| IED ID | IndEnz0018000623 |
| Enzyme Type ID | peroxidase000623 |
| 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 Rv2215 MTCY190.26 |
| 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 | MAFSVQMPALGESVTEGTVTRWLKQEGDTVELDEPLVEVSTDKVDTEIPSPAAGVLTKIIAQEDDTVEVGGELAVIGDAKDAGEAAAPAPEKVPAAQPESKPAPEPPPVQPTSGAPAGGDAKPVLMPELGESVTEGTVIRWLKKIGDSVQVDEPLVEVSTDKVDTEIPSPVAGVLVSISADEDATVPVGGELARIGVAADIGAAPAPKPAPKPVPEPAPTPKAEPAPSPPAAQPAGAAEGAPYVTPLVRKLASENNIDLAGVTGTGVGGRIRKQDVLAAAEQKKRAKAPAPAAQAAAAPAPKAPPAPAPALAHLRGTTQKASRIRQITANKTRESLQATAQLTQTHEVDMTKIVGLRARAKAAFAEREGVNLTFLPFFAKAVIDALKIHPNINASYNEDTKEITYYDAEHLGFAVDTEQGLLSPVIHDAGDLSLAGLARAIADIAARARSGNLKPDELSGGTFTITNIGSQGALFDTPILVPPQAAMLGTGAIVKRPRVVVDASGNESIGVRSVCYLPLTYDHRLIDGADAGRFLTTIKHRLEEGAFEADLGL |
| Enzyme Length | 553 |
| Uniprot Accession Number | P9WIS7 |
| Absorption | |
| Active Site | ACT_SITE 523; /evidence=ECO:0000250; ACT_SITE 527; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by rhodanine compounds. Some of them almost exclusively kill non-replicating mycobacteria in synergy with products of host immunity, such as nitric oxide and hypoxia, and are effective on bacteria within macrophages. {ECO:0000269|PubMed:18329613}. |
| 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).; 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.; FUNCTION: Appears to be essential for Mtb pathogenesis. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0 for PDH complex activity. Half-maximal activity is observed at pH 7.0 and pH 9.0. Activity is abolished at pH < 5. {ECO:0000269|PubMed:16045627}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (2); Domain (3); Initiator methionine (1); Modified residue (3); Region (3) |
| Keywords | Acetylation;Acyltransferase;Antioxidant;Glycolysis;Lipoyl;Reference proteome;Repeat;Transferase;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0007744|PubMed:21969609"; MOD_RES 43; /note="N6-lipoyllysine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305|PubMed:11799204"; MOD_RES 162; /note="N6-lipoyllysine"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305|PubMed:11799204" |
| 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 |