CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.250 | Oxidized Rhodanese; domain 1 |
|
3.40.250.10 | Rhodanese-like domain |
Domain Context
CATH Clusters
| Superfamily | Rhodanese-like domain |
| Functional Family | Adenylyltransferase and sulfurtransferase MOCS3 |
Enzyme Information
| 2.8.1.11 |
Molybdopterin synthase sulfurtransferase.
based on mapping to UniProt O95396
[Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine + reduced acceptor = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + [cysteine desulfurase] + oxidized acceptor.
-!- The enzyme transfers sulfur to form a thiocarboxylate moiety on the C-terminal glycine of the small subunit of EC 2.8.1.12. -!- In the human, the reaction is catalyzed by the rhodanese-like C-terminal domain (cf. EC 2.8.1.1) of the MOCS3 protein, a bifunctional protein that also contains EC 2.7.7.80 at the N-terminal domain. -!- Formerly EC 2.8.1.n1.
|
| 2.7.7.80 |
Molybdopterin-synthase adenylyltransferase.
based on mapping to UniProt O95396
ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly- Gly-AMP.
-!- Adenylates the C-terminus of the small subunit of the molybdopterin synthase. -!- This activation is required to form the thiocarboxylated C-terminus of the active molybdopterin synthase small subunit. -!- The reaction occurs in prokaryotes and eukaryotes. -!- In the human, the reaction is catalyzed by the N-terminal domain of the protein MOCS3, which also includes a molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) C-terminal domain. -!- Formerly EC 2.7.7.n4.
|
UniProtKB Entries (1)
| O95396 |
MOCS3_HUMAN
Homo sapiens
Adenylyltransferase and sulfurtransferase MOCS3
|
PDB Structure
| PDB | 3I2V |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the human MOCS3 rhodanese-like domain
To be Published
|