Protein Domain : IPR003016

Type:  Binding_site Name:  2-oxo acid dehydrogenase, lipoyl-binding site
Description:  The 2-oxo acid dehydrogenase multienzyme complexes [] from bacterial andeukaryotic sources catalyze the oxidative decarboxylation of 2-oxo acids to the corresponding acyl-CoA. These include: Pyruvate dehydrogenase complex (PDC). 2-oxoglutarate dehydrogenase complex (OGDC). Branched-chain 2-oxo acid dehydrogenase complex (BCOADC). These three complexes share a common architecture: they are composed of multiple copies of three component enzymes - E1, E2 and E3. E1 is a thiaminepyrophosphate-dependent 2-oxo acid dehydrogenase, E2 a dihydrolipamide acyltransferase, and E3 an FAD-containing dihydrolipamide dehydrogenase. E2 acyltransferases have an essential cofactor, lipoic acid, which is covalently bound via a amide linkage to a lysine group. The E2 components ofOGCD and BCOACD bind a single lipoyl group, while those of PDC bind either one (in yeast and in Bacillus), two (in mammals), or three (in Azotobacter and inEscherichia coli) lipoyl groups []. In addition to the E2 components of the three enzymatic complexes described above, a lipoic acid cofactor is also found in the following proteins: H-protein of the glycine cleavage system (GCS) []. GCS is a multienzymecomplex of four protein components, which catalyzes the degradation of glycine. H protein shuttles the methylamine group of glycine from the Pprotein to the T protein. H-protein from either prokaryotes or eukaryotes binds a single lipoic group. Mammalian and yeast pyruvate dehydrogenase complexes differ from that of other sources, in that they contain, in small amounts, a protein of unknownfunction - designated protein X or component X. Its sequence is closelyrelated to that of E2 subunits and seems to bind a lipoic group []. Fast migrating protein (FMP) (gene acoC) from Ralstonia eutropha(Alcaligenes eutrophus) [].This protein is most probably a dihydrolipamide acyltransferase involved in acetoin metabolism. This signature contains the lipoyl-binding lysine residue. The domain surronding this site is evolutionary related to that around the biotin-binding lysine residue of biotin requiring enzymes. Short Name:  2-oxoA_DH_lipoyl-BS
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0 Child Features

0 Contains

1 Cross References

Identifier
PS00189

10 Found Ins

DB identifier Type Name
IPR017453 Family Glycine cleavage system H-protein, subgroup
IPR000089 Domain Biotin/lipoyl attachment
IPR011053 Domain Single hybrid motif
IPR006255 Family Dihydrolipoamide succinyltransferase
IPR002930 Family Glycine cleavage system H-protein
IPR006257 Family Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
IPR006256 Family Dihydrolipoamide acetyltransferase pyruvate dehydrogenase complex
IPR015761 Family Lipoamide Acyltransferase
IPR014276 Family 2-oxoglutarate dehydrogenase, E2 component
IPR017514 Family Glycine cleavage system protein H-related, Chlamydia

0 GO Annotation

0 Ontology Annotations

0 Parent Features

0 Proteins

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1825611
            2649080
            2061286
            3522581
            2682658