| IED ID | IndEnz0002004772 |
| Enzyme Type ID | protease004772 |
| Protein Name |
Dihydrolipoyl dehydrogenase, mitochondrial EC 1.8.1.4 Dihydrolipoamide dehydrogenase Fragment |
| Gene Name | DLD |
| Organism | Mesocricetus auratus (Golden hamster) |
| 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 Cricetidae Cricetinae (hamsters) Mesocricetus Mesocricetus auratus (Golden hamster) |
| Enzyme Sequence | FNRXSPGLQGVSSVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIELSEVRLNLEKMMEQKSSAVKALTGGIAHLFKQNKVVHVNGFGNITGKNQVTATKADGSSQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGAEVTAVEFLGHVGGIGIDMEISKKFQRILQKQGFKFKLNPKVPGATKRSDGKIDVSVEAAPGGKAEVIPCDVLLVCIGRRPFTQNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFR |
| Enzyme Length | 479 |
| Uniprot Accession Number | Q811C4 |
| Absorption | |
| Active Site | ACT_SITE 471; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P09624 |
| Activity Regulation | |
| Binding Site | BINDING 73; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 138; /note=FAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 227; /note=NAD; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 262; /note=NAD; via amide nitrogen and carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 298; /note=NAD; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P09622; BINDING 339; /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:0000269|PubMed:15888450}; |
| 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) (PubMed:15888450). 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 (By similarity). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (PubMed:14645106, PubMed:15888450). {ECO:0000250|UniProtKB:P09622, ECO:0000269|PubMed:14645106, ECO:0000269|PubMed:15888450}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 55..64; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 167..169; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 204..211; /note=NAD; /evidence=ECO:0000250|UniProtKB:P09622; NP_BIND 345..348; /note=FAD; /evidence=ECO:0000250|UniProtKB:P09622 |
| Features | Active site (1); Binding site (6); Chain (1); Disulfide bond (1); Modified residue (21); Non-terminal residue (2); Nucleotide binding (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 | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P09622}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:15888450}. 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 50; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 50; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 88; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 88; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 106; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 106; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 116; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 116; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 127; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P09622; MOD_RES 127; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 143; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 150; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 257; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 261; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 269; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 330; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 394; /note=N6-acetyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P09622; MOD_RES 394; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 401; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P09622; MOD_RES 404; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O08749; MOD_RES 414; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O08749 |
| Post Translational Modification | PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:14645106, ECO:0000269|PubMed:15888450}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 50,723 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15045 |
| Cross Reference Brenda | 1.8.1.4; |