Function and Biology Details
Reaction catalysed:
1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- ATP phosphoribosyltransferase, catalytic domain
- ATP phosphoribosyltransferase HisG, short form
- Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit
- ATP phosphoribosyltransferase, conserved site
- ATP phosphoribosyltransferase HisG
- Aminoacyl-tRNA synthetase, class II
1 more domain
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-169674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ATP phosphoribosyltransferase regulatory subunit
Molecule details ›
Chains: A, B, C, D
Length: 344 amino acids
Theoretical weight: 39.85 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
Sequence domains: Histidyl-tRNA synthetase
Structure domains: Bira Bifunctional Protein; Domain 2
Length: 344 amino acids
Theoretical weight: 39.85 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
- Canonical:
Q02147 (Residues: 1-328; Coverage: 100%)
Sequence domains: Histidyl-tRNA synthetase
Structure domains: Bira Bifunctional Protein; Domain 2
ATP phosphoribosyltransferase
Molecule details ›
Chains: E, F, G, H
Length: 208 amino acids
Theoretical weight: 23.71 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
Sequence domains: ATP phosphoribosyltransferase
Structure domains: Periplasmic binding protein-like II
Length: 208 amino acids
Theoretical weight: 23.71 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
- Canonical: Q02129 (Residues: 1-208; Coverage: 100%)
Sequence domains: ATP phosphoribosyltransferase
Structure domains: Periplasmic binding protein-like II
