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 |
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).
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UniProtKB Entries (1)
Q93WX6 |
CNIF1_ARATH
Arabidopsis thaliana
Cysteine desulfurase 1, chloroplastic
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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.
Acta Crystallogr F Struct Biol Commun
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