Protein profile

PA4749

phosphoglucosamine mutase

Genome: NC_002516.2

Gene: PA4749 glmM Structure source: AlphaFold UniProt Q9HV50
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Amino acids 445
Annotations 11
Features 38
PDB binders 2
Druggability 0.615

Overview

Basic information about this protein and its source genome.

Accession
PA4749
Assembly
Pseudomonas aeruginosa PAO1, complete genome
Gene
PA4749 glmM
Status
annotated
Amino acids
445
Structure source
AlphaFold
EC
5.4.2.10
GO
GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0000287 Binding to a magnesium (Mg) ion. GO:0004614 Catalysis of the reaction: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. GO:0008966 Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. GO:0004615 Catalysis of the reaction: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate. GO:0005975 The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
25.868
Human E-value
7.42e-08
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 0.615
Structure –
Pocket –

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 10 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

10
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0004614 Catalysis of the reaction: alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
  • GO:0008966 Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate.
  • GO:0004615 Catalysis of the reaction: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
  • 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:0009252 The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls and consisting of long glycan strands of alternating residues of beta-(1,4) linked N-acetylglucosamine and N-acetylmuramic acid, cross-linked by short peptides.
  • GO:0006048 The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
  • GO:0016868 Catalysis of the transfer of a phosphate group from one position to another within a single molecule.
  • GO:0071704 OBSOLETE. The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records
Show feature table
Start End DB Term Name
155 256 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
155 256 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
172 274 FunFam G3DSA:3.40.120.10:FF:000003 Phosphoglucosamine mutase
369 443 Gene3D G3DSA:3.30.310.50 -
2 153 Gene3D G3DSA:3.40.120.10 -
95 104 ProSitePatterns PS00710 Phosphoglucomutase and phosphomannomutase phosphoserine signature.
95 104 InterPro IPR016066 Alpha-D-phosphohexomutase, conserved site
256 338 Gene3D G3DSA:3.40.120.10 -
372 440 Pfam PF00408 Phosphoglucomutase/phosphomannomutase, C-terminal domain
372 440 InterPro IPR005843 Alpha-D-phosphohexomutase, C-terminal
369 444 FunFam G3DSA:3.30.310.50:FF:000001 Phosphoglucosamine mutase
6 441 NCBIfam TIGR01455 phosphoglucosamine mutase
6 441 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
173 192 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
173 192 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
94 108 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
94 108 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
233 248 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
233 248 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
2 444 PANTHER PTHR42946 PHOSPHOHEXOSE MUTASE
257 362 Pfam PF02880 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III
257 362 InterPro IPR005846 Alpha-D-phosphohexomutase, alpha/beta/alpha domain III
173 360 Gene3D G3DSA:3.40.120.10 -
357 444 SUPERFAMILY SSF55957 Phosphoglucomutase, C-terminal domain
357 444 InterPro IPR036900 Alpha-D-phosphohexomutase, C-terminal domain superfamily
156 253 Pfam PF02879 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II
156 253 InterPro IPR005845 Alpha-D-phosphohexomutase, alpha/beta/alpha domain II
2 443 Hamap MF_01554_B Phosphoglucosamine mutase [glmM].
2 443 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
2 180 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
2 180 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
5 437 CDD cd05802 GlmM
5 437 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
3 134 Pfam PF02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I
3 134 InterPro IPR005844 Alpha-D-phosphohexomutase, alpha/beta/alpha domain I
2 153 FunFam G3DSA:3.40.120.10:FF:000001 Phosphoglucosamine mutase
257 363 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
257 363 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III

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 PA4749
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 0.615
4 0.547
6 0.356
8 0.333

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.

23 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
BTB
3NA5
Q8ZQW9 209.2 Da LogP -3.01 TPSA 104.4 ✓ Ro5 ✓ Clean C(CO)N(CCO)C(CO)(CO)CO
TLA
1K2Y
P26276 150.1 Da LogP -2.12 TPSA 115.1 ✓ Ro5 ✓ Clean [C@@H]([C@H](C(=O)O)O)(C(=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.