Protein profile

KP13_00302

Cytoplasmic trehalase

Genome: KpKP13

Gene: AHE42212.1 treF Structure source: AlphaFold + ColabFold UniProt A0A0H3GYL8
Amino acids 550
Annotations 7
Features 29
PDB binders 1
Druggability 0.654

Overview

Basic information about this protein and its source genome.

Accession
KP13_00302
Gene
AHE42212.1 treF
Status
annotated
Amino acids
550
Structure source
AlphaFold + ColabFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
34.221
Human E-value
6.2e-75
Gut microbiome off-target
hit
Essential (DEG)
N
DEG identity (%)
0.0
Localization
Cytoplasmic
ColabFold pLDDT
90.89

Selected Druggability evidence

AlphaFold / UniProt model

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 0.654
Structure A0A0H3GYL8
Pocket Pocket 4
P2Rank 0.904
Structure A0A0H3GYL8
Pocket Pocket 1
ColabFold model
FPocket 0.352 · Pocket 23
P2Rank 0.858 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 76 / 4744 genomes with a hit
Normalized 0.016

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 6 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

6
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
  • GO:0071474 Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell.
  • GO:0005991 The chemical reactions and pathways involving trehalose, a disaccharide that consists of two molecules of glucose and is isomeric with sucrose.
  • GO:0004555 Catalysis of the reaction: alpha,alpha-trehalose + H2O = 2 D-glucose.
  • GO:0005993 The chemical reactions and pathways resulting in the breakdown of trehalose, a disaccharide that consists of two molecules of glucose and is isomeric with sucrose.

Sequence Features

Domain/signature hits from InterPro and related databases.

29 records
Show feature table
Start End DB Term Name
54 549 FunFam G3DSA:1.50.10.10:FF:000003 Cytoplasmic trehalase
54 549 Gene3D G3DSA:1.50.10.10 -
54 549 InterPro IPR012341 Six-hairpin glycosidase-like superfamily
61 549 PANTHER PTHR23403 TREHALASE
61 549 InterPro IPR001661 Glycoside hydrolase, family 37
34 549 Hamap MF_01059 Cytoplasmic trehalase [treF].
34 549 InterPro IPR023715 Trehalase, cytoplasmic
55 547 SUPERFAMILY SSF48208 Six-hairpin glycosidases
55 547 InterPro IPR008928 Six-hairpin glycosidase superfamily
165 178 ProSitePatterns PS00927 Trehalase signature 1.
165 178 InterPro IPR018232 Glycoside hydrolase, family 37, conserved site
452 468 PRINTS PR00744 Glycosyl hydrolase family 37 signature
452 468 InterPro IPR001661 Glycoside hydrolase, family 37
389 405 PRINTS PR00744 Glycosyl hydrolase family 37 signature
389 405 InterPro IPR001661 Glycoside hydrolase, family 37
346 363 PRINTS PR00744 Glycosyl hydrolase family 37 signature
346 363 InterPro IPR001661 Glycoside hydrolase, family 37
281 298 PRINTS PR00744 Glycosyl hydrolase family 37 signature
281 298 InterPro IPR001661 Glycoside hydrolase, family 37
314 331 PRINTS PR00744 Glycosyl hydrolase family 37 signature
314 331 InterPro IPR001661 Glycoside hydrolase, family 37
530 543 PRINTS PR00744 Glycosyl hydrolase family 37 signature
530 543 InterPro IPR001661 Glycoside hydrolase, family 37
207 225 PRINTS PR00744 Glycosyl hydrolase family 37 signature
207 225 InterPro IPR001661 Glycoside hydrolase, family 37
459 468 ProSitePatterns PS00928 Trehalase signature 2.
459 468 InterPro IPR018232 Glycoside hydrolase, family 37, conserved site
71 546 Pfam PF01204 Trehalase
71 546 InterPro IPR001661 Glycoside hydrolase, family 37

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

0 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GYL8
AlphaFold full sequence Viewing
ColabFold KP13_00302
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
4 0.654
5 0.224

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 22.03 0.876
2 8.47 0.452
3 3.41 0.122
4 3.18 0.109
5 1.66 0.028

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.

11 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
3CU P13482 205.2 Da LogP -3.51 TPSA 104.4 ✓ Ro5 ✓ Clean C1[C@@H]([C@H]([C@H]2[N@@]1[C@@H]([C@H]([C@@H]2…

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.