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-172241 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Molecule details ›
Chains: A, B, C, D, E, F
Length: 301 amino acids
Theoretical weight: 31.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 301 amino acids
Theoretical weight: 31.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15274 (Residues: 1-297; Coverage: 100%)
Sequence domains:
- Quinolinate phosphoribosyl transferase, N-terminal domain
- Quinolinate phosphoribosyl transferase, C-terminal domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL7-1
Spacegroup:
P3221
Expression system: Escherichia coli
