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 | NAD(P)(+)--arginine ADP-ribosyltransferase |
Enzyme Information
| 3.2.2.5 |
NAD(+) glycohydrolase.
based on mapping to UniProt P20974
NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
-!- This enzyme catalyzes the hydrolysis of NAD(+), without associated ADP-ribosyl cyclase activity (unlike the metazoan enzyme EC 3.2.2.6, bifunctional ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase). -!- The enzyme from Group A streptococci has been implicated in the pathogenesis of diseases such as streptococcal toxic shock-like syndrome (STSS) and necrotizing fasciitis. -!- The enzyme from the venom of the snake Agkistrodon acutus also catalyzes EC 3.6.1.5.
|
| 2.4.2.31 |
NAD(+)--protein-arginine ADP-ribosyltransferase.
based on mapping to UniProt P20974
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)
| P20974 |
NAR2B_RAT
Rattus norvegicus
T-cell ecto-ADP-ribosyltransferase 2
|
PDB Structure
| PDB | 1GXZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of the Ecto-Adp-Ribosyl Transferase Art2.2 From Rat
J.Mol.Biol.
|
