Function and Biology Details
Reaction catalysed:
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Nicotinate-nucleotide pyrophosphorylase
- Nicotinate-nucleotide pyrophosphorylase/Putative pyrophosphorylase ModD
- Aldolase-type TIM barrel
- Nicotinate phosphoribosyltransferase-like, C-terminal
- Quinolinate phosphoribosyl transferase, C-terminal
- Quinolinate phosphoribosyl transferase, N-terminal
- Quinolinate phosphoribosyl transferase, N-terminal domain superfamily
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]
Molecule details ›
Chains: A, B, C
Length: 273 amino acids
Theoretical weight: 30.85 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 273 amino acids
Theoretical weight: 30.85 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
- Canonical:
O25909 (Residues: 1-273; Coverage: 100%)
Sequence domains:
- Quinolinate phosphoribosyl transferase, N-terminal domain
- Quinolinate phosphoribosyl transferase, C-terminal domain
