Protein profile

KP13_01108

Phosphoglucosamine mutase

Genome: KpKP13

Gene: AHE42498.1 glmM Structure source: AlphaFold + ColabFold UniProt A0A0H3GW58
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Amino acids 445
Annotations 10
Features 38
PDB binders 2
Druggability 0.46

Overview

Basic information about this protein and its source genome.

Accession
KP13_01108
Assembly
Klebsiella pneumoniae subsp. pneumoniae Kp13, complete sequence
Gene
AHE42498.1 glmM
Status
annotated
Amino acids
445
Structure source
AlphaFold + ColabFold
EC
5.4.2.10
GO
GO:0008966 Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 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:0071704 OBSOLETE. The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon. GO:0000287 Binding to a magnesium (Mg) ion. GO:0016868 Catalysis of the transfer of a phosphate group from one position to another within a single molecule. GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

Target profile

Computed evidence for target prioritization.

Human off-target
hit
Human identity (%)
30.584
Human E-value
1.45e-08
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
92.584
DEG E-value
0.0
Localization
Cytoplasmic
ColabFold pLDDT
95.55

Selected Druggability evidence

AlphaFold / UniProt model

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 0.46
Structure A0A0H3GW58
Pocket Pocket 2
P2Rank 0.294
Structure A0A0H3GW58
Pocket Pocket 1
ColabFold model
FPocket 0.84 · Pocket 1
P2Rank 0.263 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 292 / 4744 genomes with a hit
Normalized 0.062

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 9 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

9
  • GO:0008966 Catalysis of the reaction: alpha-D-glucosamine 1-phosphate = D-glucosamine 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:0071704 OBSOLETE. The chemical reactions and pathways involving an organic substance, any molecular entity containing carbon.
  • GO:0000287 Binding to a magnesium (Mg) ion.
  • GO:0016868 Catalysis of the transfer of a phosphate group from one position to another within a single molecule.
  • GO:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0004615 Catalysis of the reaction: alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
  • 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.

Sequence Features

Domain/signature hits from InterPro and related databases.

38 records
Show feature table
Start End DB Term Name
156 256 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
156 256 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
3 154 FunFam G3DSA:3.40.120.10:FF:000001 Phosphoglucosamine mutase
258 365 Pfam PF02880 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III
258 365 InterPro IPR005846 Alpha-D-phosphohexomutase, alpha/beta/alpha domain III
370 445 Gene3D G3DSA:3.30.310.50 -
257 339 Gene3D G3DSA:3.40.120.10 -
6 439 CDD cd05802 GlmM
6 439 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
258 365 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
258 365 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
157 254 Pfam PF02879 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II
157 254 InterPro IPR005845 Alpha-D-phosphohexomutase, alpha/beta/alpha domain II
2 181 SUPERFAMILY SSF53738 Phosphoglucomutase, first 3 domains
2 181 InterPro IPR016055 Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/III
373 442 Pfam PF00408 Phosphoglucomutase/phosphomannomutase, C-terminal domain
373 442 InterPro IPR005843 Alpha-D-phosphohexomutase, C-terminal
173 273 FunFam G3DSA:3.40.120.10:FF:000003 Phosphoglucosamine mutase
4 136 Pfam PF02878 Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I
4 136 InterPro IPR005844 Alpha-D-phosphohexomutase, alpha/beta/alpha domain I
7 443 NCBIfam TIGR01455 phosphoglucosamine mutase
7 443 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
96 105 ProSitePatterns PS00710 Phosphoglucomutase and phosphomannomutase phosphoserine signature.
96 105 InterPro IPR016066 Alpha-D-phosphohexomutase, conserved site
3 444 PANTHER PTHR42946 PHOSPHOHEXOSE MUTASE
357 444 SUPERFAMILY SSF55957 Phosphoglucomutase, C-terminal domain
357 444 InterPro IPR036900 Alpha-D-phosphohexomutase, C-terminal domain superfamily
3 445 Hamap MF_01554_B Phosphoglucosamine mutase [glmM].
3 445 InterPro IPR006352 Phosphoglucosamine mutase, bacterial type
175 362 Gene3D G3DSA:3.40.120.10 -
174 193 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
174 193 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
95 109 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
95 109 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
234 249 PRINTS PR00509 Phosphoglucomutase/phosphomannomutase family signature
234 249 InterPro IPR005841 Alpha-D-phosphohexomutase superfamily
3 154 Gene3D G3DSA:3.40.120.10 -
370 445 FunFam G3DSA:3.30.310.50:FF:000001 Phosphoglucosamine mutase

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 + 2

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

Entry Method Resolution Chain Coverage Links Status
AlphaFold AF_A0A0H3GW58
AlphaFold — — full sequence — Viewing
ColabFold KP13_01108
ColabFold — — full sequence — Loaded
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
2 0.46
4 0.306

Pockets (P2RANK)

Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).

P2RANK Sticks Spheres Surfaces Score Probability Labels Zoom Positions
1 4.71 0.207
2 1.31 0.014

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.