Detail Information for IndEnz0018000216
IED ID IndEnz0018000216
Enzyme Type ID peroxidase000216
Protein Name Alkyl hydroperoxide reductase C
EC 1.11.1.28
Peroxiredoxin
Thioredoxin peroxidase
Gene Name MSMEG_4891 MSMEI_4766
Organism Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium smegmatis (Mycobacterium smegmatis) Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Enzyme Sequence MALLTIGDQFPEYDLTAVVGGDLSKVDAKQPDDYFTRVTSKDYEGKWRIIFFWPKDFTFVCPTEIAAFGKLNEDFEDRDAKVLGVSVDNEFVHFQWRAQHEDLKTLPFPMVSDLKRELTAACGVLNADGVADRATFIVDPNNEVQFVSVTAGSVGRNVDEVLRVLDALQSDELCACNWKKGDPTINAGELLAGAV
Enzyme Length 195
Uniprot Accession Number A0R1V9
Absorption
Active Site ACT_SITE 61; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:P9WQB7
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an alcohol + H2O; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502, Rhea:RHEA-COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.11.1.28; Evidence={ECO:0000250|UniProtKB:P9WQB7};
DNA Binding
EC Number 1.11.1.28
Enzyme Function FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Together with AhpD, DlaT and Lpd, constitutes an NADH-dependent peroxidase active against hydrogen and alkyl peroxides as well as serving as a peroxynitrite reductase, thus protecting the bacterium against reactive nitrogen intermediates and oxidative stress generated by the host immune system. Does not however seem to play a role in detoxification of isoniazid. {ECO:0000250|UniProtKB:P9WQB7}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Cross-link (1); Disulfide bond (3); Domain (1)
Keywords Antioxidant;Cytoplasm;Disulfide bond;Isopeptide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome;Stress response;Ubl conjugation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 21,626
Kinetics
Metal Binding
Rhea ID RHEA:62636
Cross Reference Brenda