CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.140 | Metal-dependent hydrolases |
Domain Context
CATH Clusters
| Superfamily | Metal-dependent hydrolases |
| Functional Family | 5-methylthioadenosine/S-adenosylhomocysteine deaminase |
Enzyme Information
| 3.5.4.28 |
S-adenosylhomocysteine deaminase.
based on mapping to UniProt Q9X034
S-adenosyl-L-homocysteine + H(2)O = S-inosyl-L-homocysteine + NH(3).
|
| 3.5.4.31 |
S-methyl-5'-thioadenosine deaminase.
based on mapping to UniProt Q9X034
S-methyl-5'-thioadenosine + H(2)O = S-methyl-5'-thioinosine + NH(3).
-!- The enzyme from Thermotoga maritima also functions as S-adenosylhomocysteine deaminase (EC 3.5.4.28) and has some activity against adenosine. -!- Adenosine-5-monophosphate (AMP) and S-adenosyl-L-methionine (SAM) are not substrates. -!- Formerly EC 3.5.4.n1.
|
UniProtKB Entries (1)
| Q9X034 |
MTAD_THEMA
Thermotoga maritima MSB8
5-methylthioadenosine/S-adenosylhomocysteine deaminase
|
PDB Structure
| PDB | 1P1M |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the hypothetical protein TM0936 from Thermotoga maritima at
1.5A bound to Ni and methionine
To be Published
|
