{ "uniprot_canonical_ac": "P09622-1", "uniprot_ac": "P09622", "uniprot_id": "DLDH_HUMAN", "mass": { "chemical_mass": 54177.0, "monoisotopic_mass": 54177.0 }, "refseq": { "ac": "NP_000099", "name": "dihydrolipoyl dehydrogenase, mitochondrial isoform 1 precursor", "summary": "This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099" }, "gene_names": [ { "name": "DLD", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/P09622", "id": "P09622" }, { "name": "DLDD; DLDH; E3; GCSL; LAD; OGDC-E3; PHE3", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099", "id": "NP_000099" }, { "name": "DLD", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099", "id": "NP_000099" }, { "name": "GCSL", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P09622", "id": "P09622" }, { "name": "LAD", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P09622", "id": "P09622" }, { "name": "PHE3", "resource": "UniProtKB", "type": "synonym", "url": "https://www.uniprot.org/uniprot/P09622", "id": "P09622" } ], "protein_names": [ { "name": "Dihydrolipoyl dehydrogenase, mitochondrial", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "P09622" }, { "name": "1.8.1.4", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09622" }, { "name": "Dihydrolipoamide dehydrogenase", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09622" }, { "name": "E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex; dihydrolipoyl dehydrogenase, mitochondrial; glycine cleavage system protein L; lipoamide reductase; lipoamide dehydrogenase; lipoyl dehydrogenase; diaphorase; glycine cleavage system L protein; epididymis secretory sperm binding protein", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099", "id": "NP_000099" }, { "name": "Glycine cleavage system L protein", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "P09622" }, { "name": "dihydrolipoyl dehydrogenase, mitochondrial isoform 1 precursor", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099", "id": "NP_000099" } ], "function": [ { "annotation": "Certain DLD mutations can simultaneously induce the loss of a primary metabolic activity and the gain of a moonlighting proteolytic activity thus contributing to the metabolic derangement associated with DLD deficiency. GeneRIF: Human, mouse, and pig Dld has moonlighting function as a protease in addition to its canonical function as a a dehydrogenase.", "evidence": [ { "database": "RefSeq", "id": "NP_000099", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099" }, { "database": "PubMed", "id": "17404228", "url": "https://glygen.org/publication/PubMed/17404228" } ] }, { "annotation": "Lipoamide dehydrogenase (LADH) deficiency: medical perspectives of the structural and functional characterization of LADH and its pathogenic variants. Review article", "evidence": [ { "database": "RefSeq", "id": "NP_000099", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099" }, { "database": "PubMed", "id": "36842090", "url": "https://glygen.org/publication/PubMed/36842090" } ] }, { "annotation": "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:15712224, PubMed:16442803, PubMed:16770810, PubMed:17404228, PubMed:20160912, PubMed:20385101). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion (PubMed:29211711). 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). 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).", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622#function" }, { "database": "PubMed", "id": "16770810", "url": "https://glygen.org/publication/PubMed/16770810" }, { "database": "PubMed", "id": "20160912", "url": "https://glygen.org/publication/PubMed/20160912" }, { "database": "PubMed", "id": "15712224", "url": "https://glygen.org/publication/PubMed/15712224" }, { "database": "PubMed", "id": "17404228", "url": "https://glygen.org/publication/PubMed/17404228" }, { "database": "UniProtKB", "id": "Q811C4", "url": "https://www.uniprot.org/uniprot/Q811C4#function" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" }, { "database": "PubMed", "id": "16442803", "url": "https://glygen.org/publication/PubMed/16442803" }, { "database": "PubMed", "id": "29211711", "url": "https://glygen.org/publication/PubMed/29211711" } ] }, { "annotation": "Pan-Cancer Analysis of the Cuproptosis-Related Gene DLD. Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_000099", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099" }, { "database": "PubMed", "id": "38077227", "url": "https://glygen.org/publication/PubMed/38077227" } ] }, { "annotation": "This gene encodes a member of the class-I pyridine nucleotide-disulfide oxidoreductase family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In homodimeric form, the encoded protein functions as a dehydrogenase and is found in several multi-enzyme complexes that regulate energy metabolism. However, as a monomer, this protein can function as a protease. Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014].", "evidence": [ { "database": "RefSeq", "id": "NP_000099", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_000099" } ] } ], "disease": [ { "disease_id": "DOID:9269", "recommended_name": { "id": "DOID:9269", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:9269", "name": "maple syrup urine disease", "description": "An organic acidemia that is caused by a deficiency of decarboxylase leading to high concentrations of valine, leucine, isoleucine, and alloisoleucine in the blood, urine, and cerebrospinal fluid and characterized by an odor of maple syrup to the urine, vomiting, hypertonicity, severe mental retardation, seizures, and eventually death unless the condition is treated with dietary measures." }, "synonyms": [ { "id": "DOID:9269", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:9269", "name": "Ketoacidaemia", "description": "" }, { "id": "DOID:9269", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:9269", "name": "branched chain ketoaciduria", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "pyruvate dehydrogenase E3 deficiency", "description": "Pyruvate dehydrogenase E3 deficiency is a very rare subtype of pyruvate dehydrogenase deficiency (PDHD) characterized by either early-onset lactic acidosis and delayed development, later-onset neurological dysfunction or liver disease." }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "DLD deficiency", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "E3-deficient maple syrup urine disease", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "dihydrolipoamide dehydrogenase deficiency", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "pyruvate dehydrogenase E3 deficiency", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "DLDD", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "Dld deficiency", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "E3 deficiency", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "lipoamide dehydrogenase deficiency, lactic acidosis due to", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "maple syrup urine disease, type 3", "description": "" }, { "id": "MONDO:0009529", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009529", "name": "maple syrup urine disease, type III", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease", "description": "An autosomal recessive inherited disorder caused by mutations in the BCKDHA, BCKDHB, DBT, and DLD genes. It is characterized by a deficiency of branched-chain alpha-keto acid dehydrogenase complex, leading to accumulation of metabolites in the body fluids. The name of the disease derives from the sweet odor of the urine in infants, reminiscent of maple syrup. Signs and symptoms usually appear in infancy and include lethargy and developmental delays. If untreated, it may lead to seizures, coma, and death." }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "BCKD deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "BCKDH deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "Ketoacidaemia", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "MSUD", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "branched chain ketoaciduria", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "branched-chain 2-ketoacid dehydrogenase deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "branched-chain ketoaciduria", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type IA", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type IB", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type II", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type 1A", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type 1B", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, type 2", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "Keto acid decarboxylase deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "branched-chain Alpha-Keto acid dehydrogenase deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "dihydrolipoamide dehydrogenase deficiency", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, Intermediate", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, classic", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, intermittent", "description": "" }, { "id": "MONDO:0009563", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0009563", "name": "maple syrup urine disease, thiamine-responsive", "description": "" }, { "id": "MONDO:0014057", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014057", "name": "maple syrup urine disease, mild variant", "description": "" }, { "id": "MONDO:0014057", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014057", "name": "maple syrup urine disease, mild variant", "description": "" }, { "id": "MONDO:0014057", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014057", "name": "MSUDMV", "description": "" }, { "id": "MIM:246900", "resource": "MIM", "url": "https://www.omim.org/entry/246900", "name": "Dihydrolipoamide dehydrogenase deficiency", "description": "Dihydrolipoamide dehydrogenase deficiency" }, { "id": "MIM:248600", "resource": "MIM", "url": "https://www.omim.org/entry/248600", "name": "Maple