CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1150 | Aspartate Aminotransferase, domain 1 |
|
3.90.1150.10 | Aspartate Aminotransferase, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 |
| Functional Family |
Enzyme Information
| 2.8.1.7 |
Cysteine desulfurase.
based on mapping to UniProt Q55793
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
-!- The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. -!- The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin). -!- In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
|
UniProtKB Entries (1)
| Q55793 |
CSD_SYNY3
Synechocystis sp. PCC 6803 substr. Kazusa
Probable cysteine desulfurase
|
PDB Structure
| PDB | 1T3I |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803.
Biochemistry
|