![]() | 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.36.1.9: Pyruvate oxidase and decarboxylase PP module [88749] (8 proteins) the N-terminal, Pyr module is separated from the C-terminal, PP module by an alpa/beta domain of Rossmann-like topology |
![]() | Protein Pyruvate decarboxylase [88750] (3 species) |
![]() | Species Brewer's yeast (Saccharomyces uvarum) [TaxId:230603] [88751] (1 PDB entry) |
![]() | Domain d1pyda3: 1pyd A:361-556 [31774] Other proteins in same PDB: d1pyda1, d1pyda2, d1pydb1, d1pydb2 complexed with mg, tdp |
PDB Entry: 1pyd (more details), 2.4 Å
SCOPe Domain Sequences for d1pyda3:
Sequence; same for both SEQRES and ATOM records: (download)
>d1pyda3 c.36.1.9 (A:361-556) Pyruvate decarboxylase {Brewer's yeast (Saccharomyces uvarum) [TaxId: 230603]} astplkqewmwnqlgnflqegdvviaetgtsafginqttfpnntygisqvlwgsigfttg atlgaafaaeeidpkkrvilfigdgslqltvqeistmirwglkpylfvlnndgytiekli hgpkaqyneiqgwdhlsllptfgakdyethrvattgewdkltqdksfndnskirmieiml pvfdapqnlvkqaklt
Timeline for d1pyda3: