CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

2.8.1.7
Cysteine desulfurase.
based on mapping to UniProt Q93WX6
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.
4.4.1.16
Selenocysteine lyase.
based on mapping to UniProt Q93WX6
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).

UniProtKB Entries (1)

Q93WX6
CNIF1_ARATH
Arabidopsis thaliana
Cysteine desulfurase 1, chloroplastic

PDB Structure

PDB 4Q76
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.
Roret, T., Pegeot, H., Couturier, J., Mulliert, G., Rouhier, N., Didierjean, C.
Acta Crystallogr F Struct Biol Commun