syrup urine disease 2", "description": "Maple syrup urine disease 2" }, { "id": "MIM:615135", "resource": "MIM", "url": "https://www.omim.org/entry/615135", "name": "Maple syrup urine disease, mild variant", "description": "Maple syrup urine disease, mild variant" } ], "evidence": [ { "id": "246900", "database": "MIM", "url": "https://www.omim.org/entry/246900" } ] } ], "snv": [ { "evidence": [ { "id": "rs768285197", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs768285197" }, { "id": "rs768285197", "database": "ExAC", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs768285197" }, { "id": "rs768285197", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs768285197#frequency_tab" }, { "id": "rs768285197", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs768285197" } ], "glycoeffect": [ "o-glyco-site-loss" ], "start_pos": 183, "end_pos": 183, "sequence_org": "T", "sequence_mut": "A", "comment": "Germline mutation passed 1 out of 1 filters: o-glyco-site-loss (T->A).", "chr_id": "7", "chr_pos": "107905469", "ref_nt": "G", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "T183", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs776129705", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs776129705" }, { "id": "rs776129705", "database": "ExAC", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs776129705" }, { "id": "rs776129705", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs776129705" } ], "glycoeffect": [ "o-glyco-site-loss" ], "start_pos": 183, "end_pos": 183, "sequence_org": "T", "sequence_mut": "M", "comment": "Germline mutation passed 1 out of 1 filters: o-glyco-site-loss (T->M).", "chr_id": "7", "chr_pos": "107905470", "ref_nt": "T", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "T183", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs1351453420", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1351453420" }, { "id": "rs1351453420", "database": "TOPMed", "url": "https://www.ncbi.nlm.nih.gov/snp/rs1351453420#frequency_tab" } ], "glycoeffect": [ "n-glyco-sequon-gain", "o-glyco-site-loss" ], "start_pos": 277, "end_pos": 277, "sequence_org": "K", "sequence_mut": "N", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (KVT->NVT).", "chr_id": "7", "chr_pos": "107915652", "ref_nt": "T", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "K277", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "rs1285861600", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1285861600" }, { "id": "rs1285861600", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs1285861600" } ], "glycoeffect": [ "n-glyco-sequon-gain" ], "start_pos": 500, "end_pos": 500, "sequence_org": "A", "sequence_mut": "S", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (NLA->NLS).", "chr_id": "7", "chr_pos": "107919227", "ref_nt": "T", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "A500", "keywords": [ "ebi", "germline" ] } ], "mutagenesis": [ { "start_pos": 383, "end_pos": 383, "sequence_org": "H", "sequence_mut": "A", "comment": "Reduces dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 383, "end_pos": 383, "sequence_org": "H", "sequence_mut": "L", "comment": "Reduces dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 448, "end_pos": 448, "sequence_org": "D", "sequence_mut": "A", "comment": "Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 448, "end_pos": 448, "sequence_org": "D", "sequence_mut": "N", "comment": "Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 466, "end_pos": 466, "sequence_org": "E", "sequence_mut": "A", "comment": "Decreases dehydrogenase activity. Loss of proteolytic activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "17404228", "url": "https://glygen.org/publication/PubMed/17404228" } ] }, { "start_pos": 473, "end_pos": 473, "sequence_org": "Y", "sequence_mut": "A", "comment": "Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 473, "end_pos": 473, "sequence_org": "Y", "sequence_mut": "F", "comment": "Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 473, "end_pos": 473, "sequence_org": "Y", "sequence_mut": "H", "comment": "Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 482, "end_pos": 482, "sequence_org": "R", "sequence_mut": "A", "comment": "Does not affect dihydrolipoyl dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20385101", "url": "https://glygen.org/publication/PubMed/20385101" } ] }, { "start_pos": 482, "end_pos": 482, "sequence_org": "R", "sequence_mut": "M", "comment": "Does not affect interaction with PDHX.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20160912", "url": "https://glygen.org/publication/PubMed/20160912" } ] }, { "start_pos": 485, "end_pos": 485, "sequence_org": "H", "sequence_mut": "A", "comment": "Loss of dehydrogenase activity. Increases proteolytic activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "17404228", "url": "https://glygen.org/publication/PubMed/17404228" } ] }, { "start_pos": 491, "end_pos": 491, "sequence_org": "S", "sequence_mut": "A", "comment": "Loss of proteolytic activity. Does not affect dehydrogenase activity.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "17404228", "url": "https://glygen.org/publication/PubMed/17404228" } ] }, { "start_pos": 492, "end_pos": 492, "sequence_org": "E", "sequence_mut": "Q", "comment": "Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20160912", "url": "https://glygen.org/publication/PubMed/20160912" } ] }, { "start_pos": 505, "end_pos": 505, "sequence_org": "K", "sequence_mut": "M", "comment": "Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20160912", "url": "https://glygen.org/publication/PubMed/20160912" } ] }, { "start_pos": 89, "end_pos": 89, "sequence_org": "K", "sequence_mut": "E", "comment": "Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "20160912", "url": "https://glygen.org/publication/PubMed/20160912" } ] } ], "expression_tissue": [ { "tissue": { "name": "Adult mammalian kidney", "namespace": "UBERON", "id": "0000082", "url": "http://purl.obolibrary.org/obo/UBERON_0000082" }, "score": "95.54", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000091140", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000091140" } ] }, { "tissue": { "name": "Oral cavity", "namespace": "UBERON", "id": "0000167", "url": "http://purl.obolibrary.org/obo/UBERON_0000167" }, "score": "96.78", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000091140", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000091140" } ] }, { "tissue": { "name": "Stomach", "namespace": "UBERON", "id": "0000945", "url": 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"database": "Bgee", "id": "ENSG00000091140", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000091140" } ] }, { "tissue": { "name": "Colon", "namespace": "UBERON", "id": "0001155", "url": "http://purl.obolibrary.org/obo/UBERON_0001155" }, "score": "96.33", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000091140", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000091140" } ] }, { "tissue": { "name": "Urinary bladder", "namespace": "UBERON", "id": "0001255", "url": "http://purl.obolibrary.org/obo/UBERON_0001255" }, "score": "95.97", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000091140", "url": "https://bgee.org/?page=gene&gene_id=ENSG00000091140" } ] }, { "tissue": { "name": "Thyroid gland", "namespace": "UBERON", "id": "0002046", "url": "http://purl.obolibrary.org/obo/UBERON_0002046" }, "score": "92.96", "present": "HIGH", "evidence": [ { "database": "Bgee", "id": "ENSG00000091140", "url": 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"" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate carcinoma", "description": "Prostate carcinoma that has developed in relatives of patients with a history of prostate carcinoma." }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "familial prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate cancer", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "hereditary prostate carcinoma", "description": "" }, { "id": "MONDO:0023122", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023122", "name": "prostate cancer, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0023122", 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"categories": [ "Protein" ] }, { "id": "F2Z2E3", "url": "https://www.uniprot.org/uniprot/F2Z2E3", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "F2Z2E3-1", "url": "https://www.uniprot.org/uniprot/F2Z2E3-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "F8WDM5", "url": "https://www.uniprot.org/uniprot/F8WDM5", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "F8WDM5-1", "url": "https://www.uniprot.org/uniprot/F8WDM5-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "F8WDY5", "url": "https://www.uniprot.org/uniprot/F8WDY5", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "F8WDY5-1", "url": "https://www.uniprot.org/uniprot/F8WDY5-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09622-1", "url": "https://www.uniprot.org/uniprot/P09622-1", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09622-2", "url": "https://www.uniprot.org/uniprot/P09622-2", "database": "UniProtKB", "categories": [ "Protein" ] }, { "id": "P09622-3", "url": "https://www.uniprot.org/uniprot/P09622-3", "database": "UniProtKB", "categories": [ "Protein" ] } ], "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF", "length": 509, "header": "sp|P09622-1|DLDH_HUMAN Isoform 1 of Dihydrolipoyl dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=2 CANONICAL=P09622-1" }, "isoforms": [ { "isoform_ac": "E9PEX6-1", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF", "length": 486, "header": "tr|E9PEX6-1|DLDH_HUMAN Computationally mapped isoform of Dihydrolipoyl dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=1 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107919256, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000440410.5", "url": "https://www.ensembl.org/id/ENST00000440410.