Protein profile

PA5372

choline dehydrogenase

Genome: NC_002516.2

Gene: PA5372 betA Structure source: AlphaFold UniProt Q9HTJ2
Amino acids 561
Annotations 8
Features 22
PDB binders 8
Druggability 0.721

Overview

Basic information about this protein and its source genome.

Accession
PA5372
Gene
PA5372 betA
Status
annotated
Amino acids
561
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
49.724
Human E-value
4.8e-174
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
CytoplasmicMembrane

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 0.721
Structure
Pocket

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

2 EC 6 GO

Enzyme Commission (EC)

2

Gene Ontology (GO)

6
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
  • GO:0008802 Catalysis of the reaction: betaine aldehyde + NAD+ + H2O = betaine + NADH + H+.
  • GO:0008812 Catalysis of the reaction: A + choline = AH(2) + betaine aldehyde.
  • GO:0050660 Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
  • GO:0019285 The chemical reactions and pathways resulting in the formation of betaine (N-trimethylglycine) from the oxidation of choline.
  • GO:0016614 Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group act as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records
Show feature table
Start End DB Term Name
297 479 SUPERFAMILY SSF54373 FAD-linked reductases, C-terminal domain
1 540 PIRSF PIRSF000137 Alcohol_oxidase
1 540 InterPro IPR012132 Glucose-methanol-choline oxidoreductase
5 302 Pfam PF00732 GMC oxidoreductase
5 302 InterPro IPR000172 Glucose-methanol-choline oxidoreductase, N-terminal
6 527 Gene3D G3DSA:3.50.50.60 -
6 527 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
4 541 PANTHER PTHR11552 GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE
4 541 InterPro IPR012132 Glucose-methanol-choline oxidoreductase
45 474 Gene3D G3DSA:3.30.560.10 Glucose Oxidase, domain 3
1 537 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
1 537 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
3 556 Hamap MF_00750 Oxygen-dependent choline dehydrogenase [betA].
3 556 InterPro IPR011533 Oxygen-dependent choline dehydrogenase
84 107 ProSitePatterns PS00623 GMC oxidoreductases signature 1.
84 107 InterPro IPR000172 Glucose-methanol-choline oxidoreductase, N-terminal
261 275 ProSitePatterns PS00624 GMC oxidoreductases signature 2.
261 275 InterPro IPR000172 Glucose-methanol-choline oxidoreductase, N-terminal
395 529 Pfam PF05199 GMC oxidoreductase
395 529 InterPro IPR007867 Glucose-methanol-choline oxidoreductase, C-terminal
6 539 NCBIfam TIGR01810 choline dehydrogenase
6 539 InterPro IPR011533 Oxygen-dependent choline dehydrogenase

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 + 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 PA5372
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 0.721

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.

58 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
BET Q7X2H8 118.2 Da LogP -0.22 TPSA 37.3 ✓ Ro5 ✓ Clean C[N+](C)(C)CC(=O)O
FAO Q7X2H8 789.6 Da LogP -2.56 TPSA 355.8 3 viol. ✓ Clean Cc1cc2c(cc1C)[N@@]([C@@H]3[C@H](N2)C(=O)NC(=O)N…
FDA B8MX95 787.6 Da LogP -1.75 TPSA 363.3 3 viol. ✓ Clean Cc1cc2c(cc1C)N(C3=C(N2)C(=O)NC(=O)N3)C[C@@H]([C…
OXY P13006 32.0 Da LogP 0.07 TPSA 34.1 ✓ Ro5 ✓ Clean O=O
P4C P13006 324.4 Da LogP -0.72 TPSA 92.7 ✓ Ro5 ✓ Clean C(COCCOCCOCCOCCOCCOCC=O)O
PLM A0A248QE08 256.4 Da LogP 5.55 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCC(=O)O
PXM Q5NT46 168.2 Da LogP 0.05 TPSA 79.4 ✓ Ro5 ✓ Clean Cc1c(c(c(cn1)CO)CN)O
STE A0A248QE08 284.5 Da LogP 6.33 TPSA 37.3 1 viol. ✓ Clean CCCCCCCCCCCCCCCCCC(=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.