IED ID | IndEnz0007000030 |
Enzyme Type ID | catalase000030 |
Protein Name |
Monothiol bacilliredoxin BrxC Monothiol Brx-C Bacillithiol system redox-active protein YtxJ ORF2 ORF3 |
Gene Name | brxC ytxJ BSU29760 HIR78_17325 |
Organism | Bacillus subtilis (strain 168) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
Enzyme Sequence | MAKQLIQSEEEFKRIAEQEGVFVFLKHSTTCPISQAAFHEFDAFANQHEDVPAYYLQVQEARPLSNFIAETYGVKHESPQIFIIQNGEVKWHTSHSQITEAAIEQHLS |
Enzyme Length | 108 |
Uniprot Accession Number | P39914 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a monothiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) GapA and GapB in vivo and probably a number of other oxidized cytosolic proteins. Debacillithiolates the S-bacillithiolated Bdr (Bdr-SSB) and BrxB (BrxB-SSB) in vitro. Involved in maintaining redox homeostasis in response to disulfide stress conditions. {ECO:0000269|PubMed:33722570}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Modified residue (1); Mutagenesis (1) |
Keywords | Oxidoreductase;Redox-active center;Reference proteome |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 31; /note=S-bacillithiol cysteine disulfide; /evidence=ECO:0000269|PubMed:33722570 |
Post Translational Modification | PTM: Cys can react with bacillithiol (BSH) to form mixed disulfides. S-bacillithiolation protects Cys residues against overoxidation by acting as a redox switch in response to oxidative stress. {ECO:0000269|PubMed:33722570}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 33722570; |
Motif | |
Gene Encoded By | |
Mass | 12,402 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |