Protein profile

PA3584

glycerol-3-phosphate dehydrogenase

Genome: NC_002516.2

Gene: PA3584 glpD Structure source: AlphaFold UniProt P52111
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Amino acids 512
Annotations 8
Features 30
PDB binders 0
Druggability 0.666

Overview

Basic information about this protein and its source genome.

Accession
PA3584
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA3584 glpD
Status
annotated
Amino acids
512
Structure source
AlphaFold
EC
1.1.5.3
GO
GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. 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.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
31.875
Human E-value
1.8500000000000002e-29
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 0.666
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

MSQAHTPSAPLAEVYDVAVVGGGINGVGIAADAAGRGLSVFLCEQHDLAQHTSSASSKLIHGGLRYLEHYEFRLVREALAEREVLLAKAPHIVKPLRFVLPHRPHLRPAWMIRAGLFLYDHLGKREKLPASRGLRFTGSSPLKAEIRRGFEYSDCAVDDARLVVLNAISAREHGAHVHTRTRCVSARRSKGLWHLHLERSDGSLYSIRARALVNAAGPWVARFIQDDLKQKSPYGIRLIQGSHIIVPKLYEGEHAYILQNEDRRIVFAIPYLDRFTMIGTTDREYQGDPAKVAISEEETAYLLQVVNAHFKQQLAAADILHSFAGVRPLCDDESDEPSAITRDYTLSLSAGNGEPPLLSVFGGKLTTYRKLAESALTQLQPFFANLGPAWTAKAPLPGGEQMQSVEALTEQLANRYAWLDRELALRWARTYGTRVWRLLDGVNGEADLGEHLGGGLYAREVDYLCKHEWAQDAEDILWRRSKLGLFLSPSQQVRLGQYLQSEHPHRPRVHAA

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 7 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

7
  • GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
  • 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.

30 records
Show feature table
Start End DB Term Name
391 486 Pfam PF16901 C-terminal domain of alpha-glycerophosphate oxidase
391 486 InterPro IPR031656 Alpha-glycerophosphate oxidase, C-terminal
20 37 ProSitePatterns PS00977 FAD-dependent glycerol-3-phosphate dehydrogenase signature 1.
20 37 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
110 330 Gene3D G3DSA:3.30.9.10 -
16 369 Pfam PF01266 FAD dependent oxidoreductase
16 369 InterPro IPR006076 FAD dependent oxidoreductase
401 471 FunFam G3DSA:1.10.8.870:FF:000002 Glycerol-3-phosphate dehydrogenase
8 486 PANTHER PTHR11985 GLYCEROL-3-PHOSPHATE DEHYDROGENASE
8 486 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
402 471 Gene3D G3DSA:1.10.8.870 -
402 471 InterPro IPR038299 Alpha-glycerophosphate oxidase, C-terminal domain superfamily
362 372 ProSitePatterns PS00978 FAD-dependent glycerol-3-phosphate dehydrogenase signature 2.
44 56 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
44 56 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
357 369 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
357 369 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
89 101 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
89 101 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
323 329 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
323 329 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
15 27 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
15 27 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
28 38 PRINTS PR01001 FAD-dependent glycerol-3-phosphate dehydrogenase family signature
28 38 InterPro IPR000447 FAD-dependent glycerol-3-phosphate dehydrogenase
15 398 Gene3D G3DSA:3.50.50.60 -
15 398 InterPro IPR036188 FAD/NAD(P)-binding domain superfamily
472 509 Gene3D G3DSA:6.10.250.1890 -
15 306 SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain
15 306 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

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA3584
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 0.666
2 0.343