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000417016.1", "url": "https://www.ensembl.org/id/ENSP00000417016.1" } ] } }, { "isoform_ac": "F2Z2E3-1", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIETLG", "length": 115, "header": "tr|F2Z2E3-1|F2Z2E3_HUMAN Computationally mapped isoform of dihydrolipoyl dehydrogenase OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=1 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107904870, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000451081.5", "url": "https://www.ensembl.org/id/ENST00000451081.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000388077.1", "url": "https://www.ensembl.org/id/ENSP00000388077.1" } ] } }, { "isoform_ac": "F8WDM5-1", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIENL", "length": 114, "header": "tr|F8WDM5-1|F8WDM5_HUMAN Computationally mapped isoform of dihydrolipoyl dehydrogenase OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=1 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107904667, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000450038.5", "url": "https://www.ensembl.org/id/ENST00000450038.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000409590.1", "url": "https://www.ensembl.org/id/ENSP00000409590.1" } ] } }, { "isoform_ac": "F8WDY5-1", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPSFIEQLSLLPYGPWKRFCI", "length": 58, "header": "tr|F8WDY5-1|F8WDY5_HUMAN Computationally mapped isoform of Dihydrolipoamide dehydrogenase OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=1 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107903533, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000415325.5", "url": "https://www.ensembl.org/id/ENST00000415325.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000402593.1", "url": "https://www.ensembl.org/id/ENSP00000402593.1" } ] } }, { "isoform_ac": "P09622-1", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF", "length": 509, "header": "sp|P09622-1|DLDH_HUMAN Isoform 1 of Dihydrolipoyl dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=2 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107919256, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000417551.5", "url": "https://www.ensembl.org/id/ENST00000417551.5" }, { "database": "Ensembl Peptide", "id": "ENSP00000390667.1", "url": "https://www.ensembl.org/id/ENSP00000390667.1" } ] } }, { "isoform_ac": "P09622-2", "url": "", "sequence": { "sequence": "MAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKVVHVNGYGKITGKNQVTATKADGGTQVIDTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF", "length": 410, "header": "sp|P09622-2|DLDH_HUMAN Isoform 2 of Dihydrolipoyl dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=2 CANONICAL=P09622-1" }, "locus": {} }, { "isoform_ac": "P09622-3", "url": "", "sequence": { "sequence": "MQSWSRVYCSLAKRGHFNRISHGLQGLSAVPLRTYADQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEMSEVRLNLDKMMEQKSTAVKALTGGIAHLFKQNKIDEDTIVSSTGALSLKKVPEKMVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGVGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSIEAASGGKAEVITCDVLLVCIGRRPFTKNLGLEELGIELDPRGRIPVNTRFQTKIPNIYAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGIEYKVGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASCEDIARVCHAHPTLSEAFREANLAASFGKSINF", "length": 461, "header": "sp|P09622-3|DLDH_HUMAN Isoform 3 of Dihydrolipoyl dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=DLD PE=1 SV=2 CANONICAL=P09622-1" }, "locus": { "chromosome": "7", "start_pos": 107919256, "end_pos": 107891251, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000437604.6", "url": "https://www.ensembl.org/id/ENST00000437604.6" }, { "database": "Ensembl Peptide", "id": "ENSP00000387542.2", "url": "https://www.ensembl.org/id/ENSP00000387542.2" } ] } } ], "glycosylation": [ { "glytoucan_ac": "G49108TO", "type": "O-linked", "subtype": "O-GlcNAcylation", "site_category": "reported_with_glycan", "site_seq": "T", "relation": "attached", "comment": "O-GlcNAcylation", "start_pos": 183, "start_aa": "Thr", "end_pos": 183, "end_aa": "Thr", "residue": "Thr", "site_lbl": "Thr183", "evidence": [ { "id": "P09622", "database": "O-GlcNAc Database", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=P09622" }, { "id": "30379171", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/30379171" }, { "id": "34725712", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/34725712" }, { "id": "26853435", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/26853435" }, { "id": "38253038", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/38253038" }, { "id": "32119511", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/32119511" }, { "id": "34229054", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/34229054" } ] } ], "phosphorylation": [ { "start_pos": 276, "end_pos": 276, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "P09622", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09622" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" } ], "site_lbl": "Thr276" }, { "start_pos": 285, "end_pos": 285, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "site_lbl": "Ser285" }, { "start_pos": 297, "end_pos": 297, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "site_lbl": "Ser297" }, { "start_pos": 341, "end_pos": 341, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Thr", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "P09622", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09622" }, { "database": "PubMed", "id": "20068231", "url": "https://glygen.org/publication/PubMed/20068231" } ], "site_lbl": "Thr341" }, { "start_pos": 502, "end_pos": 502, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" }, { "database": "iPTMnet", "id": "P09622", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/P09622" } ], "site_lbl": "Ser502" } ], "glycation": [], "keywords": [ "enzyme", "glycoprotein", "glycoprotein_reported_with_glycan" ], "publication": [ { "title": "Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.", "journal": "European journal of biochemistry", "date": "1999", "authors": "Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y", "evidence": [ { "database": "Reactome", "id": "R-HSA-389661", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389661" } ], "reference": [ { "type": "PubMed", "id": "10103005", "url": "https://glygen.org/publication/PubMed/10103005" } ] }, { "title": "Lipoamide dehydrogenase deficiency due to a novel mutation in the interface domain.", "journal": "Biochemical and biophysical research communications", "date": "1999", "authors": "Shany E, Saada A, Landau D, Shaag A, Hershkovitz E, Elpeleg ON", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "reference": [ { "type": "PubMed", "id": "10448086", "url": "https://glygen.org/publication/PubMed/10448086" } ] }, { "title": "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II.", "journal": "Human molecular genetics", "date": "1999", "authors": "Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP", "evidence": [ { "database": "Reactome", "id": "R-HSA-389661", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389661" } ], "reference": [ { "type": "PubMed", "id": "10484776", "url": "https://glygen.org/publication/PubMed/10484776" } ] }, { "title": "Expression, purification, and crystal structure determination of recombinant human epidermal-type fatty acid binding protein.", "journal": "Biochemistry", "date": "1999", "authors": "Hohoff C, Borchers T, Rustow B, Spener F, van Tilbeurgh H", "evidence": [ { "database": "Reactome", "id": "R-HSA-5362517", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5362517" } ], "reference": [ { "type": "PubMed", "id": "10493790", "url": "https://glygen.org/publication/PubMed/10493790" } ] }, { "title": "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase.", "journal": "Biochimica et biophysica acta", "date": "1999", "authors": "Rumsby G, Cregeen DP", "evidence": [ { "database": "Reactome", "id": "R-HSA-389661", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389661" } ], "reference": [ { "type": "PubMed", "id": "10524214", "url": "https://glygen.org/publication/PubMed/10524214" } ] }, { "title": "Aconitase polymorphism in man.", "journal": "Annals of human genetics", "date": "1975", "authors": "Slaughter CA, Hopkinson DA, Harris H", "evidence": [ { "database": "Reactome", "id": "R-HSA-71403", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71403" } ], "reference": [ { "type": "PubMed", "id": "1052766", "url": "https://glygen.org/publication/PubMed/1052766" } ] }, { "title": "L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases.", "journal": "The Biochemical journal", "date": "2000", "authors": "Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-71064", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71064" } ], "reference": [ { "type": "PubMed", "id": "10642506", "url": "https://glygen.org/publication/PubMed/10642506" } ] }, { "title": "The high-resolution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from human heart mitochondria.", "journal": "Structure (London, England : 1993)", "date": "2000", "authors": "White SA, Peake SJ, McSweeney S, Leonard G, Cotton NP, Jackson JB", "evidence": [ { "database": "Reactome", "id": "R-HSA-71403", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71403" } ], "reference": [ { "type": "PubMed", "id": "10673423", "url": "https://glygen.org/publication/PubMed/10673423" } ] }, { "title": "Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency.", "journal": "Human mutation", "date": "2000", "authors": "Lissens W, De Meirleir L, Seneca S, Liebaers I, Brown GK, Brown RM, Ito M, Naito E, Kuroda Y, Kerr DS, Wexler ID, Patel MS, Robinson BH, Seyda A", "evidence": [ { "database": "Reactome", "id": "R-HSA-70268", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-70268" } ], "reference": [ { "type": "PubMed", "id": "10679936", "url": "https://glygen.org/publication/PubMed/10679936" } ] }, { "title": "Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia.", "journal": "The Journal of clinical investigation", "date": "2000", "authors": "Furuyama K, Sassa S", "evidence": [ { "database": "Reactome", "id": "R-HSA-71403", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71403" } ], "reference": [ { "type": "PubMed", "id": "10727444", "url": "https://glygen.org/publication/PubMed/10727444" } ] }, { "title": "Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease.", "journal": "Structure (London, England : 1993)", "date": "2000", "authors": "AEvarsson A, Chuang JL, Wynn RM, Turley S, Chuang DT, Hol WG", "evidence": [ { "database": "Reactome", "id": "R-HSA-70895", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-70895" } ], "reference": [ { "type": "PubMed", "id": "10745006", "url": "https://glygen.org/publication/PubMed/10745006" } ] }, { "title": "Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia.", "journal": "American journal of human genetics", "date": "2000", "authors": "Sacksteder KA, Biery BJ, Morrell JC, Goodman BK, Geisbrecht BV, Cox RP, Gould SJ, Geraghty MT", "evidence": [ { "database": "Reactome", "id": "R-HSA-71064", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71064" } ], "reference": [ { "type": "PubMed", "id": "10775527", "url": "https://glygen.org/publication/PubMed/10775527" } ] }, { "title": "Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.", "journal": "The Journal of biological chemistry", "date": "2000", "authors": "Jones JM, Morrell JC, Gould SJ", "evidence": [ { "database": "Reactome", "id": "R-HSA-389661", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389661" } ], "reference": [ { "type": "PubMed", "id": "10777549", "url": "https://glygen.org/publication/PubMed/10777549" } ] }, { "title": "2-Methylbutyryl-coenzyme A dehydrogenase deficiency: a new inborn error of L-isoleucine metabolism.", "journal": "Pediatric research", "date": "2000", "authors": "Gibson KM, Burlingame TG, Hogema B, Jakobs C, Schutgens RB, Millington D, Roe CR, Roe DS, Sweetman L, Steiner RD, Linck L, Pohowalla P, Sacks M, Kiss D, 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"MLRIRSLLNNKRAFSSTVRTLTINKSHDVVIIGGGPAGYVAAIKAAQLGFNTACVEKRGKLGGTCLNVGCIPSKALLNNSHLFHQMHTEAQKRGIDVNGDIKINVANFQKAKDDAVKQLTGGIELLFKKNKVTYYKGNGSFEDETKIRVTPVDGLEGTVKEDHILDVKNIIVATGSEVTPFPGIEIDEEKIVSSTGALSLKEIPKRLTIIGGGIIGLEMGSVYSRLGSKVTVVEFQPQIGASMDGEVAKATQKFLKKQGLDFKLSTKVISAKRNDDKNVVEIVVEDTKTNKQENLEAEVLLVAVGRRPYIAGLGAEKIGLEVDKRGRLVIDDQFNSKFPHIKVVGDVTFGPMLAHKAEEEGIAAVEMLKTGHGHVNYNNIPSVMYSHPEVAWVGKTEEQLKEAGIDYKIGKFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAEDVARVCHAHPTLSEAFKEANMAAYDKAIHC", "length": 499 }, "evidence": [ { "id": "P09622", "url": "https://omabrowser.org/oma/group/P09622/", "database": "OMA" } ], "common_name": "Yeast" }, { "uniprot_canonical_ac": "Q6P6R2-1", "protein_name": "Dihydrolipoyl dehydrogenase, mitochondrial", "gene_name": "Dld", "tax_id": 10116, "organism": "Rattus norvegicus", "sequence": { "sequence": "MQSWSRVYCSLAKKGHFNRLSHGLQGASSVPLRTYSDQPIDADVTVIGSGPGGYVAAIKAAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHLAHGKDFASRGIEIPEVRLNLEKMMEQKRSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATTADGSTQVIGTKNILIATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQKQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQNLGLEELGIELDPKGRIPVNTRFQTKIPNIFAIGDVVAGPMLAHKAEDEGIICVEGMAGGAVHIDYNCVPSVIYTHPEVAWVGKSEEQLKEEGVEFKVGKFPFAANSRAKTNADTDGMVKILGHKSTDRILGAHILGPGAGEMVNEAALALEYGASCEDVARVCHAHPTLSEAFREANLAASFGKPINF", "length": 509 }, "evidence": [ { "id": "45919113", "url": "http://www.informatics.jax.org/homology/45919113", "database": "MGI" } ], "common_name": "Rat" }, { "uniprot_canonical_ac": "Q9VVL7-1", "protein_name": "Dihydrolipoyl dehydrogenase", "gene_name": "E3", "tax_id": 7227, "organism": "Drosophila melanogaster", "sequence": { "sequence": "MQFTLRHVVSAVAKTPLRTNAAILGALNARCYSSTHEADIVVIGSGPGGYVAAIKAAQMGMKTVSVEKEATLGGTCLNVGCIPSKALLNNSHYYHMAHSGDLEKRGISCGSVSLDLEKLMGQKSNAVKALTGGIAMLFKKNKVTQLTGFGTIVNPNEVEVKKSDGSTETVKTKNILIATGSEVTPFPGIEIDEEVIVSSTGALKLAKVPKHLVVIGAGVIGLELGSVWSRLGAEVTAIEFMDTIGGVGIDNEVSKTFQKVLTKQGLKFKLGTKVTAASRSGDNVTVSVENAKSGEKEEIQCDALLVSVGRRPYTEGLGLEAVGIVKDDRGRIPVNATFQTVVPNIYAIGDCIHGPMLAHKAEDEGLITIEGINGGHVHIDYNCVPSVVYTHPEVAWVGKSEEQLKQEGVAYKVGKFPFLANSRAKTNNDTDGFVKVLADQATDKILGTHIIGPGAGELINEAVLAMEYGAAAEDVARVCHAHPTCSEALREANVAAAFGKPINF", "length": 504 }, "evidence": [ { "id": "P09622", "url": "https://omabrowser.org/oma/group/P09622/", "database": "OMA" } ], "common_name": "Fruit fly" } ], "go_annotation": { "categories": [ { "name": "Molecular Function", "total": 3, "go_terms": [ { "name": "oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor", "id": "GO:0016668", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016668", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "flavin adenine dinucleotide binding", "id": "GO:0050660", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050660", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "dihydrolipoyl dehydrogenase activity", "id": "GO:0004148", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004148", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 11, "go_terms": [ { "name": "motile cilium", "id": "GO:0031514", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031514", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "acrosomal vesicle", "id": "GO:0001669", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001669", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "nucleus", "id": "GO:0005634", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "mitochondrion", "id": "GO:0005739", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005739", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "mitochondrial matrix", "id": "GO:0005759", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005759", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "acrosomal matrix", "id": "GO:0043159", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043159", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "mitochondrial pyruvate dehydrogenase complex", "id": "GO:0005967", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005967", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "mitochondrial alpha-ketoglutarate dehydrogenase complex", "id": "GO:0005947", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005947", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "oxoglutarate dehydrogenase complex", "id": "GO:0045252", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045252", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "pyruvate dehydrogenase complex", "id": "GO:0045254", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045254", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "acetyltransferase complex", "id": "GO:1902493", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1902493", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" } ] }, { "name": "Biological Process", "total": 8, "go_terms": [ { "name": "proteolysis", "id": "GO:0006508", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006508", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "regulation of membrane potential", "id": "GO:0042391", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042391", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "branched-chain amino acid catabolic process", "id": "GO:0009083", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0009083", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "sperm capacitation", "id": "GO:0048240", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048240", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "mitochondrial electron transport, NADH to ubiquinone", "id": "GO:0006120", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006120", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "gastrulation", "id": "GO:0007369", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007369", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "acetyl-CoA biosynthetic process from pyruvate", "id": "GO:0006086", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006086", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" }, { "name": "histone succinylation", "id": "GO:0106077", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0106077", "evidence": [ { "database": "UniProtKB", "id": "P09622", "url": "https://www.uniprot.org/uniprot/P09622" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 73, "end_pos": 75, "annotation": "n_glycosylation_sequon" }, { "start_pos": 93, "end_pos": 95, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [], "interactions": [], "reactions": [ { "id": "15045", "name": "", "equation": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q6P6R2-1", "A0A8I6A931-1", "P09622-1", "O08749-1", "P09624-1", "Q54EW8-1", "Q9VVL7-1" ], "evidence": [ { "id": "15045", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/15045" } ] }, { "id": "R-HSA-203946", "name": "PDK isoforms phosphorylate lipo-PDH", "equation": "", "summary": "The mitochondrial pyruvate dehydrogenase (PDH) complex (lipo-PDH) irreversibly decarboxylates pyruvate to acetyl CoA, thereby serving to oxidatively remove lactate, which is in equilibrium with pyruvate, and to link glycolysis in the cytosol to the tricarboxylic acid cycle in the mitochondria matrix. Pyruvate Dehydrogenase Kinase (PDK) in the mitochondrial matrix catalyzes the phosphorylation of serine residues of the E1 alpha subunit of the PDH complex, inactivating it. Pyruvate negatively regulates this reaction, and NADH and acetyl CoA positively regulate it (Bao et al. 2004). Four PDK isoforms have been identified and shown to catalyze the phosphorylation of E1 alpha in vitro (Gudi et al. 1995, Kolobova et al. 2001, Rowles et al. 1996). They differ in their expression patterns and quantitative responses to regulatory small molecules. All four isoforms catalyze the phosphorylation of serine residues 293 (\\site 1\\) and 300 (\\site 2\\); PDK1 can also catalyse the phosphorylation of serine 232 (\\site 3\\). Phosphorylation of a single site in a single E1 alpha subunit is sufficient for enzyme inactivation (Bowker-Kinley et al. 1998, Gudi et al. 1995, Kolobova et al. 