Detail Information for IndEnz0007000030
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