Target Pathogen

Overview

Basic information about this protein and its source genome.

Accession: PA3025
Assembly: Pseudomonas aeruginosa PAO1, complete genome
Gene: PA3025
Status: annotated
Amino acids: 526
Structure source: AlphaFold

GO

GO:0004368 Catalysis of the reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol. GO:0006071 The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids. GO:0046168 The chemical reactions and pathways resulting in the breakdown of glycerol-3-phosphate, a phosphoric monoester of glycerol. GO:0006072 The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol. 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. GO:0009331 An enzyme complex that catalyzes the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate, with concurrent reduction of flavin adenine dinucleotide (FAD) to FADH2. In E. coli, the complex is either a GlpA-GlpB-GlpC heterotrimer that functions in anaerobic conditions, or a GlpD homodimer that functions in aerobic conditions.

Target profile

Computed evidence for target prioritization.

Human off-target: hit
Human identity (%): 31.615
Human E-value: 1.27e-40
Gut microbiome off-target: hit
Essential (DEG): N
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 0.595

Structure –

Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

6 GO

Gene Ontology (GO)

6

GO:0004368 Catalysis of the reaction: sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
GO:0006071 The chemical reactions and pathways involving glycerol, 1,2,3-propanetriol, a sweet, hygroscopic, viscous liquid, widely distributed in nature as a constituent of many lipids.
GO:0046168 The chemical reactions and pathways resulting in the breakdown of glycerol-3-phosphate, a phosphoric monoester of glycerol.
GO:0006072 The chemical reactions and pathways involving glycerol-3-phosphate, a phosphoric monoester of glycerol.
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.
GO:0009331 An enzyme complex that catalyzes the oxidation of sn-glycerol 3-phosphate to dihydroxyacetone phosphate, with concurrent reduction of flavin adenine dinucleotide (FAD) to FADH2. In E. coli, the complex is either a GlpA-GlpB-GlpC heterotrimer that functions in anaerobic conditions, or a GlpD homodimer that functions in aerobic conditions.

Sequence Features

Domain/signature hits from InterPro and related databases.

25 records

Show feature table

Start	End	DB	Term	Name
412	523	Gene3D	G3DSA:1.10.8.870	-
412	523	InterPro	IPR038299	Alpha-glycerophosphate oxidase, C-terminal domain superfamily
10	519	PANTHER	PTHR11985	GLYCEROL-3-PHOSPHATE DEHYDROGENASE
10	519	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
334	340	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
334	340	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
51	63	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
51	63	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
96	108	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
96	108	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
365	377	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
365	377	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
35	45	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
35	45	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
22	34	PRINTS	PR01001	FAD-dependent glycerol-3-phosphate dehydrogenase family signature
22	34	InterPro	IPR000447	FAD-dependent glycerol-3-phosphate dehydrogenase
414	505	Pfam	PF16901	C-terminal domain of alpha-glycerophosphate oxidase
414	505	InterPro	IPR031656	Alpha-glycerophosphate oxidase, C-terminal
22	345	SUPERFAMILY	SSF51905	FAD/NAD(P)-binding domain
22	345	InterPro	IPR036188	FAD/NAD(P)-binding domain superfamily
104	341	Gene3D	G3DSA:3.30.9.10	-
23	344	Pfam	PF01266	FAD dependent oxidoreductase
23	344	InterPro	IPR006076	FAD dependent oxidoreductase
20	377	Gene3D	G3DSA:3.50.50.60	-
20	377	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 PA3025	AlphaFold	—	—	full sequence	—	Viewing

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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
2				0.595
1				0.297

PA3025