TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*3.B.1.1.1









Na+-transporting oxalo-acetate decarboxylase. Subunit stoichiometries have been described (Balsera et al., 2011). The crystal structure of the carboxyltransferase at 1.7 A resolution shows a dimer of alpha(8)beta(8) barrels with an active site metal ion, identified spectroscopically as Zn2+ (Granjon et al. 2010).

Bacteria
Proteobacteria
Oxaloacetate decarboxylase of Salmonella typhimurium
*3.B.1.1.2









Na+-transporting methylmalonyl-CoA decarboxylase
Bacteria
Firmicutes
Methylmalonyl-CoA decarboxylase of Veillonella parvula
*3.B.1.1.3









Na+-transporting glutaconyl-CoA decarboxylase
Bacteria
Firmicutes
Glutaconyl-CoA decarboxylase of Acidaminococcus fermentans
*3.B.1.1.4









Na+-transporting malonate decarboxylase
Bacteria
Proteobacteria
Malonate decarboxylase of Malonomonas rubra
*3.B.1.1.5









Putative Na+-transporting methylmalonyl-CoA decarboxylase (Cohen et al., 2003)
Archaea
Euryarchaeota
Putative methylmalonyl-CoA decarboxylase of Pyrococcus abyssi (α,β,γ,δ subunits)
α (MmdA)
β (MmdB)
γ (MmdC)
δ (MmdD)
*3.B.1.1.6









Na+-exporting oxaloacetate decarboxylase with three subunits, OadA (α), OadB (β) and OadG (γ) of 599 aas and 0 TMSs, 433 aas and 11 TMSs, and 90 aas and 1 TMS, respectively.  These three subunits are 72%, 70% and 40% identical to 3.B.1.1.1.  The stoichiometry of the three subunits is 4:2:2, and large amounts of the protein can be generated for crystalographic studies (Inoue and Li 2015).

Bacteria
Proteobacteria
OadABG of Vibrio cholerae