![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily) 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465 |
![]() | Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (9 families) ![]() there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules |
![]() | Family c.36.1.5: Pyruvate oxidase and decarboxylase Pyr module [88724] (8 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpha/beta domain of Rossmann-like topology automatically mapped to Pfam PF02776 |
![]() | Protein Pyruvate oxidase [88729] (2 species) |
![]() | Domain d1powa2: 1pow A:9-182 [31797] Other proteins in same PDB: d1powa1, d1powa3, d1powb1, d1powb3 complexed with fad, mg, tpp; mutant |
PDB Entry: 1pow (more details), 2.5 Å
SCOPe Domain Sequences for d1powa2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1powa2 c.36.1.5 (A:9-182) Pyruvate oxidase {Lactobacillus plantarum [TaxId: 1590]} tnilagaavikvleawgvdhlygipggsinsimdalsaerdrihyiqvrheevgamaaaa dakltgkigvcfgsagpggthlmnglydaredhvpvlaligqfgttgmnmdtfqemnenp iyadvadynvtavnaatlphvideairrayahqgvavvqipvdlpwqqipaedw
Timeline for d1powa2: