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 | Sulfurtransferase |
Enzyme Information
| 2.8.1.2 |
3-mercaptopyruvate sulfurtransferase.
based on mapping to UniProt P31142
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin.
-!- The enzyme catalyzes a transsulfuration reaction from 3-mercaptopyruvate to an internal cysteine residue. -!- In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. -!- The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
|
UniProtKB Entries (1)
| P31142 |
THTM_ECOLI
Escherichia coli K-12
3-mercaptopyruvate sulfurtransferase
|
PDB Structure
| PDB | 1URH |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The "Rhodanese" Fold and Catalytic Mechanism of 3-Mercaptopyruvate Sulfurtransferases: Crystal Structure of Ssea from Escherichia Coli
J.Mol.Biol.
|
