CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.176 | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
|
3.90.176.10 | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
| Functional Family |
Enzyme Information
| 2.4.2.31 |
NAD(+)--protein-arginine ADP-ribosyltransferase.
based on mapping to UniProt P21454
NAD(+) + protein-L-arginine = nicotinamide + N(omega)-(ADP-D-ribosyl)- protein-L-arginine.
-!- Arginine residues in proteins act as acceptors. -!- Free arginine, agmatine ((4-aminobutyl)guanidine), arginine methyl ester and guanidine can also do so. -!- The enzyme from some, but not all, species can also use NADP(+) as acceptor (giving rise to N(omega)-((2'-phospho-ADP)-D-ribosyl)- protein-L-arginine as the product), but more slowly. -!- Catalyzes the NAD(+)-dependent activation of EC 4.6.1.1. -!- Some bacterial enterotoxins possess similar enzymatic activities (cf. EC 2.4.2.36).
|
UniProtKB Entries (1)
| P21454 |
SPVB_SALTM
Salmonella enterica subsp. enterica serovar Typhimurium
Mono(ADP-ribosyl)transferase SpvB
|
PDB Structure
| PDB | 2GWM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A steric antagonism of actin polymerization by a salmonella virulence protein.
Structure
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