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 | Cysteine desulfurase IscS |
Enzyme Information
| 2.8.1.7 |
Cysteine desulfurase.
based on mapping to UniProt Q9Y697
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 (2)
| P0A6A8 |
ACP_ECOLI
Escherichia coli K-12
Acyl carrier protein
|
| Q9Y697 |
NFS1_HUMAN
Homo sapiens
Cysteine desulfurase, mitochondrial
|
PDB Structure
| PDB | 5USR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.
Proc. Natl. Acad. Sci. U.S.A.
|