2001, Korotchkina and Patel, 2001). The PDH-PDK axis is emerging as an important therapeutic point in genetic mitochondrial diseases, pulmonary arterial hypertension and cancer where cellular metabolism is perturbed (James et al. 2017). Dichloroacetate (DCA) is an acid salt analogue of acetic acid that is used as a drug to inhibit PDK (Li et al. 2009). The effect is to keep the PDH complex in an active form thus stimulating mitochondrial oxidative metabolism. Chronic DCA administration may cause reversible peripheral neuropathy in adults (Kaufmann et al. 2006), but is well tolerated in children and adolescents suffering from the primary mitochondrial disease lactic acidosis (Abdelmalak et al. 2013, Stacpoole et al. 2008). The Warburg effect is the observation that cancer cells prefer aerobic glycolysis to oxidative phosphorylation (Warburg 1956). Whether this effect is the consequence of genetic dysregulation in cancer or the cause of cancer remains unknown. It stands true for most types of cancer cells and has become one of the hallmarks of cancer. Aerobic glycolysis produces ATP at a much faster rate than oxidative phosphorylation, confering growth advantages to tumor cells. DCA, binding to and inhibiting PDK isoforms, promotes a shift from glycolysis to oxidative phosphorylation and reversing the Warburg effect. Its potential role, alone or in combination, in several cancers is being investigated (Kankotia & Stacpoole 2014, Tran et al. 2016).", "cellular_location": "mitochondrial matrix", "input_participant_list": [ "R-HSA-70070" ], "output_participant_list": [], "enzyme_list": [ "P10515-1", "P29803-1", "Q15120-1", "Q16654-1", "P09622-1", "P08559-1", "P11177-1", "Q15118-1", "Q15119-1" ], "evidence": [ { "id": "R-HSA-203946", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-203946" } ] }, { "id": "R-HSA-204169", "name": "PDP dephosphorylates p-lipo-PDH", "equation": "", "summary": "Pyruvate dehydrogenase phosphatase (PDP) in the mitochondrial matrix catalyzes the hydrolytic removal of phosphate groups from phosphoserine residues in the E1 alpha subunit of the pyruvate dehydrogenase complex. The active form of PDP is a heterodimer of a catalytic subunit and a regulatory one. Two isoforms of the catalytic subunit have been identified and biochemically characterized (Huang et al. 1998) and mutations in PDP1 have been associated with PDP deficiency in vivo (Maj et al. 2005). The properties of the human regulatory subunit have been deduced from those of its bovine homologue (Lawson et al. 1997). The activity of PDP1 is greatly enhanced through Ca2+ -dependent binding of the catalytic subunit (PDP1c) to the L2 (inner lipoyl) domain of dihydrolipoyl acetyltransferase (E2), which is also integrated in the pyruvate dehydrogenase complex. PDP activity requires Mg2+ (Huang et al. 1998).", "cellular_location": "mitochondrial matrix", "input_participant_list": [ "R-HSA-210342" ], "output_participant_list": [], "enzyme_list": [ "P10515-1", "P29803-1", "P09622-1", "Q9P0J1-1", "P08559-1", "P11177-1", "Q9P2J9-1" ], "evidence": [ { "id": "R-HSA-204169", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-204169" } ] }, { "id": "R-HSA-5693148", "name": "BCKDK phosphorylates BCKDH", "equation": "", "summary": "Mitochondrial 3-methyl-2-oxobutanoate dehydrogenase (lipoamide) kinase (BCKDK) catalyses the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways (Li et al. 2004, Wynn et al. 2004). BCKDH occupies a strategic point in the branched-chain amino acid (BCAA) catabolic pathway, and careful regulation of its activity is essential for correct BCAA metabolism. The overall activity of the BCKDH complex is controlled by the phosphorylation (inactivation)/dephosphorylation (activation) cycle.
Defects in BCKDK can cause branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD; MIM:614923), a metabolic disorder characterised by autism, epilepsy, intellectual disability, and reduced BCAAs (Novarino et al. 2012, Garcia-Cazorla et al. 2014).", "cellular_location": "mitochondrial matrix", "input_participant_list": [ "R-HSA-70019" ], "output_participant_list": [], "enzyme_list": [ "P11182-1", "P09622-1", "O14874-1", "P12694-1", "P21953-1" ], "evidence": [ { "id": "R-HSA-5693148", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693148" } ] }, { "id": "R-HSA-5693153", "name": "PPM1K dephosphorylates p-BCKDH", "equation": "", "summary": "The branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex occupies a strategic point in the branched-chain amino acid (BCAA) catabolic pathway, and careful regulation of its activity is essential for correct BCAA metabolism. The overall activity of the BCKDH complex is controlled by the phosphorylation (inactivation)/dephosphorylation (activation) cycle. Mitochondrial protein phosphatase 1K (PPM1K) dephosphorylates the E1 beta subunit of BCKDH therby regaining its active state. PPM1K requires Mn2+ as a cofactor for phosphatase activity (Wynn et al. 2012).", "cellular_location": "mitochondrial matrix", "input_participant_list": [ "R-HSA-5693120" ], "output_participant_list": [], "enzyme_list": [ "P11182-1", "P09622-1", "Q8N3J5-1", "P12694-1", "P21953-1" ], "evidence": [ { "id": "R-HSA-5693153", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5693153" } ] }, { "id": "R-HSA-5694018", "name": "DLD dimer:2xFAD oxidises GCSH:DHLL to GCSH:lipoate", "equation": "", "summary": "The last step in the glycine cleavage system is the reoxidation of the reduced lipoate (dihydrolipoyl group) attached to the H protein (GCSH:DHLL) catalysed by the L protein (mitochondrial dihydrolipoyl dehydrogenase, DLD) (Harris et al. 1997, Ciszak et al. 2006).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P09622-1" ], "evidence": [ { "id": "R-HSA-5694018", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5694018" } ] }, { "id": "R-HSA-6792572", "name": "LIPT1 transfers lipoyl group from lipoyl-GCSH to DHs", "equation": "", "summary": "Lipoate is an essential cofactor for two enzymes from energy metabolism (alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase) and three from amino acid metabolism (branched-chain ketoacid dehydrogenase, 2-oxoadipate dehydrogenase, and the glycine cleavage system). Lipoate synthesis in mitochondria requires three steps. In the third step, mitochondrial lipoyltransferase 1 (LIPT1) catalyses the transfer of a lipoyl group from lipoyl-K107-GCSH to lysine residue(s) of lipoate-dependent enzymes (Fujiwara et al. 1999). Defects in LIPT1 reduce lipoylation of pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, causing a cofactor disorder of mitochondrial energy metabolism (Soreze et al. 2013, Tort et al. 2014).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P36957-1", "Q02218-1", "P10515-1", "P29803-1", "P11182-1", "P09622-1", "Q96HY7-1", "P08559-1", "P11177-1", "P12694-1", "P21953-1", "Q9Y234-1" ], "evidence": [ { "id": "R-HSA-6792572", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6792572" } ] }, { "id": "R-HSA-70713", "name": "BCKDH transfers CoA group from CoA-SH to BCAAs", "equation": "", "summary": "The mitochondrial branched-chain alpha-ketoacid dehydrogenase (BKCDH) complex catalyzes the reactions of alpha-ketoisocaproate, alpha-keto beta-methylvalerate, or alpha-ketoisovalerate with CoA and NAD+ to form isovaleryl-CoA, a-methylbutyryl-CoA, or isobutyryl-CoA, respectively, and CO2 and NADH (Chuang and Shih 2001). While bovine and microbial BCKD complexes have been characterized most extensively (Reed and Hackert 1990), structural studies of individual components and subcomplexes of human BKCD have confirmed their structures and roles in the overall oxidative carboxylation process, and have related these features to the disruptive effects of mutations on branched-chain amino acid metabolism in vivo: E1a and E1b components - AEvarsson et al. 2000; E2 - Chang et al. 2002; E3- Brautigam et al. 2005. In addition, structural studies have confirmed the lipoylation of lysine residue 44 in E2 protein (Chang et al. 2002) and the loss of an aminoterminal mitochondrial transport sequence from mature E3 protein (Bruatigam et al. 2005). Loss of mitochondrial transport sequences from proteins E1a, E1b, and E2 has been domstrated by sequence analysis (Wynn et al. 1999).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P11182-1", "P09622-1", "P12694-1", "P21953-1" ], "evidence": [ { "id": "R-HSA-70713", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-70713" } ] }, { "id": "R-HSA-71037", "name": "alpha-ketoadipate + CoASH + NAD+ => glutaryl-CoA + CO2 + NADH + H+", "equation": "", "summary": "The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoadipate, CoASH, and NAD+ to form glutaryl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha-ketoadipate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the glutaryl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P36957-1", "Q02218-1", "P09622-1" ], "evidence": [ { "id": "R-HSA-71037", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71037" } ] }, { "id": "R-HSA-71397", "name": "lipo-PDH decarboxylates PYR to Ac-CoA", "equation": "", "summary": "The mitochondrial pyruvate dehydrogenase complex catalyzes the reaction of pyruvate, CoASH, and NAD+ to form acetylCoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 alpha, E1 beta, E2, and E3, each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of pyruvate catalyzed by E1 alpha and beta (pyruvate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the acetyl group derived from pyruvate is transferred to coenzyme A in two steps catalyzed by E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with pyruvate dehydrogenase complex and subunits purified from bovine tissue and other non-human sources. Direct evidence for the roles of the corresponding human proteins comes from studies of patients expressing mutant forms of E1 alpha (Lissens et al. 2000), E1 beta (Brown et al. 2004), E2 (Head et al. 2005), and E3 (Brautigam et al. 2005).