CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1170 | Aldehyde Oxidoreductase; domain 3 |
|
3.90.1170.20 | Quinolinate phosphoribosyl transferase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Quinolinate phosphoribosyl transferase, N-terminal domain |
| Functional Family |
Enzyme Information
| 2.4.2.19 |
Nicotinate-nucleotide diphosphorylase (carboxylating).
based on mapping to UniProt P9WJJ7
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)
| P9WJJ7 |
NADC_MYCTU
Mycobacterium tuberculosis H37Rv
Nicotinate-nucleotide pyrophosphorylase [carboxylating]
|
PDB Structure
| PDB | 1QPN |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of quinolinic acid phosphoribosyltransferase from Mycobacterium tuberculosis: a potential TB drug target.
Structure
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