CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
| Superfamily | Aldolase class I |
| Functional Family | Nicotinate-nucleotide pyrophosphorylase, carboxylating |
Enzyme Information
| 2.4.2.19 |
Nicotinate-nucleotide diphosphorylase (carboxylating).
based on mapping to UniProt P30012
Beta-nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3- dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate.
-!- The reaction is catalyzed in the opposite direction. -!- Since quinolinate is synthesized from L-tryptophan in eukaryotes, but from L-aspartate in some prokaryotes, this is the first NAD(+) biosynthesis enzyme shared by both eukaryotes and prokaryotes.
|
UniProtKB Entries (1)
| P30012 |
NADC_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Nicotinate-nucleotide pyrophosphorylase [carboxylating]
|
PDB Structure
| PDB | 1QAP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.
Structure
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