| IED ID | IndEnz0002014271 |
| Enzyme Type ID | protease014271 |
| Protein Name |
Dihydrolipoyl dehydrogenase, mitochondrial EC 1.8.1.4 Dihydrolipoamide dehydrogenase |
| Gene Name | Dld |
| Organism | Mus musculus (Mouse) |
| 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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNNRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEFKIGKFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAAAFGKPINF |
| Enzyme Length | 509 |
| Uniprot Accession Number | O08749 |
| Absorption | |
| Active Site | ACT_SITE 487; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P09624 |
| Activity Regulation | |
| Binding Site | BINDING 89; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 154; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 243; /note=NAD; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 278; /note=NAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 314; /note=NAD; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 355; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622 |
| 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; Evidence={ECO:0000250|UniProtKB:P09622}; |
| DNA Binding | |
| EC Number | 1.8.1.4 |
| Enzyme Function | FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (By similarity). 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 (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). {ECO:0000250|UniProtKB:P09622, ECO:0000250|UniProtKB:Q811C4, ECO:0000269|PubMed:17404228}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 71..80; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 183..185; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 220..227; /note=NAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 361..364; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622 |
| Features | Active site (1); Binding site (6); Chain (1); Disulfide bond (1); Modified residue (26); Nucleotide binding (4); Sequence conflict (4); Site (2); Transit peptide (1) |
| Keywords | Acetylation;Cell projection;Cilium;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;FAD;Flagellum;Flavoprotein;Mitochondrion;NAD;Nucleus;Oxidoreductase;Phosphoprotein;Redox-active center;Reference proteome;Transit peptide |
| Interact With | O54910 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:9169128}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15888450}. 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:0000250|UniProtKB:P09622}. |
| Modified Residue | MOD_RES 66; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337"; MOD_RES 66; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 104; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 104; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 122; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 122; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 132; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 132; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 143; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 143; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 159; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 166; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 273; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 277; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 285; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 297; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q6P6R2"; MOD_RES 334; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 334; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 346; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 410; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337"; MOD_RES 410; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 417; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:P09622"; MOD_RES 420; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 430; /note="N6-succinyllysine"; /evidence="ECO:0007744|PubMed:23806337"; MOD_RES 505; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:23576753"; MOD_RES 505; /note="N6-succinyllysine; alternate"; /evidence="ECO:0007744|PubMed:23806337" |
| Post Translational Modification | PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12904583; 14651853; 14681479; 15009635; 15356189; 16615898; 16635246; 16916647; 17500595; 17626619; 17634366; 18423880; 18614015; 19423573; 19455133; 19573295; 19834914; 21267068; 23263557; 23475850; 23624931; 24391134; 25576851; 26078703; 27215380; 28245920; 29128334; 8672127; 9373037; 9405644; |
| Motif | |
| Gene Encoded By | |
| Mass | 54,272 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15045 |
| Cross Reference Brenda |