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UniProt functional annotation for P09624 | ||
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| UniProt code: P09624. |
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| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
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| Function: | |
Lipoamide dehydrogenase is a component of the alpha-ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl- CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine. |
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| Catalytic activity: | |
Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)- lipoyl-L-lysyl-[protein] + H(+) + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; |
| Cofactor: | |
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; |
| Subunit: | |
LPD1 is a homodimer. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. LPD1 is a component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H. {ECO:0000269|PubMed:7498764, ECO:0000269|PubMed:9538259, ECO:0000269|Ref.9}. |
| Subcellular location: | |
Mitochondrion matrix. |
| Miscellaneous: | |
The active site is a redox-active disulfide bond. |
| Miscellaneous: | |
Present with 24600 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.