| IED ID | IndEnz0002004177 |
| Enzyme Type ID | protease004177 |
| Protein Name |
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial EC 2.3.1.61 2-oxoglutarate dehydrogenase complex component E2 OGDC-E2 Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex E2K |
| Gene Name | DLST DLTS |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFFRTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL |
| Enzyme Length | 453 |
| Uniprot Accession Number | P36957 |
| Absorption | |
| Active Site | ACT_SITE 424; /evidence=ECO:0000269|PubMed:30929736; ACT_SITE 428; /evidence=ECO:0000250|UniProtKB:Q9N0F1 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120; EC=2.3.1.61; Evidence={ECO:0000269|PubMed:30929736};PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15215; Evidence={ECO:0000305|PubMed:30929736}; |
| DNA Binding | |
| EC Number | 2.3.1.61 |
| Enzyme Function | FUNCTION: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711, PubMed:30929736). A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (PubMed:29211711). {ECO:0000269|PubMed:29211711, ECO:0000269|PubMed:30929736}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle. {ECO:0000269|PubMed:30929736}. |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (2); Beta strand (9); Chain (1); Compositional bias (1); Domain (1); Helix (11); Modified residue (8); Mutagenesis (2); Natural variant (6); Region (1); Sequence conflict (7); Transit peptide (1); Turn (4) |
| Keywords | 3D-structure;Acetylation;Acyltransferase;Alternative splicing;Direct protein sequencing;Disease variant;Lipoyl;Mitochondrion;Nucleus;Phosphoprotein;Reference proteome;Transferase;Transit peptide;Tricarboxylic acid cycle |
| Interact With | Q8N1W1-4; Q8TAB5; O94983-5; P06493; O75175; Q6UXH1-2; P49184; Q8IY82; Q99944; P16422; Q9NVM1; Q96GK7; Q10981; P36382; P09471; P79483; P14060; P42858; Q7Z6Z7-2; O75874; Q9ULR0; A0JP07; P26715; Q6P5S2; P09382; O00214-2; P43356; Q7Z434; Q8NCR3; Q8TB02; Q96EY8; A2RUH7; Q9NPC7; P55209; Q9HC98-4; Q8NCF5-2; Q96P20; Q8N323; Q6P4D5-2; Q8N2W9; Q8NBT0; O14829; Q96QH2; Q9Y617; P43686; Q13200; Q9Y3Y4; Q13636; Q96E17; P61224; P50749; Q96I25; P52756; Q02978; Q3SY56; Q96L03; Q7Z698; F6Y2X3; P48775; Q9BQ29; Q9BT49; P49746; Q96JJ7-2; Q9H2S6-2; Q68CL5-3; Q9ULW0; Q9NX07; P07437; Q7Z780; O75317; P62258; Q96EF9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:29211711}. Nucleus {ECO:0000269|PubMed:29211711}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000269|PubMed:29211711}. |
| Modified Residue | MOD_RES 81; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 110; /note=N6-lipoyllysine; /evidence=ECO:0000255|PROSITE-ProRule:PRU01066; MOD_RES 154; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 267; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 272; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 273; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 277; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2; MOD_RES 307; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:Q9D2G2 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1) |
| Cross Reference PDB | 6H05; |
| Mapped Pubmed ID | 10103005; 10227647; 11436125; 11445257; 11752427; 11825528; 12577067; 12805207; 15038610; 15946682; 16169070; 17174955; 17220478; 17353931; 19615732; 19703396; 20379614; 20562859; 20711500; 20869947; 20877624; 2188967; 21911578; 22235656; 23475850; 23606334; 23902751; 24189400; 24256811; 24341803; 25525879; 25609649; 26496610; 26876595; 33180916; 33684457; 34233924; 9727038; |
| Motif | |
| Gene Encoded By | |
| Mass | 48,755 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15213; RHEA:15215 |
| Cross Reference Brenda |