clean c1cc2c(cc1O)OC(=O)C=C2
1LR RCSB PDB
4JPF
G3XDA2 257.2 Da LogP 2.34 TPSA 86.6 ✓ Ro5 ✓ Clean c1ccc(cc1)C(=O)Nc2cccc(c2O)C(=O)O
1X9 RCSB PDB
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 RCSB PDB
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
3MQ RCSB PDB
3MQD
Q2YQQ9 181.2 Da LogP 1.90 TPSA 46.3 ✓ Ro5 ✓ Clean c1cc(sc1)c2cc(no2)CO
6W5 RCSB PDB
5KOF
P0A953 395.3 Da LogP -1.59 TPSA 174.3 1 viol. ✓ Clean CC(C)(COP(=O)(O)O)[C@@H](C(=O)NCCC(=O)NCCNC(=O)…
CER RCSB PDB
1FJ8
P0A953 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
DAO RCSB PDB
1EK4
P0A953 200.3 Da LogP 3.99 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCCCC(=O)O
DKA RCSB PDB
1F91
P0A953 172.3 Da LogP 3.21 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCCCC(=O)O
MRJ RCSB PDB
6OKC
P0A953 523.6 Da LogP 2.14 TPSA 174.3 2 viol. ✓ Clean CCCCCCCCCCCC(=O)NCCNC(=O)CCNC(=O)[C@@H](C(C)(C)…
N32 RCSB PDB
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…
NH4 RCSB PDB
2BUH
P0A953 18.0 Da LogP 0.38 TPSA 36.5 ✓ Ro5 ✓ Clean [NH4+]
OCA RCSB PDB
2BUI
P0A953 144.2 Da LogP 2.43 TPSA 37.3 ✓ Ro5 ✓ Clean CCCCCCCC(=O)O
TL5 RCSB PDB
2AQ7
P0A953 224.3 Da LogP 3.37 TPSA 37.3 ✓ Ro5 ✓ Clean C\C=C\C(=C\[C@@]1(C(=C(C(=O)S1)C)O)C)\C
TL6 RCSB PDB
2AQB
P0A953 196.3 Da LogP 2.59 TPSA 37.3 ✓ Ro5 ✓ Clean CC1=C([C@@](SC1=O)(C)\C=C\C=C)O
TLM RCSB PDB
1FJ4
P0A953 210.3 Da LogP 2.98 TPSA 37.3 ✓ Ro5 ✓ Clean CC1=C([C@@](SC1=O)(C)\C=C(/C)\C=C)O

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.

Cross-references

External database identifiers for this protein, its structures, ligands, and metabolic reactions.

Sequence

UniProt A0A0H3GR90

Pathways

BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Myristoyl-ACPs/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C12-H24/CARBON-DIOXIDE/ACP.90. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Octanoyl-ACPs/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C6-H12/CARBON-DIOXIDE/ACP.88. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-POLYMER-INST-Saturated-Fatty-Acyl-ACPs-C16-H32/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C18-H36/CARBON-DIOXIDE/ACP.122. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Stearoyl-ACPs/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C16-H32/CARBON-DIOXIDE/ACP.89. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-POLYMER-INST-Saturated-Fatty-Acyl-ACPs-C2-H4/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C4-H8/CARBON-DIOXIDE/ACP.118. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Dodecanoyl-ACPs/MALONYL-ACP/PROTON//CPD-28058/CARBON-DIOXIDE/ACP.65. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Palmitoyl-ACPs/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C14-H28/CARBON-DIOXIDE/ACP.90. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-Decanoyl-ACPs/MALONYL-ACP/PROTON//3-oxo-dodecanoyl-ACPs/CARBON-DIOXIDE/ACP.75. BioCyc 3-OXOACYL-ACP-SYNTH-RXN-POLYMER-INST-Saturated-Fatty-Acyl-ACPs-C0-H0/MALONYL-ACP/PROTON//POLYMER-INST-B-KETOACYL-ACP-C2-H4/CARBON-DIOXIDE/ACP.118. BioCyc RXN-9652