Protein profile

PA4548

D-amino acid oxidase

Genome: NC_002516.2

Gene: PA4548 thiO Structure source: AlphaFold UniProt P33642
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Amino acids 364
Annotations 7
Features 16
PDB binders 10
Druggability 0.687

Overview

Basic information about this protein and its source genome.

Accession
PA4548
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4548 thiO
Status
annotated
Amino acids
364
Structure source
AlphaFold
EC
1.4.3.19
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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:0043799 Catalysis of the reactions: (1) glycine + H2O + O2 = glyoxylate + NH4+ + H2O2; (2) D-alanine + H2O + O2 = pyruvate + NH4+ + H2O2; (3) sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2; (4) N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2. GO:0009228 The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver. GO:0009229 The chemical reactions and pathways resulting in the formation of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle. GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
25.258
Human E-value
9.66e-08
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 0.687
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSERVVVVGAGVIGLLTARELALAGLRVTLVERGESGREASWAGGGIVSPLYPWRYSPAVTALAHWSQDFYPALGQRLLDETGLDPEVHTVGLYWLDLDDQTEALQWARKHTRPLKEVPIEEAYAAVPGLGAGFQRAVYMSGVANVRNPRLARSLRASLQQFANLELHEQTEVRGWLRDGDRVVGVATSRGEIRGDKVLLAAGAWSGELLKPLGLELPVVPVKGQMILYKCAADFLPRMVLAKGRYAIPRRDGHILIGSTLEHSGFDKTPTDEAQESLRASAAELLPELADMQPVAHWAGLRPGSPEGIPYIGPVPGFDGLWLNTGHYRNGLVLAPASCRLLADLMSGREPIIDPAPYAPAGRL

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: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:0043799 Catalysis of the reactions: (1) glycine + H2O + O2 = glyoxylate + NH4+ + H2O2; (2) D-alanine + H2O + O2 = pyruvate + NH4+ + H2O2; (3) sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2; (4) N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2.
  • GO:0009228 The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver.
  • GO:0009229 The chemical reactions and pathways resulting in the formation of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle.
  • GO:0016491 Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

Sequence Features

Domain/signature hits from InterPro and related databases.

16 records
Show feature table
Start End DB Term Name
17 24 Phobius SIGNAL_PEPTIDE_C_REGION C-terminal region of a signal peptide.
219 304 SUPERFAMILY SSF54373 FAD-linked reductases, C-terminal domain
4 345 Pfam PF01266 FAD dependent oxidoreductase
4 345 InterPro IPR006076 FAD dependent oxidoreductase
5 16 Phobius SIGNAL_PEPTIDE_H_REGION Hydrophobic region of a signal peptide.
25 364 Phobius NON_CYTOPLASMIC_DOMAIN Region of a membrane-bound protein predicted to be outside the membrane, in the extracellular region.
1 24 Phobius SIGNAL_PEPTIDE Signal peptide region
90 305 Gene3D G3DSA:3.30.9.10 -
3 356 PANTHER PTHR13847 SARCOSINE DEHYDROGENASE-RELATED
6 346 Gene3D G3DSA:3.50.50.60 -
6 346 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
1 4 Phobius SIGNAL_PEPTIDE_N_REGION N-terminal region of a signal peptide.
5 349 NCBIfam TIGR02352 glycine oxidase ThiO
5 349 InterPro IPR012727 Glycine oxidase ThiO
4 360 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
4 360 InterPro IPR036188 FAD/NAD(P)-binding 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 PA4548
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 0.687

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.

60 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
16A
5HXW
Q9LCB2 284.6 Da LogP 6.17 TPSA 0.0 1 viol. ✓ Clean CCCCCCCCCCCCCCCC[N+](C)(C)C
AAC
1NG3
O31616 117.1 Da LogP -0.79 TPSA 66.4 ✓ Ro5 ✓ Clean CC(=O)NCC(=O)O
B6X
6J39
X5IYZ1 248.3 Da LogP 2.62 TPSA 74.6 ✓ Ro5 ✓ Clean CCCCCC[C@H](CC(=O)O)SCC(=O)O
BE2
5FJN
A0A158RFS7 137.1 Da LogP 0.97 TPSA 63.3 ✓ Ro5 ✓ Clean c1ccc(c(c1)C(=O)O)N
DMG
1VRQ
Q50LF2 103.1 Da LogP -0.37 TPSA 40.5 ✓ Ro5 ✓ Clean CN(C)CC(=O)O
FON
1VRQ
Q50LF2 473.4 Da LogP -0.73 TPSA 219.8 1 viol. ✓ Clean c1cc(ccc1C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC[C@@H]2…
GOA
1RYI
O31616 76.1 Da LogP -0.94 TPSA 57.5 ✓ Ro5 ✓ Clean C(C(=O)O)O
MTG
3AD7
Q50LF2 105.1 Da LogP -0.90 TPSA 40.1 ✓ Ro5 ✓ Clean CSCC(=O)[O-]
PEO
1NG4
O31616 34.0 Da LogP 0.02 TPSA 40.5 ✓ Ro5 ✓ Clean OO
PYC
3AD8
Q50LF2 110.1 Da LogP -0.62 TPSA 55.9 ✓ Ro5 ✓ Clean c1cc([nH]c1)C(=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.