Function and Biology Details
Reaction catalysed:
(1a) [enzyme]-L-histidine + 2,3-bisphospho-D-glycerate = [enzyme]-N(tau)-phospho-L-histidine + 2/3-phospho-D-glycerate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-174692 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Molecule details ›
Chain: A
Length: 257 amino acids
Theoretical weight: 28.96 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
Length: 257 amino acids
Theoretical weight: 28.96 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
- Canonical:
Q3JWH7 (Residues: 1-249; Coverage: 100%)
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
Molecule details ›
Chain: B
Length: 257 amino acids
Theoretical weight: 29.04 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
Length: 257 amino acids
Theoretical weight: 29.04 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
- Canonical: Q3JWH7 (Residues: 1-249; Coverage: 100%)
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like
