Detail Information for IndEnz0018000623
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