| IED ID | IndEnz0018000622 |
| Enzyme Type ID | peroxidase000622 |
| Protein Name |
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex EC 2.3.1.12 Component of peroxynitrite reductase/peroxidase complex Component of PNR/P Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex Pyruvate dehydrogenase complex component E2 PDH component E2 |
| Gene Name | dlaT sucB MT2272 |
| 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 | MAFSVQMPALGESVTEGTVTRWLKQEGDTVELDEPLVEVSTDKVDTEIPSPAAGVLTKIIAQEDDTVEVGGELAVIGDAKDAGEAAAPAPEKVPAAQPESKPAPEPPPVQPTSGAPAGGDAKPVLMPELGESVTEGTVIRWLKKIGDSVQVDEPLVEVSTDKVDTEIPSPVAGVLVSISADEDATVPVGGELARIGVAADIGAAPAPKPAPKPVPEPAPTPKAEPAPSPPAAQPAGAAEGAPYVTPLVRKLASENNIDLAGVTGTGVGGRIRKQDVLAAAEQKKRAKAPAPAAQAAAAPAPKAPPAPAPALAHLRGTTQKASRIRQITANKTRESLQATAQLTQTHEVDMTKIVGLRARAKAAFAEREGVNLTFLPFFAKAVIDALKIHPNINASYNEDTKEITYYDAEHLGFAVDTEQGLLSPVIHDAGDLSLAGLARAIADIAARARSGNLKPDELSGGTFTITNIGSQGALFDTPILVPPQAAMLGTGAIVKRPRVVVDASGNESIGVRSVCYLPLTYDHRLIDGADAGRFLTTIKHRLEEGAFEADLGL |
| Enzyme Length | 553 |
| Uniprot Accession Number | P9WIS6 |
| Absorption | |
| Active Site | ACT_SITE 523; /evidence=ECO:0000250; ACT_SITE 527; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; |
| DNA Binding | |
| EC Number | 2.3.1.12 |
| Enzyme Function | FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). {ECO:0000250}.; FUNCTION: Together with AhpC, AhpD 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. {ECO:0000250}.; FUNCTION: Appears to be essential for Mtb pathogenesis. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (3); Modified residue (2); Region (3) |
| Keywords | Acyltransferase;Antioxidant;Glycolysis;Lipoyl;Repeat;Transferase;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 43; /note=N6-lipoyllysine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01066; MOD_RES 162; /note=N6-lipoyllysine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01066 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 57,088 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:17017 |
| Cross Reference Brenda |