CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.20 | Up-down Bundle | |
1.20.82 | ADP Ribosyl Cyclase; Chain A, domain 1 | |
1.20.82.10 | ADP Ribosyl Cyclase; Chain A, domain 1 |
Domain Context
CATH Clusters
Superfamily | ADP Ribosyl Cyclase; Chain A, domain 1 |
Functional Family | ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 |
Enzyme Information
3.2.2.6 |
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
based on mapping to UniProt P28907
NAD(+) + H(2)O = ADP-D-ribose + nicotinamide.
-!- This multiunctional enzyme catalyzes both the synthesis and hydrolysis of cyclic ADP-ribose, a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 2.4.99.20. -!- It is also able to act on beta-nicotinamide D-ribonucleotide. -!- Cf. EC 3.2.2.5.
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2.4.99.20 |
2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase.
based on mapping to UniProt P28907
NADP(+) + nicotinate = nicotinate-adenine dinucleotide phosphate + nicotinamide.
-!- This multiunctional enzyme catalyzes both the removal of nicotinamide from NADP(+), forming 2'-phospho-cyclic ADP-ribose, and the addition of nicotinate to the cyclic product, forming NAADP(+), a calcium messenger that can mobilize intracellular Ca(2+) stores and activate Ca(2+) influx to regulate a wide range of physiological processes. -!- In addition, the enzyme also catalyzes EC 3.2.2.6.
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UniProtKB Entries (1)
P28907 |
CD38_HUMAN
Homo sapiens
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
|
PDB Structure
PDB | 2EF1 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structure of the extracellular domain of human CD38
To be Published
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