| Description | This entry represents the PP-binding module found in the C-terminal of pyruvate oxidase (POXB) and similar proteins from bacteria and archaea [ , ].The thiamine pyrophosphate (TPP) family has a thiamin diphosphate-binding fold consisting of two different functional modules, the pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules.TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain ( ), binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation [ , , ]. This entry represents the PP domain. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure []. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits [, ]. POXB decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate []. This entry also includes a closely homologous member, pyruvate dehydrogenase [ubiquinone]PoxB from Escherichia coli, a peripheral membrane protein that catalyses the oxidative decarboxylation of the central metabolite pyruvate to CO(2) and acetate. It has pyruvate oxidase as an alternate name [ , , , , ]. | Name | Pyruvate oxidase POXB-like, PP-binding domain |
| Short Name | TPP_POXB-like | Type | Domain |
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