Protein profile

PA2152

trehalose synthase

Genome: NC_002516.2

Gene: PA2152 Structure source: AlphaFold UniProt Q9I1W3
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Amino acids 1100
Annotations 5
Features 24
PDB binders 3
Druggability 0.7

Overview

Basic information about this protein and its source genome.

Accession
PA2152
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA2152
Status
annotated
Amino acids
1100
Structure source
AlphaFold
EC
5.4.99.16
GO
GO:0047471 Catalysis of the reaction: maltose = trehalose. GO:0046872 Binding to a metal ion. 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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
50.0
Human E-value
2.47e-15
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 0.7
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MARREKPVFLNDPQWYKDAVIYQVHVKSFYDANNDGIGDFAGLIEKLDYIADLGVNTLWLLPFYPSPRRDDGYDIAQYRGVHSDYGSLADARRFIAEAHRRGLRVITELVINHTSDQHPWFIRARHAKKGSRARDYYVWSDSDEKYQGTRIIFIDTEQSNWTWDPVAQQYYWHRFYSHQPDLNFDNPQVLREVLGVMRYWLDMGVDGLRLDAIPYLIERDGTSSENLPETHQVLKRIRAELDAHYPDRMLLAEANQWPEDTRPYFGGEDGGEGDECHMAFHFPLMPRMYMAIAQEDRYPITDILRQTPDIPANCQWAIFLRNHDELTLEMVTDDERDYLWNHYAADRRARLNLGIRRRLAPLVERDRRRIELLHSLLLSMPGTPTLYYGDEIGMGDNIYLGDRDGVRTPMQWSVDRNGGFSRADPAKLVLPPILDPLYGYQTINVEAQARDPHSLLNWMRRLLAVRSQQKAFGRGSLKMLAPSNRRILAYLREYAEGERQDSILCVANLSRAAQAVELDLASHAGKVPVEMIGGMSFPPIGELTYLLTLPPYGFYWFYLADATQMPSWHVAADERLPELPTLVVKQRLGELLQGASRNILEGETLPAYLPKRRWFAGEKGQPRLCYIVPLDEAEPRCALCEVEIDGLRYQLPLGFLDADQRGDSLPQLLALARLRRGRKVGLLTDAASLPLFARKVLAQLRAEAVIAHGDGEIQFIPAAGLAEMDDIADEDVLPFSVEQSNSSIRFGERMVLKVLRKILPGLHPEIEVGGYLTRHGYPGIAPLLGEVRRVGADGEPHTLMILQGYLNNQGDAWNWTLDNLERAVRDEISAASEALEGQYDSLAELRGFAANLGARLGEMHSVLAGESDDPAFGSRESDEASVQAWALRIAEQLREAGKRLSEPPRPLQGEAAEQARRLLERLPALLERLPLLARQAAGGLLIRVHGDLHLGQVLMVQGDARFIDFEGEPARSLEERRQRHSPMKDVGGMLRSFDYAAAMVLRNAQSTDSSEQADSARRKVAMRYRSEARDAFLAGYRAAAAGLMHAWHGREGEGAALALACLEKAAYELLYEADYRPDWLEVPLAGLAELTEHLLKGKNR

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 4 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

4
  • GO:0047471 Catalysis of the reaction: maltose = trehalose.
  • GO:0046872 Binding to a metal ion.
  • 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:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.

Sequence Features

Domain/signature hits from InterPro and related databases.

24 records
Show feature table
Start End DB Term Name
14 466 Gene3D G3DSA:3.20.20.80 Glycosidases
15 466 CDD cd11334 AmyAc_TreS
23 427 SMART SM00642 aamy
23 427 InterPro IPR006047 Glycosyl hydrolase, family 13, catalytic domain
14 559 NCBIfam TIGR02456 maltose alpha-D-glucosyltransferase
14 559 InterPro IPR012810 Trehalose synthase/alpha-amylase, N-terminal
113 183 Gene3D G3DSA:3.90.400.10 -
113 183 InterPro IPR045857 Oligo-1,6-glucosidase, domain 2
13 559 PANTHER PTHR10357 ALPHA-AMYLASE FAMILY MEMBER
38 396 Pfam PF00128 Alpha amylase, catalytic domain
38 396 InterPro IPR006047 Glycosyl hydrolase, family 13, catalytic domain
475 556 Pfam PF16657 Maltogenic Amylase, C-terminal domain
475 556 InterPro IPR032091 Maltogenic Amylase, C-terminal
576 1090 NCBIfam TIGR02457 putative maltokinase domain
576 1090 InterPro IPR012811 Trehalose synthase/probable maltokinase, C-terminal domain
477 558 SUPERFAMILY SSF51011 Glycosyl hydrolase domain
12 472 SUPERFAMILY SSF51445 (Trans)glycosidases
12 472 InterPro IPR017853 Glycoside hydrolase superfamily
807 1099 Gene3D G3DSA:3.90.1200.10 -
180 466 FunFam G3DSA:3.20.20.80:FF:000055 Trehalose synthase
475 575 Gene3D G3DSA:2.60.40.1180 -
475 575 InterPro IPR013780 Glycosyl hydrolase, all-beta
724 1041 SUPERFAMILY SSF56112 Protein kinase-like (PK-like)
724 1041 InterPro IPR011009 Protein kinase-like domain superfamily

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 PA2152
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 0.373
4 0.333
5 0.257

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.

54 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
CTS
2PWG
Q2PS28 189.2 Da LogP -2.48 TPSA 84.2 ✓ Ro5 ✓ Clean C1C[N@]2C[C@@H]([C@H]([C@@H]([C@H]2[C@H]1O)O)O)O
FLC
3GBE
D0VX20 189.1 Da LogP -5.25 TPSA 140.6 ✓ Ro5 ✓ Clean C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O
NOJ
3GBE
D0VX20 163.2 Da LogP -2.97 TPSA 93.0 ✓ Ro5 ✓ Clean C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)O)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.