| IED ID | IndEnz0018000211 |
| Enzyme Type ID | peroxidase000211 |
| Protein Name |
Dihydrolipoyl dehydrogenase LPD EC 1.8.1.4 Component of peroxynitrite reductase/peroxidase complex Component of PNR/P Dihydrolipoamide dehydrogenase E3 component of alpha-ketoacid dehydrogenase complexes |
| Gene Name | lpdC lpd MT0478 |
| Organism | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
| 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 CDC 1551 / Oshkosh) |
| Enzyme Sequence | MTHYDVVVLGAGPGGYVAAIRAAQLGLSTAIVEPKYWGGVCLNVGCIPSKALLRNAELVHIFTKDAKAFGISGEVTFDYGIAYDRSRKVAEGRVAGVHFLMKKNKITEIHGYGTFADANTLLVDLNDGGTESVTFDNAIIATGSSTRLVPGTSLSANVVTYEEQILSRELPKSIIIAGAGAIGMEFGYVLKNYGVDVTIVEFLPRALPNEDADVSKEIEKQFKKLGVTILTATKVESIADGGSQVTVTVTKDGVAQELKAEKVLQAIGFAPNVEGYGLDKAGVALTDRKAIGVDDYMRTNVGHIYAIGDVNGLLQLAHVAEAQGVVAAETIAGAETLTLGDHRMLPRATFCQPNVASFGLTEQQARNEGYDVVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDLTASELARNVHTHPTMSEALQECFHGLVGHMINF |
| Enzyme Length | 464 |
| Uniprot Accession Number | P9WHH8 |
| Absorption | |
| Active Site | ACT_SITE 443; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | BINDING 50; /note=FAD; BINDING 113; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250; BINDING 201; /note=NAD; /evidence=ECO:0000250; BINDING 309; /note=FAD; /evidence=ECO:0000250; BINDING 317; /note=FAD; via amide nitrogen; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; |
| DNA Binding | |
| EC Number | 1.8.1.4 |
| Enzyme Function | FUNCTION: Lipoamide dehydrogenase is an essential component of the alpha-ketoacid dehydrogenase complexes, namely the pyruvate dehydrogenase (PDH) complex, the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, and likely also the 2-oxoglutarate dehydrogenase (ODH) complex. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes (By similarity). {ECO:0000250}.; FUNCTION: Together with AhpC, AhpD and DlaT, 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. {ECO:0000250}.; FUNCTION: Appears to be essential for Mtb pathogenesis. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 33..41; /note=FAD; /evidence=ECO:0000250; NP_BIND 178..182; /note=NAD; /evidence=ECO:0000250; NP_BIND 266..269; /note=NAD; /evidence=ECO:0000250 |
| Features | Active site (1); Binding site (5); Chain (1); Disulfide bond (1); Nucleotide binding (3) |
| Keywords | Antioxidant;Cytoplasm;Disulfide bond;FAD;Flavoprotein;Glycolysis;NAD;Oxidoreductase;Redox-active center;Tricarboxylic acid cycle;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,239 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15045 |
| Cross Reference Brenda | 1.8.1.4; |