| IED ID | IndEnz0018000116 |
| Enzyme Type ID | peroxidase000116 |
| Protein Name |
Alkyl hydroperoxide reductase AhpD EC 1.11.1.28 Alkylhydroperoxidase AhpD |
| Gene Name | ahpD Rv2429 MTCY428.17c |
| Organism | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Enzyme Sequence | MSIEKLKAALPEYAKDIKLNLSSITRSSVLDQEQLWGTLLASAAATRNPQVLADIGAEATDHLSAAARHAALGAAAIMGMNNVFYRGRGFLEGRYDDLRPGLRMNIIANPGIPKANFELWSFAVSAINGCSHCLVAHEHTLRTVGVDREAIFEALKAAAIVSGVAQALATIEALSPS |
| Enzyme Length | 177 |
| Uniprot Accession Number | P9WQB5 |
| Absorption | |
| Active Site | ACT_SITE 130; /note="Proton donor"; /evidence="ECO:0000255|HAMAP-Rule:MF_01676, ECO:0000269|PubMed:11914371"; ACT_SITE 133; /note="Cysteine sulfenic acid (-SOH) intermediate"; /evidence="ECO:0000255|HAMAP-Rule:MF_01676, ECO:0000269|PubMed:11914371" |
| 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:0000255|HAMAP-Rule:MF_01676}; |
| DNA Binding | |
| EC Number | 1.11.1.28 |
| Enzyme Function | FUNCTION: Antioxidant protein with alkyl hydroperoxidase activity. Required for the reduction of the AhpC active site cysteine residues and for the regeneration of the AhpC enzyme activity.; FUNCTION: Together with AhpC, 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. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:12761216}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (1); Chain (1); Disulfide bond (2); Helix (10); Mutagenesis (7); Turn (2) |
| Keywords | 3D-structure;Antioxidant;Disulfide bond;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1GU9; 1KNC; 1LW1; 1ME5; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 18,781 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62636 |
| Cross Reference Brenda | 1.11.1.28; |