Protein profile

VK055_3124

UDP-N-acetylenolpyruvoylglucosamine reductase

Genome: KpATCC43816

Gene: AIK81701.1 murB Structure source: AlphaFold + ColabFold UniProt A0A0H3GPZ2
Export view
Amino acids 342
Annotations 9
Features 23
PDB binders 4
Druggability 0.027

Overview

Basic information about this protein and its source genome.

Accession
VK055_3124
Assembly
Klebsiella pneumoniae subsp. pneumoniae strain ATCC 43816 KPPR1, complete genome
Gene
AIK81701.1 murB
Status
annotated
Amino acids
342
Structure source
AlphaFold + ColabFold
EC
1.3.1.98
GO
GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. GO:0008762 Catalysis of the reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+. 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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Human identity (%)
0.0
Gut microbiome off-target
hit
Essential (DEG)
Y
DEG identity (%)
78.947
DEG E-value
0.0
Localization
CytoplasmicMembrane
ColabFold pLDDT
97.62

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 0.027
Structure A0A0H3GPZ2
Pocket Pocket 14
P2Rank 0.977
Structure A0A0H3GPZ2
Pocket Pocket 1
ColabFold model
FPocket 0.905 · Pocket 8
P2Rank 0.979 · Pocket 1
Core conservation Conserved core gene
Roary core
CoreCruncher core
Gut microbiome 132 / 4744 genomes with a hit
Normalized 0.028

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

1 EC 8 GO

Enzyme Commission (EC)

1

Gene Ontology (GO)

8
  • GO:0071949 Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
  • GO:0008762 Catalysis of the reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+.
  • 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:0005829 The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
  • GO:0051301 The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
  • GO:0071555 A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis.
  • 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:0008360 Any process that modulates the surface configuration of a cell.

Sequence Features

Domain/signature hits from InterPro and related databases.

23 records
Show feature table
Start End DB Term Name
69 218 FunFam G3DSA:3.30.465.10:FF:000018 UDP-N-acetylenolpyruvoylglucosamine reductase
69 218 Gene3D G3DSA:3.30.465.10 -
69 218 InterPro IPR016169 FAD-binding, type PCMH, subdomain 2
5 330 NCBIfam TIGR00179 UDP-N-acetylmuramate dehydrogenase
5 330 InterPro IPR003170 UDP-N-acetylenolpyruvoylglucosamine reductase
3 197 SUPERFAMILY SSF56176 FAD-binding/transporter-associated domain-like
3 197 InterPro IPR036318 FAD-binding, type PCMH-like superfamily
19 148 Pfam PF01565 FAD binding domain
19 148 InterPro IPR006094 FAD linked oxidase, N-terminal
13 183 ProSiteProfiles PS51387 PCMH-type FAD-binding domain profile.
13 183 InterPro IPR016166 FAD-binding domain, PCMH-type
1 68 Gene3D G3DSA:3.30.43.10 -
1 68 InterPro IPR016167 FAD-binding, type PCMH, subdomain 1
219 342 Gene3D G3DSA:3.90.78.10 -
219 342 InterPro IPR036635 UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain superfamily
1 342 Hamap MF_00037 UDP-N-acetylenolpyruvoylglucosamine reductase [murB].
1 342 InterPro IPR003170 UDP-N-acetylenolpyruvoylglucosamine reductase
202 339 SUPERFAMILY SSF56194 Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain
202 339 InterPro IPR036635 UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain superfamily
206 329 Pfam PF02873 UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain
206 329 InterPro IPR011601 UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal
2 329 PANTHER PTHR21071 UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE
2 329 InterPro IPR003170 UDP-N-acetylenolpyruvoylglucosamine reductase

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

Loading 3D structure...

Legend High Medium Low

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_A0A0H3GPZ2
AlphaFold — — full sequence — Viewing
ColabFold VK055_3124
ColabFold — — full sequence — Loaded
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer

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 20.4 0.854
2 8.88 0.476
3 2.95 0.095
4 1.73 0.031

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.

39 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
973
2Q85
P08373 348.8 Da LogP 5.36 TPSA 46.5 1 viol. ✓ Clean c1ccc2c(c1)cccc2\C=C/3\C(=C(C(=O)O3)c4ccc(cc4)C…
B3P
4JAY
Q9HZM7 282.3 Da LogP -4.01 TPSA 145.4 1 viol. ✓ Clean C(CNC(CO)(CO)CO)CNC(CO)(CO)CO
EEB
1MBB
P08373 693.4 Da LogP -3.76 TPSA 332.2 3 viol. ✓ Clean CCC(C(=O)O)O[C@@H]1[C@H]([C@H](O[C@@H]([C@H]1O)…
EPU
1UXY
P08373 677.4 Da LogP -4.03 TPSA 332.2 3 viol. ✓ Clean CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1O[P@@]…

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.