4.1.1.112	dimer	2 * 49000, SDS-PAGE	4283	
4.1.1.112	dimer	dimer of dimers, X-ray crystallography	678331	
4.1.1.112	dimer	in the absence of beta- or alpha-subunits, the gamma-subunit forms a homodimer through a dimerization interface in the carboxyltransferase domain	726821	
4.1.1.112	heterotrimer	-	716673	
4.1.1.112	heterotrimer	OAD contains three different subunits: Oad-alpha, a biotinylated extrinsic protein that catalyzes the alpha-ketodecarboxylation of oxaloacetate; Oad-gamma, a structural bitopic membrane protein whose cytosolic tail (named as Oad-gamma’) binds tightly to Oad-alpha, and Oad-beta, a multispan transmembrane-alpha-helical protein that constitutes the Na+-channel	715662	
4.1.1.112	homodimer	2 * 29000, gel filtration	704327	
4.1.1.112	homodimer	2 * 29000, SDS-PAGE	748206	
4.1.1.112	homodimer	2 * 51000, gel filtration	681424	
4.1.1.112	monomer	1 * 63000, SDS-PAGE	654328	
4.1.1.112	additional information	the alpha-subunit binds the gamma-subunit with a distinct association domain which is flanked on both sides with proline- and alanine-rich linker peptides	664904	
4.1.1.112	tetramer	4 * 31700, SDS-PAGE	4276	
4.1.1.112	tetramer	oxaloacetate decarboxylase OAD-2	-, 663796	
4.1.1.112	tetramer	the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. The small 9 kDa gamma-subunit is an integral membrane protein with a single membrane-spanning helix at the N-terminus, followed by a hydrophilic C-terminal domain which interacts with the alpha-subunit. The gamma-subunit is essential for the overall stability of the complex, and likely serves as an anchor to hold the alpha- and beta-subunits in place	726821	
4.1.1.112	tetramer	the enzyme consists of alpha-, beta-, and gamma-subunits as well as a biotin carboxyl carrier protein domain. The about 65 kDa hydrophilic alpha-subunit consists of an N-terminal carboxyltransferase domain connected to a C-terminal biotin carboxyl carrier protein domain. The about 45 kDa beta-subunit is an integral membrane protein with nine transmembrane segments, which serves to couple the decarboxylation of carboxybiotin to the translocation of Na+ from the cytoplasm to the periplasm. the site of interaction with the gamma-subunit in Vibrio cholerae OADC is located in an intervening region between the carboxyltransferase and biotin carboxyl carrier protein domains of the alpha-subunit, termed the association domain. Tetramerization of alpha-OADC is mediated by an interaction between the association domain of the alpha-subunit and the cytosolic portion of the gamma-subunit in a manner. A biotin binding pocket, termed the exo-binding site, is located at the interface between the association domain and the carboxyltransferase domain. The interaction is facilitated by the tetramerization of alpha-OADC through interactions between the association domain and the the cytosolic portion of the gamma-subunit, which maintain two of the four alpha-OADC molecules in close proximity to the membrane-bound beta-subunit	726821	
4.1.1.112	tetramer	the enzyme is constituted of four subunits: catalytic subunit OadA (termed Ef-A), membrane pump Ef-B, biotin acceptor protein Ef-D, and subunit Ef-H. Subunits Ef-A, Ef-D, and Ef-H form a cytoplasmic soluble complex, Ef-AHD, which is also associated with the membrane. The Ef-H subunit is involved in the cytoplasmic Ef-AHD complex formation. Analysis of subunit interactions and complex formation, overview	-, 726737	
4.1.1.112	trimer	alpha, beta, gamma	650185, 651122, 653877