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P10515-1", "P29803-1", "P09622-1", "P08559-1", "P11177-1" ], "evidence": [ { "id": "R-HSA-71397", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71397" } ] }, { "id": "R-HSA-71401", "name": "alpha-ketoglutarate + CoASH + NAD+ => succinyl-CoA + CO2 + NADH + H+", "equation": "", "summary": "The mitochondrial alpha-ketoglutarate dehydrogenase complex catalyzes the reaction of alpha-ketoglutarate, CoASH, and NAD+ to form succinyl-CoA, CO2, and NADH. The enzyme complex contains multiple copies of three different proteins, E1 (OGDH), E2 (DLST), and E3 (DLD), each with distinct catalytic activities (Reed and Hackert 1990; Zhou et al 2001). The reaction starts with the oxidative decarboxylation of alpha ketoglutarate catalyzed by E1alpha and beta (alpha ketoglutarate dehydrogenase). Lipoamide cofactor associated with E1 is reduced at the same time. Next, the succinyl group derived from alpha ketoglutarate is transferred to coenzyme A in two steps catalyzed E2 (dihydrolipolyl transacetylase). Finally, the oxidized form of lipoamide is regenerated and electrons are transferred to NAD+ in two steps catalyzed by E3 (dihydrolipoyl dehydrogenase). The biochemical details of this reaction have been worked out with alpha ketoglutarate dehydrogenase complex and subunits purified from bovine tissue (McCartney et al. 1998). While all of the human proteins are known as predicted protein products of cloned genes, direct experimental evidence for their functions is available only for E3 (DLD) (Brautigam et al. 2005).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P36957-1", "Q02218-1", "P09622-1" ], "evidence": [ { "id": "R-HSA-71401", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-71401" } ] }, { "id": "R-HSA-9838035", "name": "CLPXP binds mitochondrial matrix proteins", "equation": "", "summary": "The CLPXP complex is an ATP-dependent protease located in the mitochondrial matrix that binds, unfolds, and degrades a specific set of protein substrates. The CLPXP complex comprises two heptameric rings of CLPP protease subunits and two hexameric rings of CLPX ATPase subunits (Kang et al. 2002, 2005). Upon binding the CLPXP complex, substrate proteins are unfolded by CLPX in an ATP-dependent reaction and translocated to the CLPP protease (reviewed in Baker and Sauer 2012, Liu et al. 2014). The CLPXP complex interacts with more than 200 mitochondrial proteins (Cole et al. 2015, Ishizawa et al. 2019, Mabanglo et al. 2022) and degrades several mitochondrial matrix proteins (Lee et al. 2021, Key et al. 2021), including ERAL1, a putative 12S rRNA chaperone (inferred from mouse homologs in Szczepanowska et al. 2016, Key et al. 2022) and heme-bound ALAS1 (Kubota et al. 2016, Nomura et al. 2021). CLPXP can also regulate proteins involved in bioenergetics such as components of the electron transport chain suggesting that it can regulate proteins in the inner mitochondrial membrane (Seo et al. 2016, Ishizawa et al. 2019, Mabanglo et al. 2022). CLPXP is also thought to be involved in the mitochondrial unfolded protein response (inferred from C. elegans homologs in Haynes et al. 2007 and mouse homologs in Lian et al. 2023).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O75390-1", "Q96I99-1", "P28331-1", "Q02218-1", "P48735-1", "P07954-1", "O75489-1", "P49753-1", "Q99798-1", "P06576-1", "Q9UKU7-1", "P30837-1", "P05091-1", "P78540-1", "Q16740-1", "P22830-1", "Q9NWU1-1", "P55809-1", "P09622-1", "P42126-1", "Q13011-1", "P10809-1", "P13196-1", "Q02338-1", "P08559-1", "P11177-1", "P24752-1", "P40926-1", "P50213-1", "P23368-1", "Q16836-1", "Q15118-1" ], "evidence": [ { "id": "R-HSA-9838035", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9838035" } ] }, { "id": "R-HSA-9838289", "name": "CLPXP degrades mitochondrial matrix proteins", "equation": "", "summary": "The CLPXP complex comprises two heptameric rings of the barrel-shaped CLPP protease and two hexameric rings of the AAA+ CLPX ATPase (Kang et al. 2002, 2005). Though isolated CLPP subunits have peptidase activity, they only have significant protease activity when complexed with CLPX (Kang et al. 2005). The CLPX subunit unfolds proteins so they can enter the axial pore of the CLPP protease (reviewed in Baker and Sauer 2012, Liu et al. 2014). The CLPXP complex binds and degrades several mitochondrial matrix proteins (Lee et al. 2021, Key et al. 2021), including ALAS1 bound to heme (Kubota et al. 2016, Nomura et al. 2021). CLPXP can also regulate proteins involved in bioenergetics such as components of the electron transport chain suggesting that it can regulate proteins in the inner mitochondrial membrane (Seo et al. 2016, Ishizawa et al. 2019, Mabanglo et al. 2022). CLPXP is thought to be involved in the mitochondrial unfolded protein response (inferred from C. elegans homologs in Haynes et al. 2007 and mouse homologs in Lian et al. 2023). Peptides produced by CLPXP are transported from the mitochondria into the cytosol and activate ATF5 (ATFS-1 in C. elegans). ATF5 subsequently translocates to the nucleus where it enhances the expression of mitochondrial proteases (CLPP and LONP1) and chaperones (HSP60 and GRP75) to restore proteostasis (inferred from C. elegans homologs in Haynes et al. 2010, inferred from mouse homologs in Deepa et al. 2016, Fiorese et al. 2016, inferred from rat homologs in Lian et al. 2023). Recessive mutations in the CLPP subunit of the CLPXP complex cause Perreault Syndrome, which is characterized by congenital sensorineural loss, ataxia, azoospermia (male infertility), ovarian failure, psychomotor retardation, ataxia, autism and epilepsy (Jenkinson et al. 2013, Demain et al. 2017, Faridi et al. 2022).", "cellular_location": "mitochondrial matrix", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O75390-1", "Q96I99-1", "P28331-1", "Q02218-1", "P48735-1", "P07954-1", "O75489-1", "P49753-1", "Q99798-1", "P06576-1", "Q9UKU7-1", "P30837-1", "P05091-1", "P78540-1", "Q16740-1", "P22830-1", "Q9NWU1-1", "P55809-1", "P09622-1", "P42126-1", "Q13011-1", "P10809-1", "P13196-1", "Q02338-1", "P08559-1", "P11177-1", "P24752-1", "P40926-1", "P50213-1", "P23368-1", "Q16836-1", "Q15118-1" ], "evidence": [ { "id": "R-HSA-9838289", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9838289" } ] } ], "reaction_participants": [ { "participant_id": "R-HSA-210342", "participant_name": "p-lipo-PDH [mitochondrial matrix]", "crossref": [ { "id": "CPX-6242", "database": "ComplexPortal", "url": "" }, { "id": "CPX-6233", "database": "ComplexPortal", "url": "" } ] }, { "participant_id": "R-HSA-5693120", "participant_name": "p-BCKDH [mitochondrial matrix]", "crossref": [ { "id": "CPX-2216", "database": "ComplexPortal", "url": "" } ] }, { "participant_id": "R-HSA-70019", "participant_name": "lipo-BCKDH [mitochondrial matrix]", "crossref": [ { "id": "CPX-2216", "database": "ComplexPortal", "url": "" } ] }, { "participant_id": "R-HSA-70070", "participant_name": "lipo-PDH [mitochondrial matrix]", "crossref": [ { "id": "CPX-6233", "database": "ComplexPortal", "url": "" }, { "id": "CPX-6242", "database": "ComplexPortal", "url": "" } ] } ], "reaction_enzymes": [ { "uniprot_ac": "A0A8I6A931", "gene_name": "ENSRNOG00000069392", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "A0A8I6A931", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A8I6A931" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "A0A8I6A931", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A8I6A931" } ] } ] }, { "uniprot_ac": "O08749", "gene_name": "Dld", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "O08749", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O08749" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "O08749", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O08749" } ] } ] }, { "uniprot_ac": "O14874", "gene_name": "BCKDK", "activity": [ { "ec_number": "2.7.11.-", "activity": "", "evidence": [ { "id": "O14874", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14874" } ] }, { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "O14874", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14874" } ] }, { "ec_number": "2.7.11.4", "activity": "ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase].", "evidence": [ { "id": "O14874", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14874" } ] }, { "ec_number": "2.7.11.1", "activity": "", "evidence": [ { "id": "O14874", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O14874" } ] } ] }, { "uniprot_ac": "O75390", "gene_name": "CS", "activity": [ { "ec_number": "2.3.3.1", "activity": "acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+).", "evidence": [ { "id": "O75390", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75390" } ] }, { "ec_number": "2.3.3.1", "activity": "", "evidence": [ { "id": "O75390", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75390" } ] } ] }, { "uniprot_ac": "O75489", "gene_name": "NDUFS3", "activity": [ { "ec_number": "7.1.1.2", "activity": "a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+).", "evidence": [ { "id": "O75489", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75489" } ] }, { "ec_number": "7.1.1.2", "activity": "", "evidence": [ { "id": "O75489", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/O75489" } ] } ] }, { "uniprot_ac": "P05091", "gene_name": "ALDH2", "activity": [ { "ec_number": "1.2.1.3", "activity": "an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH.", "evidence": [ { "id": "P05091", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05091" } ] }, { "ec_number": "1.2.1.3", "activity": "", "evidence": [ { "id": "P05091", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P05091" } ] } ] }, { "uniprot_ac": "P06576", "gene_name": "ATP5F1B", "activity": [ { "ec_number": "7.1.2.2", "activity": "ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate.", "evidence": [ { "id": "P06576", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06576" } ] }, { "ec_number": "7.1.2.2", "activity": "", "evidence": [ { "id": "P06576", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P06576" } ] } ] }, { "uniprot_ac": "P07954", "gene_name": "FH", "activity": [ { "ec_number": "4.2.1.2", "activity": "(S)-malate = fumarate + H2O.", "evidence": [ { "id": "P07954", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07954" } ] }, { "ec_number": "4.2.1.2", "activity": "", "evidence": [ { "id": "P07954", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P07954" } ] } ] }, { "uniprot_ac": "P08559", "gene_name": "PDHA1", "activity": [ { "ec_number": "1.2.4.1", "activity": "H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase].", "evidence": [ { "id": "P08559", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08559" } ] }, { "ec_number": "1.2.4.1", "activity": "", "evidence": [ { "id": "P08559", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08559" } ] } ] }, { "uniprot_ac": "P09622", "gene_name": "DLD", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "P09622", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09622" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "P09622", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09622" } ] } ] }, { "uniprot_ac": "P09624", "gene_name": "LPD1", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "P09624", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09624" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "P09624", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09624" } ] } ] }, { "uniprot_ac": "P10515", "gene_name": "DLAT", "activity": [ { "ec_number": "2.3.1.12", "activity": "acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein].", "evidence": [ { "id": "P10515", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10515" } ] }, { "ec_number": "2.3.1.12", "activity": "", "evidence": [ { "id": "P10515", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10515" } ] }, { "ec_number": "2.3.1.-", "activity": "", "evidence": [ { "id": "P10515", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10515" } ] } ] }, { "uniprot_ac": "P10809", "gene_name": "HSPD1", "activity": [ { "ec_number": "5.6.1.7", "activity": "ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.", "evidence": [ { "id": "P10809", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10809" } ] }, { "ec_number": "5.6.1.7", "activity": "", "evidence": [ { "id": "P10809", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P10809" } ] } ] }, { "uniprot_ac": "P11177", "gene_name": "PDHB", "activity": [ { "ec_number": "1.2.4.1", "activity": "H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase].", "evidence": [ { "id": "P11177", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11177" } ] }, { "ec_number": "1.2.4.1", "activity": "", "evidence": [ { "id": "P11177", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11177" } ] } ] }, { "uniprot_ac": "P11182", "gene_name": "DBT", "activity": [ { "ec_number": "2.3.1.-", "activity": "", "evidence": [ { "id": "P11182", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11182" } ] }, { "ec_number": "2.3.1.168", "activity": "2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[protein].", "evidence": [ { "id": "P11182", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11182" } ] }, { "ec_number": "2.3.1.168", "activity": "", "evidence": [ { "id": "P11182", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P11182" } ] } ] }, { "uniprot_ac": "P12694", "gene_name": "BCKDHA", "activity": [ { "ec_number": "1.2.4.4", "activity": "3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase].", "evidence": [ { "id": "P12694", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12694" } ] }, { "ec_number": "1.2.4.4", "activity": "", "evidence": [ { "id": "P12694", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P12694" } ] } ] }, { "uniprot_ac": "P13196", "gene_name": "ALAS1", "activity": [ { "ec_number": "2.3.1.37", "activity": "glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA.", "evidence": [ { "id": "P13196", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P13196" } ] }, { "ec_number": "2.3.1.37", "activity": "", "evidence": [ { "id": "P13196", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P13196" } ] } ] }, { "uniprot_ac": "P21953", "gene_name": "BCKDHB", "activity": [ { "ec_number": "1.2.4.4", "activity": "3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase].", "evidence": [ { "id": "P21953", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P21953" } ] }, { "ec_number": "1.2.4.4", "activity": "", "evidence": [ { "id": "P21953", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P21953" } ] } ] }, { "uniprot_ac": "P22830", "gene_name": "FECH", "activity": [ { "ec_number": "4.98.1.1", "activity": "2 H(+) + heme b = Fe(2+) + protoporphyrin IX.", "evidence": [ { "id": "P22830", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22830" } ] }, { "ec_number": "4.98.1.1", "activity": "", "evidence": [ { "id": "P22830", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22830" } ] } ] }, { "uniprot_ac": "P23368", "gene_name": "ME2", "activity": [ { "ec_number": "1.1.1.38", "activity": "H(+) + oxaloacetate = CO2 + pyruvate.", "evidence": [ { "id": "P23368", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23368" } ] }, { "ec_number": "1.1.1.38", "activity": "", "evidence": [ { "id": "P23368", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23368" } ] } ] }, { "uniprot_ac": "P24752", "gene_name": "ACAT1", "activity": [ { "ec_number": "2.3.1.9", "activity": "2 acetyl-CoA = acetoacetyl-CoA + CoA.", "evidence": [ { "id": "P24752", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24752" } ] }, { "ec_number": "2.3.1.9", "activity": "", "evidence": [ { "id": "P24752", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P24752" } ] } ] }, { "uniprot_ac": "P28331", "gene_name": "NDUFS1", "activity": [ { "ec_number": "7.1.1.2", "activity": "a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+).", "evidence": [ { "id": "P28331", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28331" } ] }, { "ec_number": "7.1.1.2", "activity": "", "evidence": [ { "id": "P28331", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P28331" } ] } ] }, { "uniprot_ac": "P29803", "gene_name": "PDHA2", "activity": [ { "ec_number": "1.2.4.1", "activity": "H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase].", "evidence": [ { "id": "P29803", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29803" } ] }, { "ec_number": "1.2.4.1", "activity": "", "evidence": [ { "id": "P29803", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P29803" } ] } ] }, { "uniprot_ac": "P30837", "gene_name": "ALDH1B1", "activity": [ { "ec_number": "1.2.1.3", "activity": "an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH.", "evidence": [ { "id": "P30837", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30837" } ] }, { "ec_number": "1.2.1.3", "activity": "", "evidence": [ { "id": "P30837", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P30837" } ] } ] }, { "uniprot_ac": "P36957", "gene_name": "DLST", "activity": [ { "ec_number": "2.3.1.61", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex component E2].", "evidence": [ { "id": "P36957", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P36957" } ] }, { "ec_number": "2.3.1.61", "activity": "", "evidence": [ { "id": "P36957", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P36957" } ] }, { "ec_number": "2.3.1.-", "activity": "", "evidence": [ { "id": "P36957", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P36957" } ] } ] }, { "uniprot_ac": "P40926", "gene_name": "MDH2", "activity": [ { "ec_number": "1.1.1.37", "activity": "(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate.", "evidence": [ { "id": "P40926", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P40926" } ] }, { "ec_number": "1.1.1.37", "activity": "", "evidence": [ { "id": "P40926", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P40926" } ] } ] }, { "uniprot_ac": "P42126", "gene_name": "ECI1", "activity": [ { "ec_number": "5.3.3.8", "activity": "a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA.", "evidence": [ { "id": "P42126", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42126" } ] }, { "ec_number": "5.3.3.8", "activity": "", "evidence": [ { "id": "P42126", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42126" } ] } ] }, { "uniprot_ac": "P48735", "gene_name": "IDH2", "activity": [ { "ec_number": "1.1.1.42", "activity": "D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH.", "evidence": [ { "id": "P48735", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48735" } ] }, { "ec_number": "1.1.1.42", "activity": "", "evidence": [ { "id": "P48735", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48735" } ] } ] }, { "uniprot_ac": "P49753", "gene_name": "ACOT2", "activity": [ { "ec_number": "3.1.2.2", "activity": "H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate.", "evidence": [ { "id": "P49753", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P49753" } ] }, { "ec_number": "3.1.2.2", "activity": "", "evidence": [ { "id": "P49753", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P49753" } ] } ] }, { "uniprot_ac": "P50213", "gene_name": "IDH3A", "activity": [ { "ec_number": "1.1.1.41", "activity": "D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH.", "evidence": [ { "id": "P50213", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P50213" } ] }, { "ec_number": "1.1.1.41", "activity": "", "evidence": [ { "id": "P50213", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P50213" } ] } ] }, { "uniprot_ac": "P55809", "gene_name": "OXCT1", "activity": [ { "ec_number": "2.8.3.5", "activity": "a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate.", "evidence": [ { "id": "P55809", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55809" } ] }, { "ec_number": "2.8.3.5", "activity": "", "evidence": [ { "id": "P55809", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P55809" } ] } ] }, { "uniprot_ac": "P78540", "gene_name": "ARG2", "activity": [ { "ec_number": "3.5.3.1", "activity": "H2O + L-arginine = L-ornithine + urea.", "evidence": [ { "id": "P78540", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P78540" } ] }, { "ec_number": "3.5.3.1", "activity": "", "evidence": [ { "id": "P78540", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P78540" } ] } ] }, { "uniprot_ac": "Q02218", "gene_name": "OGDH", "activity": [ { "ec_number": "1.2.4.2", "activity": "2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue succinyltransferase].", "evidence": [ { "id": "Q02218", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q02218" } ] }, { "ec_number": "1.2.4.2", "activity": "", "evidence": [ { "id": "Q02218", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q02218" } ] } ] }, { "uniprot_ac": "Q02338", "gene_name": "BDH1", "activity": [ { "ec_number": "1.1.1.30", "activity": "(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH.", "evidence": [ { "id": "Q02338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q02338" } ] }, { "ec_number": "1.1.1.30", "activity": "", "evidence": [ { "id": "Q02338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q02338" } ] } ] }, { "uniprot_ac": "Q13011", "gene_name": "ECH1", "activity": [ { "ec_number": "5.3.3.