CATH Domain 1i29A02

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.640	Aspartate Aminotransferase; domain 2
	3.40.640.10	Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Domain Context

CATH Clusters

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

Enzyme Information

2.8.1.7

Cysteine desulfurase.

based on mapping to UniProt P77444

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 P77444

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)

P77444

SUFS_ECOLI

Escherichia coli K-12

Cysteine desulfurase

PDB Structure

PDB	1I29
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine. Mihara, H., Fujii, T., Kato, S., Kurihara, T., Hata, Y., Esaki, N. J.BIOCHEM.(TOKYO)