Overview
Basic information about this protein and its source genome.
- Accession
- KP13_02413
- Gene
- AHE43150.1 pheA
- Status
- annotated
- Amino acids
- 386
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- No hit
- Human identity (%)
- 0.0
- Gut microbiome off-target
- hit
- Essential (DEG)
- Y
- DEG identity (%)
- 55.319
- DEG E-value
- 1.1899999999999999e-150
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 92.43
Selected Druggability evidence
AlphaFold / UniProt modelSelected 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.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
5- GO:0009094 The chemical reactions and pathways resulting in the formation of L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0046417 The chemical reactions and pathways involving chorismate, the anion of (3R-trans)-3-((1-carboxyethenyl)oxy)-4-hydroxy-1,5-cyclohexadiene-1-carboxylic acid.
- GO:0004106 Catalysis of the reaction: chorismate = prephenate.
- GO:0004664 Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 108 | 191 | FunFam | G3DSA:3.40.190.10:FF:000044 | Chorismate mutase/prephenate dehydratase |
| 106 | 286 | Pfam | PF00800 | Prephenate dehydratase |
| 106 | 286 | InterPro | IPR001086 | Prephenate dehydratase |
| 105 | 285 | ProSiteProfiles | PS51171 | Prephenate dehydratase domain profile. |
| 105 | 285 | InterPro | IPR001086 | Prephenate dehydratase |
| 280 | 377 | SUPERFAMILY | SSF55021 | ACT-like |
| 280 | 377 | InterPro | IPR045865 | ACT-like domain |
| 11 | 91 | SMART | SM00830 | CM_2_4 |
| 11 | 91 | InterPro | IPR002701 | Chorismate mutase II, prokaryotic-type |
| 325 | 332 | ProSitePatterns | PS00858 | Prephenate dehydratase signature 2. |
| 325 | 332 | InterPro | IPR018528 | Prephenate dehydratase, conserved site |
| 297 | 376 | CDD | cd04905 | ACT_CM-PDT |
| 1 | 380 | PIRSF | PIRSF001500 | Chor_mut_pdt_Ppr |
| 1 | 380 | InterPro | IPR008242 | Bifunctional P-protein, chorismate mutase/prephenate dehydratase |
| 105 | 291 | SUPERFAMILY | SSF53850 | Periplasmic binding protein-like II |
| 1 | 92 | ProSiteProfiles | PS51168 | Chorismate mutase domain profile. |
| 1 | 92 | InterPro | IPR002701 | Chorismate mutase II, prokaryotic-type |
| 1 | 107 | Gene3D | G3DSA:1.20.59.10 | Chorismate mutase |
| 1 | 107 | InterPro | IPR036979 | Chorismate mutase domain superfamily |
| 108 | 281 | Gene3D | G3DSA:3.40.190.10 | - |
| 7 | 27 | Coils | Coil | Coil |
| 291 | 383 | FunFam | G3DSA:3.30.70.260:FF:000022 | Chorismate mutase/prephenate dehydratase |
| 11 | 89 | Pfam | PF01817 | Chorismate mutase type II |
| 11 | 89 | InterPro | IPR002701 | Chorismate mutase II, prokaryotic-type |
| 261 | 283 | ProSitePatterns | PS00857 | Prephenate dehydratase signature 1. |
| 261 | 283 | InterPro | IPR018528 | Prephenate dehydratase, conserved site |
| 299 | 376 | ProSiteProfiles | PS51671 | ACT domain profile. |
| 299 | 376 | InterPro | IPR002912 | ACT domain |
| 192 | 274 | FunFam | G3DSA:3.40.190.10:FF:000034 | Chorismate mutase/prephenate dehydratase |
| 58 | 378 | PANTHER | PTHR21022 | PREPHENATE DEHYDRATASE P PROTEIN |
| 103 | 287 | CDD | cd13631 | PBP2_Ct-PDT_like |
| 291 | 383 | Gene3D | G3DSA:3.30.70.260 | - |
| 189 | 274 | Gene3D | G3DSA:3.40.190.10 | - |
| 1 | 107 | FunFam | G3DSA:1.20.59.10:FF:000002 | Chorismate mutase/prephenate dehydratase |
| 7 | 89 | NCBIfam | TIGR01797 | chorismate mutase |
| 7 | 89 | InterPro | IPR010952 | Chorismate mutase, gammaproteobacteria |
| 6 | 93 | SUPERFAMILY | SSF48600 | Chorismate mutase II |
| 6 | 93 | InterPro | IPR036263 | Chorismate mutase type II superfamily |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GTV9
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02413
|
ColabFold | — | — | 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 | 0.694 | ||||||
| 10 | 0.362 | ||||||
| 2 | 0.274 |
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 | 11.6 | 0.617 | ||||||
| 2 | 8.66 | 0.463 | ||||||
| 3 | 2.41 | 0.065 | ||||||
| 4 | 1.37 | 0.016 |
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 | 0.537 |
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 | 10.86 | 0.583 | ||||||
| 2 | 6.75 | 0.344 | ||||||
| 3 | 1.69 | 0.029 |
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.
Highest-confidence structural evidence: ligands co-crystallized with this exact protein. If the source PDB is loaded in TPW, use Open crystal to inspect it in the structure viewer.
No PDB structure with a co-crystallized ligand found for this exact protein.
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.
| Ligand | Source crystal | UniProt (homolog) | MW · LogP · TPSA | Lipinski | PAINS | SMILES |
|---|---|---|---|---|---|---|
| TSA | P0A9J8 | 228.2 Da LogP -0.38 TPSA 104.1 | ✓ Ro5 | ✓ Clean |
C1[C@@H]2[C@@H](C=C[C@]1(C[C@H](O2)C(=O)O)C(=O)…
|
Experimental bioactivity from ChEMBL measured directly on this protein. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL bioactivity data found for this exact protein.
Bioactivity inferred from similar proteins in ChEMBL. Score = pchembl (−log Ki/IC₅₀; higher = more potent).
No ChEMBL hits found through similar proteins.
Proposed virtual-screening candidates from ZINC. Score = Tanimoto similarity to a known binder (0–1; higher = more similar).
No virtual-screening candidates for this protein.
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.