-", "activity": "", "evidence": [ { "id": "Q13011", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q13011" } ] } ] }, { "uniprot_ac": "Q15118", "gene_name": "PDK1", "activity": [ { "ec_number": "2.7.11.-", "activity": "", "evidence": [ { "id": "Q15118", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15118" } ] }, { "ec_number": "2.7.11.2", "activity": "ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit].", "evidence": [ { "id": "Q15118", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15118" } ] }, { "ec_number": "2.7.11.2", "activity": "", "evidence": [ { "id": "Q15118", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15118" } ] } ] }, { "uniprot_ac": "Q15119", "gene_name": "PDK2", "activity": [ { "ec_number": "2.7.11.-", "activity": "", "evidence": [ { "id": "Q15119", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15119" } ] }, { "ec_number": "2.7.11.2", "activity": "ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit].", "evidence": [ { "id": "Q15119", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15119" } ] }, { "ec_number": "2.7.11.2", "activity": "", "evidence": [ { "id": "Q15119", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15119" } ] } ] }, { "uniprot_ac": "Q15120", "gene_name": "PDK3", "activity": [ { "ec_number": "2.7.11.2", "activity": "ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit].", "evidence": [ { "id": "Q15120", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15120" } ] }, { "ec_number": "2.7.11.2", "activity": "", "evidence": [ { "id": "Q15120", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q15120" } ] } ] }, { "uniprot_ac": "Q16654", "gene_name": "PDK4", "activity": [ { "ec_number": "2.7.11.2", "activity": "ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit].", "evidence": [ { "id": "Q16654", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16654" } ] }, { "ec_number": "2.7.11.2", "activity": "", "evidence": [ { "id": "Q16654", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16654" } ] } ] }, { "uniprot_ac": "Q16740", "gene_name": "CLPP", "activity": [ { "ec_number": "3.4.21.92", "activity": "Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).", "evidence": [ { "id": "Q16740", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16740" } ] }, { "ec_number": "3.4.21.92", "activity": "", "evidence": [ { "id": "Q16740", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16740" } ] } ] }, { "uniprot_ac": "Q16836", "gene_name": "HADH", "activity": [ { "ec_number": "1.1.1.35", "activity": "a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH.", "evidence": [ { "id": "Q16836", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16836" } ] }, { "ec_number": "1.1.1.35", "activity": "", "evidence": [ { "id": "Q16836", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q16836" } ] } ] }, { "uniprot_ac": "Q54EW8", "gene_name": "lpd", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "Q54EW8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q54EW8" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "Q54EW8", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q54EW8" } ] } ] }, { "uniprot_ac": "Q6P6R2", "gene_name": "Dld", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "Q6P6R2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6P6R2" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "Q6P6R2", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q6P6R2" } ] } ] }, { "uniprot_ac": "Q8N3J5", "gene_name": "PPM1K", "activity": [ { "ec_number": "3.1.3.16", "activity": "H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate.", "evidence": [ { "id": "Q8N3J5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8N3J5" } ] }, { "ec_number": "3.1.3.52", "activity": "H2O + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] + phosphate.", "evidence": [ { "id": "Q8N3J5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8N3J5" } ] }, { "ec_number": "3.1.3.16", "activity": "", "evidence": [ { "id": "Q8N3J5", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q8N3J5" } ] } ] }, { "uniprot_ac": "Q96HY7", "gene_name": "DHTKD1", "activity": [ { "ec_number": "1.2.4.-", "activity": "", "evidence": [ { "id": "Q96HY7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q96HY7" } ] } ] }, { "uniprot_ac": "Q96I99", "gene_name": "SUCLG2", "activity": [ { "ec_number": "6.2.1.4", "activity": "CoA + GTP + succinate = GDP + phosphate + succinyl-CoA.", "evidence": [ { "id": "Q96I99", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q96I99" } ] }, { "ec_number": "6.2.1.4", "activity": "", "evidence": [ { "id": "Q96I99", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q96I99" } ] } ] }, { "uniprot_ac": "Q99798", "gene_name": "ACO2", "activity": [ { "ec_number": "4.2.1.3", "activity": "citrate = D-threo-isocitrate.", "evidence": [ { "id": "Q99798", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q99798" } ] }, { "ec_number": "4.2.1.3", "activity": "", "evidence": [ { "id": "Q99798", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q99798" } ] } ] }, { "uniprot_ac": "Q9NWU1", "gene_name": "OXSM", "activity": [ { "ec_number": "2.3.1.41", "activity": "a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] + CO2 + holo-[ACP].", "evidence": [ { "id": "Q9NWU1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NWU1" } ] }, { "ec_number": "2.3.1.41", "activity": "", "evidence": [ { "id": "Q9NWU1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9NWU1" } ] } ] }, { "uniprot_ac": "Q9P0J1", "gene_name": "PDP1", "activity": [ { "ec_number": "3.1.3.43", "activity": "H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate.", "evidence": [ { "id": "Q9P0J1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9P0J1" } ] }, { "ec_number": "3.1.3.43", "activity": "", "evidence": [ { "id": "Q9P0J1", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9P0J1" } ] } ] }, { "uniprot_ac": "Q9P2J9", "gene_name": "PDP2", "activity": [ { "ec_number": "3.1.3.43", "activity": "H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate.", "evidence": [ { "id": "Q9P2J9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9P2J9" } ] }, { "ec_number": "3.1.3.43", "activity": "", "evidence": [ { "id": "Q9P2J9", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9P2J9" } ] } ] }, { "uniprot_ac": "Q9UKU7", "gene_name": "ACAD8", "activity": [ { "ec_number": "1.3.8.5", "activity": "2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein].", "evidence": [ { "id": "Q9UKU7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UKU7" } ] }, { "ec_number": "1.3.8.5", "activity": "", "evidence": [ { "id": "Q9UKU7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9UKU7" } ] } ] }, { "uniprot_ac": "Q9VVL7", "gene_name": "E3", "activity": [ { "ec_number": "1.8.1.4", "activity": "N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH.", "evidence": [ { "id": "Q9VVL7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VVL7" } ] }, { "ec_number": "1.8.1.4", "activity": "", "evidence": [ { "id": "Q9VVL7", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9VVL7" } ] } ] }, { "uniprot_ac": "Q9Y234", "gene_name": "LIPT1", "activity": [ { "ec_number": "2.3.1.-", "activity": "", "evidence": [ { "id": "Q9Y234", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y234" } ] }, { "ec_number": "2.3.1.200", "activity": "L-lysyl-[lipoyl-carrier protein] + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] = L-lysyl-[glycine-cleavage complex H protein] + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein].", "evidence": [ { "id": "Q9Y234", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y234" } ] }, { "ec_number": "2.3.1.200", "activity": "", "evidence": [ { "id": "Q9Y234", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/Q9Y234" } ] } ] } ], "biomarkers": [], "synthesized_glycans": [], "cluster_types": [ { "name": "isoformset.uniprotkb", "label": "Isoforms" }, { "name": "homologset.mgi", "label": "MGI Homologs" }, { "name": "homologset.oma", "label": "OMA Homologs" } ], "sequence_features": { "n_linked_sites": [], "o_linked_sites": [ 183 ], "snv_sites": [ 183, 277, 500 ], "glycation_sites": [], "phosphorylation_sites": [ 276, 285, 297, 341, 502 ], "sequon_annotation_sites": [ { "start_pos": 73, "end_pos": 75 }, { "start_pos": 93, "end_pos": 95 } ] }, "section_stats": [ { "table_id": "glycosylation", "table_stats": [ { "field": "total", "count": 1 }, { "field": "total_sites", "count": 1 }, { "field": "n_linked_glycans", "count": 0 }, { "field": "n_linked_glycan_sites", "count": 0 }, { "field": "o_linked_glycans", "count": 1 }, { "field": "o_linked_glycan_sites", "count": 1 } ], "sort_fields": [ "glytoucan_ac", "type", "subtype", "site_category", "site_seq", "relation", "comment", "start_pos", "start_aa", "end_pos", "end_aa", "residue", "site_lbl" ] }, { "table_id": "glycosylation_reported", "table_stats": [ { "field": "total", 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