CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.140 | nicotinate phosphoribosyltransferase |
|
3.20.140.10 | nicotinate phosphoribosyltransferase |
Domain Context
CATH Clusters
| Superfamily | nicotinate phosphoribosyltransferase |
| Functional Family | Nicotinate phosphoribosyltransferase |
Enzyme Information
| 6.3.4.21 |
Nicotinate phosphoribosyltransferase.
based on mapping to UniProt P39683
Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H(2)O = beta- nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.
-!- The enzyme, which is involved in pyridine nucleotide recycling, can form beta-nicotinate D-ribonucleotide and diphosphate from nicotinate and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) in the absence of ATP. -!- However, when ATP is available the enzyme is phosphorylated resulting in a much lower K(m) for nicotinate. -!- The phospho-enzyme is hydrolyzed during the transferase reaction, regenerating the low affinity form. -!- The presence of ATP shifts the products/substrates equilibrium from 0.67 to 1100. -!- Formerly EC 2.4.2.11.
|
UniProtKB Entries (1)
| P39683 |
NPT1_YEAST
Saccharomyces cerevisiae S288C
Nicotinate phosphoribosyltransferase
|
PDB Structure
| PDB | 1VLP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases.
Structure
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