Cysteine desulfurase, SufS (IPR010970)

Short name: Cys_dSase_SufS

Overlapping homologous superfamilies

Family relationships


Cysteine desulfurases are pyridoxal-phosphate enzymes which catalyse the removal of sulphur from L-cysteine to form L-alanine and elemental sulphur. These enzymes have been shown to play an important role in the biosynthesis of iron-sulphur clusters, thionucleosides in tRNA, thiamine, biotin, lipoate and molydopterin [PMID: 12382038].

This entry represents a subfamily of NifS-related cysteine desulfurases that are often involved in iron-sulphur cluster formation, which is needed for nitrogen fixation and other vital functions [PMID: 11498000]. Many of these enzymes, in addition to cysteine desulfurase activity, also show selenocysteine lyase activity where L-selenocysteine is converted to L-alanine and selenide [PMID: 10329673]. Some of these enzymes are much more specific for selenocysteine than cysteine and are thus believed to function in selenium metabolism rather than sulphur metabolism.

Structural studies of the Escherichia coli [PMID: 11827487] and Synechocystis [PMID: 15379559] enzymes indicate that they are homodimers which show a similar fold to other members of the alpha family of pyridoxal-phosphate enzymes [PMID: 9914259].

GO terms

Biological Process

GO:0006534 cysteine metabolic process

Molecular Function

GO:0031071 cysteine desulfurase activity
GO:0030170 pyridoxal phosphate binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.