| UniProt functional annotation for O32164 | |||
| UniProt code: O32164. |
| Organism: | Bacillus subtilis (strain 168). | |
| Taxonomy: | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus. | |
| Function: | Enzyme able to deliver sulfur to partners involved in Fe-S cluster assembly. Catalyzes the removal of elemental sulfur atoms from L-cysteine to produce L-alanine. Activity is stimulated 40- to 100-fold by SufU, which acts as a second substrate for this enzyme following release of Ala, and generating SufU.S. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity. {ECO:0000269|PubMed:20097860, ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21744456}. | |
| Catalytic activity: | Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L- alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA- COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:20822158}; | |
| Cofactor: | Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250}; | |
| Activity regulation: | A Cys to Ala mutation in SufU (Cys-41-Ala) has been described to be a competivie inhibitor of SufS activity and a non- competitive inhibitor (PubMed:21236255, PubMed:24321018). {ECO:0000269|PubMed:21236255, ECO:0000269|PubMed:24321018}. | |
| Biophysicochemical properties: | Kinetic parameters: KM=86 uM for L-cysteine {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; KM=30 uM for SufU {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; Vmax=1157 nmol/min/mg enzyme in the presence of SufU {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}; Note=In the presence of dithiothreitol, which regenerates the second reaction product SufU.S.; | |
| Subunit: | Homodimer. Interacts with SufU; the complex is more stable in the presence of L-cysteine. An N-terminal His-tag destabilizes this interaction. {ECO:0000269|PubMed:20822158, ECO:0000269|PubMed:21236255}. | |
| Similarity: | Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.