CATH Classification

Domain Context

CATH Clusters

Superfamily Type I PLP-dependent aspartate aminotransferase-like (Major domain)
Functional Family Cysteine desulfurase CsdA

Enzyme Information

4.4.1.-
Carbon-sulfur lyases.
based on mapping to UniProt Q46925
4.4.1.16
Selenocysteine lyase.
based on mapping to UniProt Q46925
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
-!- Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. -!- The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).
2.8.1.7
Cysteine desulfurase.
based on mapping to UniProt Q46925
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)

P0AGF2
CSDE_ECOLI
Escherichia coli K-12
Sulfur acceptor protein CsdE

PDB Structure

PDB 5FT8
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Mechanism of Sulfur Transfer Across Protein-Protein Interfaces: The Cysteine Desulfurase Model System
Fernandez, F.J., Arda, A., Lopez-Estepa, M., Aranda, J., Penya-Soler, E., Garces, F., Quintana, J.F., Round, A., Campos-Oliva, R., Bruix, M., Coll, M., Tunon, I., Jimenez-Barbero, J., Vega, M.C.
Acs Catalysis