› 5z0a

X-ray diffraction
2.09Å resolution

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
Acetyl-CoA + alpha-D-galactosamine 1-phosphate = CoA + N-acetyl-alpha-D-galactosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188843 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional sugar-1-phosphate nucleotidylyltransferase/acetyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 409 amino acids
Theoretical weight: 45.6 KDa
Source organism: Sulfurisphaera tokodaii str. 7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q975F9 (Residues: 1-401; Coverage: 100%)
Gene names: ST0452, STK_04520
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P1
Unit cell:
a: 90.843Å b: 94.951Å c: 101.906Å
α: 110.62° β: 101.47° γ: 113.03°
R-values:
R R work R free
0.195 0.193 0.232
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

A Glycolipid Glycosyltransferase with Broad Substrate Specificity from the Marine Bacterium "Candidatus Pelagibacter sp." Strain HTCC7211.
Wei et al. (2021)

1 mention without citation

Improvement of ST0452 N-Acetylglucosamine-1-Phosphate Uridyltransferase Activity by the Cooperative Effect of Two Single Mutations Identified through Structure-Based Protein Engineering.
Honda et al. (2018)